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Conserved domains on  [gi|578803747|ref|XP_006712362|]
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myosin-IIIb isoform X2 [Homo sapiens]

Protein Classification

myosin-IIIb( domain architecture ID 10159714)

myosin-IIIb is an actin-based motor with serine/threonine-protein kinase activity, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
366-1055 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 1269.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADeTGRVMHDITSKESYRRQFEAIQHCFRIIGFTD 605
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQN-DGLTVQDIVNNSGNREKFEEIEQCFKVIGFTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAISSQHQTDKSE-VPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDR 684
Cdd:cd01379   240 EEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSrISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  685 AADVRDAMSKALYGRLFSWIVNRINTLLQPDENICsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVF 764
Cdd:cd01379   320 ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAS--DEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  765 ALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPKGVELCFGIQ 844
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  845 HYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLqqlfsipltktgnlaqtraritvassslpphfsagkakvdtle 924
Cdd:cd01379   478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV------------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  925 virhpeettnmkRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSH 1004
Cdd:cd01379   515 ------------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747 1005 RILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd01379   583 RILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKVFLK 633
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
13-303 0e+00

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 670.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   13 LYGLFHYNPMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPN 92
Cdd:cd06639     1 LYGLFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   93 VVKFYGMFYKADHCVGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 172
Cdd:cd06639    81 VVKFYGMFYKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  173 LTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVK 252
Cdd:cd06639   161 LTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  253 TLFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06639   241 ALFKIPRNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
 
Name Accession Description Interval E-value
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
366-1055 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 1269.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADeTGRVMHDITSKESYRRQFEAIQHCFRIIGFTD 605
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQN-DGLTVQDIVNNSGNREKFEEIEQCFKVIGFTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAISSQHQTDKSE-VPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDR 684
Cdd:cd01379   240 EEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSrISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  685 AADVRDAMSKALYGRLFSWIVNRINTLLQPDENICsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVF 764
Cdd:cd01379   320 ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAS--DEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  765 ALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPKGVELCFGIQ 844
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  845 HYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLqqlfsipltktgnlaqtraritvassslpphfsagkakvdtle 924
Cdd:cd01379   478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV------------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  925 virhpeettnmkRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSH 1004
Cdd:cd01379   515 ------------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747 1005 RILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd01379   583 RILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKVFLK 633
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
355-1062 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 794.06  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    355 DDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVT 434
Cdd:smart00242    9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNMLN 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    435 LSKDQCIVISGESGSGKTESAHLIVQHLTFLGKAN--NQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT 512
Cdd:smart00242   89 DKENQSIIISGESGAGKTENTKKIMQYLASVSGSNteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDAK 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    513 GVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrQFE 592
Cdd:smart00242  169 GKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELK-KELGLKSPEDYRYLNQGGCLTVDGIDDAE----EFK 243
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    593 AIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTdkSEVPNAEALQNAASVLCISPEELQEALTSHCVVTR 672
Cdd:smart00242  244 ETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAA--STVKDKEELSNAAELLGVDPEELEKALTKRKIKTG 321
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    673 GETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIAN 752
Cdd:smart00242  322 GEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF-----IGVLDIYGFEIFEVNSFEQLCINYAN 396
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    753 EQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDK----FEDNLRc 828
Cdd:smart00242  397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKlnqhHKKHPH- 475
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    829 kYFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraritvasss 908
Cdd:smart00242  476 -FSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP---------------------- 532
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    909 lpphfsagkakvdtleviRHPEETTNMKR-QTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLR 987
Cdd:smart00242  533 ------------------SGVSNAGSKKRfQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLR 594
                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747    988 STGILETVSIRRQGYSHRILFEEFVKRYYYLAF-TAHQTPLASKESCVAILEKSRLDH--WVLGKTKVFLKYYHVEQL 1062
Cdd:smart00242  595 YLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPdTWPPWGGDAKKACEALLQSLGLDEdeYQLGKTKVFLRPGQLAEL 672
Myosin_head pfam00063
Myosin head (motor domain);
355-1055 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 682.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   355 DDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVT 434
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   435 LSKDQCIVISGESGSGKTESAHLIVQHLTFLGKANNQ----TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFT 510
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   511 PTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrQ 590
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLK-KELRLTNPKDYHYLSQSGCYTIDGIDDSE----E 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   591 FEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQtdkSEVPNAEALQNAASVLCISPEELQEALTSHCVV 670
Cdd:pfam00063  237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   671 TRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQpdeniCSAGGGMNV-GILDIFGFENFQRNSFEQLCIN 749
Cdd:pfam00063  314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLD-----VKTIEKASFiGVLDIYGFEIFEKNSFEQLCIN 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   750 IANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL-RC 828
Cdd:pfam00063  389 YVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFsKH 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   829 KYFWRPK-GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARITvass 907
Cdd:pfam00063  469 PHFQKPRlQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST---- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   908 slpphFSAGKAKvdtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLR 987
Cdd:pfam00063  545 -----PKRTKKK----------------RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLR 603
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747   988 STGILETVSIRRQGYSHRILFEEFVKRYYYLA-FTAHQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:pfam00063  604 CNGVLEGIRIRRAGFPNRITFQEFVQRYRILApKTWPKWKGDAKKGCEAILQSLNLDKeeYQFGKTKIFFR 674
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
13-303 0e+00

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 670.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   13 LYGLFHYNPMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPN 92
Cdd:cd06639     1 LYGLFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   93 VVKFYGMFYKADHCVGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 172
Cdd:cd06639    81 VVKFYGMFYKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  173 LTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVK 252
Cdd:cd06639   161 LTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  253 TLFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06639   241 ALFKIPRNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
COG5022 COG5022
Myosin heavy chain [General function prediction only];
324-1134 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 636.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  324 KHQNPVAKTRHERMHTRRPYHVEDAEKYCLE---DDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSI 400
Cdd:COG5022    35 KVTEEGKKEDGESVSVKKKVLGNDRIKLPKFdgvDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  401 YSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGESGSGKTESAHLIVQHLTFLGKANN---QTLREKI 477
Cdd:COG5022   115 YTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTveiSSIEKQI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  478 LQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQ-KKL 556
Cdd:COG5022   195 LATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEElKKL 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  557 SDFRLPEEKppRYIADETGRVMHDITSKESYRRQFEAiqhcFRIIGFTDKEVHSVYRILAGILNIGNIEFAAissqHQTD 636
Cdd:COG5022   275 LLLQNPKDY--IYLSQGGCDKIDGIDDAKEFKITLDA----LKTIGIDEEEQDQIFKILAAILHIGNIEFKE----DRNG 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  637 KSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPde 716
Cdd:COG5022   345 AAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-- 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  717 nicSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQK 796
Cdd:COG5022   423 ---SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKK 499
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  797 -PLGLLALLDEESRFPQATDQTLVDKFEDNLRCK---YFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVV 872
Cdd:COG5022   500 nPLGILSLLDEECVMPHATDESFTSKLAQRLNKNsnpKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLEL 579
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  873 LRTSENKLLQQLFSIpltktgnlaqtraritvassslpphfsagkakvdtlevirhpEETTNMKRQ--TVASYFRYSLMD 950
Cdd:COG5022   580 LKASTNEFVSTLFDD------------------------------------------EENIESKGRfpTLGSRFKESLNS 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  951 LLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLA-----FTAHQT 1025
Cdd:COG5022   618 LMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTW 697
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747 1026 PLASKESCVAILEKSRLDHWV--LGKTKVFLK----YYHVEQLNLLLREVIGRvvvLQAYTKGWLGARRYKRVReKREKG 1099
Cdd:COG5022   698 KEDTKNAVKSILEELVIDSSKyqIGNTKVFFKagvlAALEDMRDAKLDNIATR---IQRAIRGRYLRRRYLQAL-KRIKK 773
                         810       820       830
                  ....*....|....*....|....*....|....*
gi 578803747 1100 AIAIQSAWRGYDARRKFKKISNRRNESAAHNQAGD 1134
Cdd:COG5022   774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGS 808
PTZ00014 PTZ00014
myosin-A; Provisional
361-1108 1.35e-136

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 439.08  E-value: 1.35e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  361 EVLDedtiihQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASN-PPHIFASADAAYQCMVTLSKDQ 439
Cdd:PTZ00014  111 CVLD------FLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQ 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  440 CIVISGESGSGKTESAHLIVQH-LTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGA 518
Cdd:PTZ00014  185 TIIVSGESGAGKTEATKQIMRYfASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  519 RISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrqFEAIQHCF 598
Cdd:PTZ00014  265 SIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMK-EKYKLKSLEEYKYINPKCLDVPGIDDVKD-----FEEVMESF 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  599 RIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEV--PNAEALQNAASVLCISPEELQEALTSHCVVTRGETI 676
Cdd:PTZ00014  339 DSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIsdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKI 418
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  677 IRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDenicsagGGMNV--GILDIFGFENFQRNSFEQLCINIANEQ 754
Cdd:PTZ00014  419 EGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP-------GGFKVfiGMLDIFGFEVFKNNSLEQLFINITNEM 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  755 IQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRP 834
Cdd:PTZ00014  492 LQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKP 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 --KGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAqtraritvassslpph 912
Cdd:PTZ00014  572 akVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA---------------- 635
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 fsagkakvdtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGIL 992
Cdd:PTZ00014  636 -----------------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSIL 692
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  993 ETVSIRRQGYSHRILFEEFVKRYYYLAF-TAHQTPLASKESCVAILEKSRL--DHWVLGKTKVFLKYYHVEQLNLLLREV 1069
Cdd:PTZ00014  693 EALQLRQLGFSYRRTFAEFLSQFKYLDLaVSNDSSLDPKEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELTQIQREK 772
                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 578803747 1070 IGRVVVLQAYTKGWLGARRYKRVREKREKGAIAIQSAWR 1108
Cdd:PTZ00014  773 LAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
36-302 2.85e-84

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 275.56  E-value: 2.85e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747     36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKkkKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDK-----LYL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    114 VLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:smart00220   75 VMEYCEGGDLFDL----LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    194 RlRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPE-KWC 272
Cdd:smart00220  151 E-KLTTFVGTPEYMAPEVLLGKG-----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDIS 224
                           250       260       270
                    ....*....|....*....|....*....|
gi 578803747    273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:smart00220  225 PEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
36-298 3.25e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 197.54  E-value: 3.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYkadhcVGGQL 111
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARErfrrEARALARL-NHPNIVRVYDVGE-----EDGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:COG0515    83 YLVMEYVEGESLADL----LRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRL-RRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEK 270
Cdd:COG0515   159 GATLtQTGTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRP 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  271 WC-EEFNHFISQCLIKDFERRP-SVTHLLD 298
Cdd:COG0515   234 DLpPALDAIVLRALAKDPEERYqSAAELAA 263
Pkinase pfam00069
Protein kinase domain;
36-302 4.91e-47

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 167.81  E-value: 4.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA---EYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNilrEIKILKKL-NHPNIVRLYDAFEDKDN-----LY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   113 LVLELCNGGSVTElvkgLLRCGQRLDEAMISYILYGALLGLqhlhnnriihrdvkgnnillttEGGVKLVDFgvsaqlts 192
Cdd:pfam00069   75 LVLEYVEGGSLFD----LLSEKGAFSEREAKFIMKQILEGL----------------------ESGSSLTTF-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   193 trlrrntsVGTPFWMAPEVIACeQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWC 272
Cdd:pfam00069  121 --------VGTPWYMAPEVLGG-NPYGPK----VDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLS 187
                          250       260       270
                   ....*....|....*....|....*....|
gi 578803747   273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:pfam00069  188 EEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
37-320 8.86e-38

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 145.74  E-value: 8.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL-----DPVSdmdEEIEAEYNILQFLpNHPNVVKFYGMFykaDHcvGGQL 111
Cdd:PLN00034   77 ERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVR---RQICREIEILRDV-NHPNVVKCHDMF---DH--NGEI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTelvkgllrcGQRL-DEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:PLN00034  148 QVLLEFMDGGSLE---------GTHIaDEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSVGTPFWMAPEVIACEQQyDSSYDARC-DVWSLGITAIELGDGDPPLfdmhPV-----------KTLFKIP 258
Cdd:PLN00034  219 AQTMDPCNSSVGTIAYMSPERINTDLN-HGAYDGYAgDIWSLGVSILEFYLGRFPF----GVgrqgdwaslmcAICMSQP 293
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  259 RNPPPTLlhpekwCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFLQKQLAKVL 320
Cdd:PLN00034  294 PEAPATA------SREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQLL 349
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
37-247 1.02e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 94.86  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvsDM--DEEIeaeynILQF---------LpNHPNVVKFYgmfykaDh 105
Cdd:NF033483   10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRP--DLarDPEF-----VARFrreaqsaasL-SHPNIVSVY------D- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 cVG---GQLWLVLELCNGgsvtELVKGLLRCGQRL--DEAMisYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK 180
Cdd:NF033483   75 -VGedgGIPYIVMEYVDG----RTLKDYIREHGPLspEEAV--EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  181 LVDFGVSAQLTSTRLRRNTSV-GTPFWMAPeviacEQQYDSSYDARCDVWSLGITAIELGDGDPPlFD 247
Cdd:NF033483  148 VTDFGIARALSSTTMTQTNSVlGTVHYLSP-----EQARGGTVDARSDIYSLGIVLYEMLTGRPP-FD 209
 
Name Accession Description Interval E-value
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
366-1055 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 1269.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADeTGRVMHDITSKESYRRQFEAIQHCFRIIGFTD 605
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQN-DGLTVQDIVNNSGNREKFEEIEQCFKVIGFTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAISSQHQTDKSE-VPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDR 684
Cdd:cd01379   240 EEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSrISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  685 AADVRDAMSKALYGRLFSWIVNRINTLLQPDENICsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVF 764
Cdd:cd01379   320 ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAS--DEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  765 ALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPKGVELCFGIQ 844
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  845 HYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLqqlfsipltktgnlaqtraritvassslpphfsagkakvdtle 924
Cdd:cd01379   478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV------------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  925 virhpeettnmkRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSH 1004
Cdd:cd01379   515 ------------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747 1005 RILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd01379   583 RILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKVFLK 633
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
366-1055 0e+00

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 816.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKR-ASNPPHIFASADAAYQCMVTLSKDQCIVIS 444
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  445 GESGSGKTESAHLIVQHLTFLGKA-------NNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMG 517
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAALSGSgssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  518 ARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKESYRRQFEAIQHC 597
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAR-EELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  598 FRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHqTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETII 677
Cdd:cd00124   240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDE-DSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  678 RANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDEnicSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQY 757
Cdd:cd00124   319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTD---AAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  758 YFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKYFWRPK 835
Cdd:cd00124   396 FFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHgsHPRFFSKKR 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  836 GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSenkllqqlfsipltktgnlaqtraritvassslpphfsa 915
Cdd:cd00124   476 KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG--------------------------------------- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  916 gkakvdtlevirhpeettnmkrqtvaSYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETV 995
Cdd:cd00124   517 --------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAV 570
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  996 SIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKE---SCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd00124   571 RIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKaavLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
355-1062 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 794.06  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    355 DDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVT 434
Cdd:smart00242    9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNMLN 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    435 LSKDQCIVISGESGSGKTESAHLIVQHLTFLGKAN--NQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT 512
Cdd:smart00242   89 DKENQSIIISGESGAGKTENTKKIMQYLASVSGSNteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDAK 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    513 GVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrQFE 592
Cdd:smart00242  169 GKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELK-KELGLKSPEDYRYLNQGGCLTVDGIDDAE----EFK 243
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    593 AIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTdkSEVPNAEALQNAASVLCISPEELQEALTSHCVVTR 672
Cdd:smart00242  244 ETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAA--STVKDKEELSNAAELLGVDPEELEKALTKRKIKTG 321
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    673 GETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIAN 752
Cdd:smart00242  322 GEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF-----IGVLDIYGFEIFEVNSFEQLCINYAN 396
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    753 EQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDK----FEDNLRc 828
Cdd:smart00242  397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKlnqhHKKHPH- 475
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    829 kYFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraritvasss 908
Cdd:smart00242  476 -FSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP---------------------- 532
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    909 lpphfsagkakvdtleviRHPEETTNMKR-QTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLR 987
Cdd:smart00242  533 ------------------SGVSNAGSKKRfQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLR 594
                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747    988 STGILETVSIRRQGYSHRILFEEFVKRYYYLAF-TAHQTPLASKESCVAILEKSRLDH--WVLGKTKVFLKYYHVEQL 1062
Cdd:smart00242  595 YLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPdTWPPWGGDAKKACEALLQSLGLDEdeYQLGKTKVFLRPGQLAEL 672
Myosin_head pfam00063
Myosin head (motor domain);
355-1055 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 682.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   355 DDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVT 434
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   435 LSKDQCIVISGESGSGKTESAHLIVQHLTFLGKANNQ----TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFT 510
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   511 PTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrQ 590
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLK-KELRLTNPKDYHYLSQSGCYTIDGIDDSE----E 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   591 FEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQtdkSEVPNAEALQNAASVLCISPEELQEALTSHCVV 670
Cdd:pfam00063  237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   671 TRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQpdeniCSAGGGMNV-GILDIFGFENFQRNSFEQLCIN 749
Cdd:pfam00063  314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLD-----VKTIEKASFiGVLDIYGFEIFEKNSFEQLCIN 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   750 IANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL-RC 828
Cdd:pfam00063  389 YVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFsKH 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   829 KYFWRPK-GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARITvass 907
Cdd:pfam00063  469 PHFQKPRlQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST---- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   908 slpphFSAGKAKvdtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLR 987
Cdd:pfam00063  545 -----PKRTKKK----------------RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLR 603
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747   988 STGILETVSIRRQGYSHRILFEEFVKRYYYLA-FTAHQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:pfam00063  604 CNGVLEGIRIRRAGFPNRITFQEFVQRYRILApKTWPKWKGDAKKGCEAILQSLNLDKeeYQFGKTKIFFR 674
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
13-303 0e+00

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 670.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   13 LYGLFHYNPMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPN 92
Cdd:cd06639     1 LYGLFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   93 VVKFYGMFYKADHCVGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 172
Cdd:cd06639    81 VVKFYGMFYKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  173 LTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVK 252
Cdd:cd06639   161 LTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  253 TLFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06639   241 ALFKIPRNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
367-1055 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 662.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd01381     2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQhltFLGKANNQ--TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYL 524
Cdd:cd01381    82 SGAGKTESTKLILQ---YLAAISGQhsWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  525 LEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIAdetgrvMHDITSKE--SYRRQFEAIQHCFRIIG 602
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEK-KKLELGDASDYYYLT------QGNCLTCEgrDDAAEFADIRSAMKVLM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  603 FTDKEVHSVYRILAGILNIGNIEFAAISSQHqTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTV 682
Cdd:cd01381   232 FTDEEIWDIFKLLAAILHLGNIKFEATVVDN-LDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  683 DRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQYYF 759
Cdd:cd01381   311 EQALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTS-----IGVLDIFGFENFEVNSFEQLCINFANENLQQFF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  760 NQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRC-KYFWRPKG-V 837
Cdd:cd01381   386 VRHIFKLEQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNnKNYLKPKSdL 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  838 ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFsipltktgnlaqtraritvassslpphfsagk 917
Cdd:cd01381   466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-------------------------------- 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  918 akvdtlEVIRHPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSI 997
Cdd:cd01381   514 ------NEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRI 587
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  998 RRQGYSHRILFEEFVKRYYYL------AFTAHQTPLASKESCVAILEKsrlDHWVLGKTKVFLK 1055
Cdd:cd01381   588 RKAGYPIRHTFEEFVERYRVLvpgippAHKTDCRAATRKICCAVLGGD---ADYQLGKTKIFLK 648
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
368-1055 0e+00

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 656.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMV----TLSKDQCIVI 443
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  444 SGESGSGKTESAHLIVQHLTFLGKANNQtLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTpTGVVMGARISEY 523
Cdd:cd14889    83 SGESGAGKTESTKLLLRQIMELCRGNSQ-LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKINEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  524 LLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVmhdiTSKESYRRQFEAIQHCFRIIGF 603
Cdd:cd14889   161 LLEKSRVVHQDGGEENFHIFYYMFAGISAEDR-ENYGLLDPGKYRYLNNGAGCK----REVQYWKKKYDEVCNAMDMVGF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  604 TDKEVHSVYRILAGILNIGNIEFaaisSQHQTDKSEVPNAEA--LQNAASVLCISPEELQEALTSHCVVTRGETIIRANT 681
Cdd:cd14889   236 TEQEEVDMFTILAGILSLGNITF----EMDDDEALKVENDSNgwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  682 VDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQ 761
Cdd:cd14889   312 KQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDD--SSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  762 HVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLR-CKYFWRPKGVELC 840
Cdd:cd14889   390 HIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKgNSYYGKSRSKSPK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  841 FGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARITVASsslpphfSAGKAKv 920
Cdd:cd14889   470 FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGS-------DNFNST- 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  921 dtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQ 1000
Cdd:cd14889   542 ---------------RKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRRE 606
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578803747 1001 GYSHRILFEEFVKRYYYLAFTAHQTplASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd14889   607 GFSWRPSFAEFAERYKILLCEPALP--GTKQSCLRILKATKLVGWKCGKTRLFFK 659
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
367-1055 0e+00

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 651.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVK-RASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14897     2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd14897    82 ESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRlpeEKPPRYI----ADETGRVMHDITSKESYRRQFEAIQHCFRII 601
Cdd:cd14897   162 EKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL---EDPDCHRilrdDNRNRPVFNDSEELEYYRQMFHDLTNIMKLI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  602 GFTDKEVHSVYRILAGILNIGNIEFAAISSqhqTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANT 681
Cdd:cd14897   239 GFSEEDISVIFTILAAILHLTNIVFIPDED---TDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  682 VDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQ 761
Cdd:cd14897   316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  762 HVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDnlRCK---YFWRPKGVE 838
Cdd:cd14897   396 YVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNK--YCGespRYVASPGNR 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  839 LCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraritvassslpphfsagka 918
Cdd:cd14897   474 VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------------- 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  919 kvdtlevirhpeettnmkrqtvaSYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIR 998
Cdd:cd14897   522 -----------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIR 578
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  999 RQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd14897   579 RDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILKTAGIKGYQFGKTKVFLK 635
COG5022 COG5022
Myosin heavy chain [General function prediction only];
324-1134 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 636.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  324 KHQNPVAKTRHERMHTRRPYHVEDAEKYCLE---DDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSI 400
Cdd:COG5022    35 KVTEEGKKEDGESVSVKKKVLGNDRIKLPKFdgvDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  401 YSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGESGSGKTESAHLIVQHLTFLGKANN---QTLREKI 477
Cdd:COG5022   115 YTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTveiSSIEKQI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  478 LQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQ-KKL 556
Cdd:COG5022   195 LATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEElKKL 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  557 SDFRLPEEKppRYIADETGRVMHDITSKESYRRQFEAiqhcFRIIGFTDKEVHSVYRILAGILNIGNIEFAAissqHQTD 636
Cdd:COG5022   275 LLLQNPKDY--IYLSQGGCDKIDGIDDAKEFKITLDA----LKTIGIDEEEQDQIFKILAAILHIGNIEFKE----DRNG 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  637 KSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPde 716
Cdd:COG5022   345 AAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-- 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  717 nicSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQK 796
Cdd:COG5022   423 ---SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKK 499
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  797 -PLGLLALLDEESRFPQATDQTLVDKFEDNLRCK---YFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVV 872
Cdd:COG5022   500 nPLGILSLLDEECVMPHATDESFTSKLAQRLNKNsnpKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLEL 579
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  873 LRTSENKLLQQLFSIpltktgnlaqtraritvassslpphfsagkakvdtlevirhpEETTNMKRQ--TVASYFRYSLMD 950
Cdd:COG5022   580 LKASTNEFVSTLFDD------------------------------------------EENIESKGRfpTLGSRFKESLNS 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  951 LLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLA-----FTAHQT 1025
Cdd:COG5022   618 LMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTW 697
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747 1026 PLASKESCVAILEKSRLDHWV--LGKTKVFLK----YYHVEQLNLLLREVIGRvvvLQAYTKGWLGARRYKRVReKREKG 1099
Cdd:COG5022   698 KEDTKNAVKSILEELVIDSSKyqIGNTKVFFKagvlAALEDMRDAKLDNIATR---IQRAIRGRYLRRRYLQAL-KRIKK 773
                         810       820       830
                  ....*....|....*....|....*....|....*
gi 578803747 1100 AIAIQSAWRGYDARRKFKKISNRRNESAAHNQAGD 1134
Cdd:COG5022   774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGS 808
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
367-1055 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 601.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd01385     2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLG-KANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd01385    82 SGSGKTESTNFLLHHLTALSqKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPpRYIADETGRVMHDitskESYRRQFEAIQHCFRIIGFTD 605
Cdd:cd01385   162 EKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDY-HYLNQSDCYTLEG----EDEKYEFERLKQAMEMVGFLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRA 685
Cdd:cd01385   237 ETQRQIFSVLSAVLHLGNIEYKK-KAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  686 ADVRDAMSKALYGRLFSWIVNRINTLLQPDENIcSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFA 765
Cdd:cd01385   316 IATRDAMAKCLYSALFDWIVLRINHALLNKKDL-EEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  766 LEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKF----EDNlrcKYFWRPKGVELCF 841
Cdd:cd01385   395 LEQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFkqqhKDN---KYYEKPQVMEPAF 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  842 GIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARITVASSSLpphfSAGKA--- 918
Cdd:cd01385   472 IIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFR----EAGRRraq 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  919 KVDTLEVIRHpEETTNM--------KRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTG 990
Cdd:cd01385   548 RTAGHSLTLH-DRTTKSllhlhkkkKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  991 ILETVSIRRQGYSHRILFEEFVKRYYYLaftAHQTPLASKESCVAILEKSRLD--HWVLGKTKVFLK 1055
Cdd:cd01385   627 MLETVRIRRSGYSVRYTFQEFITQFQVL---LPKGLISSKEDIKDFLEKLNLDrdNYQIGKTKVFLK 690
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
366-1055 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 599.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd01378     1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFL---GKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISE 522
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVsggSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  523 YLLEKSRVIKQAAREKNFHIFYYIYAGLhHQKKLSDFRLpeEKPPRYI---ADETGRV--MHDitSKEsyrrqFEAIQHC 597
Cdd:cd01378   161 YLLEKSRVVGQIKGERNFHIFYQLLKGA-SQEYLQELGL--QRPEQYYyysKSGCFDVdgIDD--AAD-----FKEVLNA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  598 FRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSqhqtDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGE--- 674
Cdd:cd01378   231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE----GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrs 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  675 TIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmNVGILDIFGFENFQRNSFEQLCINIANEQ 754
Cdd:cd01378   307 VYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKK----VIGVLDIYGFEIFEKNSFEQFCINYVNEK 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  755 IQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFP-QATDQTLVDKFEDNLRC-KYFW 832
Cdd:cd01378   383 LQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNhPHFE 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  833 RPKGVEL----CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFsipltktgnlaqtraritvasss 908
Cdd:cd01378   463 CPSGHFElrrgEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF----------------------- 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  909 lPPhfsagkakvdtlevirhPEETTNMKR-QTVASYFRYS---LMDLLSKMvvgQPHFVRCIKPNDDREALQFSRERVLA 984
Cdd:cd01378   520 -PE-----------------GVDLDSKKRpPTAGTKFKNSanaLVETLMKK---QPSYIRCIKPNDNKSPGEFDEELVLH 578
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  985 QLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLA---FTAHQTPlaSKESCVAILEKSRL--DHWVLGKTKVFLK 1055
Cdd:cd01378   579 QVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSpktWPAWDGT--WQGGVESILKDLNIppEEYQMGKTKIFIR 652
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
367-1055 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 592.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14883     2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTflGKANNQTLRE-KILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd14883    82 SGAGKTETTKLILQYLC--AVTNNHSWVEqQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSD-FRLPEEKPPRYIaDETGRV----MHDitskesyRRQFEAIQHCFRI 600
Cdd:cd14883   160 EQSRITFQAPGERNYHVFYQLLAGAKHSKELKEkLKLGEPEDYHYL-NQSGCIridnIND-------KKDFDHLRLAMNV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  601 IGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEvpNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRAN 680
Cdd:cd14883   232 LGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVE--DKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  681 TVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQYYFN 760
Cdd:cd14883   310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF-----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFN 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  761 QHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL-RCKYFWRP--KGV 837
Cdd:cd14883   385 HYVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHeKHPYYEKPdrRRW 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  838 ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPltktgNLAQTRARITVASSSLPphfSAGK 917
Cdd:cd14883   465 KTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYP-----DLLALTGLSISLGGDTT---SRGT 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  918 AKvdtlevirhpeettnmKRQTVASYFRY---SLMDLLSKMvvgQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILET 994
Cdd:cd14883   537 SK----------------GKPTVGDTFKHqlqSLVDVLSAT---QPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEI 597
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  995 VSIRRQGYSHRILFEEFVKRYYYLAFTAHQT-PLASKESCVAILEKSRL--DHWVLGKTKVFLK 1055
Cdd:cd14883   598 IRIRKEGFPIHLTFKEFVDRYLCLDPRARSAdHKETCGAVRALMGLGGLpeDEWQVGKTKVFLR 661
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
367-1055 0e+00

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 592.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd01387     2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTpTGVVMGARISEYLLE 526
Cdd:cd01387    82 SGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  527 KSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKppRYIADETGrvmHDITSKESYRRQFEAIQHCFRIIGFTDK 606
Cdd:cd01387   161 KSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEK--YFYLNQGG---NCEIAGKSDADDFRRLLAAMQVLGFSSE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  607 EVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAA 686
Cdd:cd01387   236 EQDSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQAL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  687 DVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFAL 766
Cdd:cd01387   316 DARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-----IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  767 EQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKfednlrCKY-------FWRPKGVEL 839
Cdd:cd01387   391 EQEEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEK------CHYhhalnelYSKPRMPLP 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  840 CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaQTRARITVAssslPPHFSAGKAk 919
Cdd:cd01387   465 EFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS----------SHRAQTDKA----PPRLGKGRF- 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  920 vdtleVIRHPeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRR 999
Cdd:cd01387   530 -----VTMKP------RTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRK 598
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747 1000 QGYSHRILFEEFVKRYYYLAFTAHQ--TPLASKESCVAILEKSR-LDHWVLGKTKVFLK 1055
Cdd:cd01387   599 EGYPVRLPFQVFIDRYRCLVALKLPrpAPGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
367-1055 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 587.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd01377     2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQ---------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMG 517
Cdd:cd01377    82 SGAGKTENTKKVIQYLASVAASSKKkkesgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  518 ARISEYLLEKSRVIKQAAREKNFHIFYYIYAGlHHQKKLSDFRLpeEKPP---RYIADetGRVM-HDITSKEsyrrQFEA 593
Cdd:cd01377   162 ADIETYLLEKSRVVRQAKGERNYHIFYQLLSG-ADPELKEKLLL--TGDPsyyFFLSQ--GELTiDGVDDAE----EFKL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  594 IQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQtdkSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRG 673
Cdd:cd01377   233 TDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQ---AELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  674 ETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANE 753
Cdd:cd01377   310 EWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYF-----IGVLDIAGFEIFEFNSFEQLCINYTNE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  754 QIQYYFNQHVFALEQMEYQNEGIDAVPVEY-EDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKY 830
Cdd:cd01377   385 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHlgKSKN 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  831 FWRPKG--VELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARitvaSSS 908
Cdd:cd01377   465 FKKPKPkkSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKK----GGS 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  909 LpphfsagkakvdtlevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRS 988
Cdd:cd01377   541 F----------------------------RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRC 592
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  989 TGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPL-ASKESCVAILEKSRLDHWV--LGKTKVFLK 1055
Cdd:cd01377   593 NGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFdDGKAACEKILKALQLDPELyrIGNTKVFFK 662
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
368-1055 0e+00

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 583.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADL-LIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd01380     3 VLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQTLR--EKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYL 524
Cdd:cd01380    83 SGAGKTVSAKYAMRYFATVGGSSSGETQveEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  525 LEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLsDFRLpeEKPPRYIADETGRVMHDITSkeSYRRQFEAIQHCFRIIGFT 604
Cdd:cd01380   163 LEKSRVVFQAEEERNYHIFYQLCAAASLPELK-ELHL--GSAEDFFYTNQGGSPVIDGV--DDAAEFEETRKALTLLGIS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  605 DKEVHSVYRILAGILNIGNIEFAAISSQHQTDKsevPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDR 684
Cdd:cd01380   238 EEEQMEIFRILAAILHLGNVEIKATRNDSASIS---PDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  685 AADVRDAMSKALYGRLFSWIVNRINTLL--QPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQH 762
Cdd:cd01380   315 AIVARDALAKHIYAQLFDWIVDRINKALasPVKEKQHSF-----IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  763 VFALEQMEYQNEGIDAVPVEYEDNRPLLDMFlQKPLGLLALLDEESRFPQATDQTLVDKFEDNL---RCKYFWRPKGVEL 839
Cdd:cd01380   390 VFKLEQEEYVKEEIEWSFIDFYDNQPCIDLI-EGKLGILDLLDEECRLPKGSDENWAQKLYNQHlkkPNKHFKKPRFSNT 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  840 CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENkllqqlfsipltktgnlaqtraritvassslpphfsagkak 919
Cdd:cd01380   469 AFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN----------------------------------------- 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  920 vdtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRR 999
Cdd:cd01380   508 ----------------RKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISA 571
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747 1000 QGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLD--HWVLGKTKVFLK 1055
Cdd:cd01380   572 AGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILDpdKYQFGKTKIFFR 629
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
368-1055 0e+00

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 578.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHgvKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd01383     3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQTLREkILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLEK 527
Cdd:cd01383    81 GAGKTETAKIAMQYLAALGGGSSGIENE-ILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  528 SRVIKQAAREKNFHIFYYIYAGLHH--QKKLSdfrLPEEKPPRYIADETGRVMHDITSKESYRRQFEAiqhcFRIIGFTD 605
Cdd:cd01383   160 SRVVQLANGERSYHIFYQLCAGASPalREKLN---LKSASEYKYLNQSNCLTIDGVDDAKKFHELKEA----LDTVGISK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAISSQhqtDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRA 685
Cdd:cd01383   233 EDQEHIFQMLAAVLWLGNISFQVIDNE---NHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  686 ADVRDAMSKALYGRLFSWIVNRINTLLQPDEnicsAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFA 765
Cdd:cd01383   310 IDARDALAKAIYASLFDWLVEQINKSLEVGK----RRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  766 LEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL---RCKYFWRPKGvelcFG 842
Cdd:cd01383   386 LEQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLksnSCFKGERGGA----FT 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  843 IQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQlfsipltktgnlaqtraritvassslpphFSAGKAKVDT 922
Cdd:cd01383   462 IRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQL-----------------------------FASKMLDASR 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  923 LEVIRHPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGY 1002
Cdd:cd01383   513 KALPLTKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGY 592
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747 1003 SHRILFEEFVKRYYYL---AFTAHQTPLAskeSCVAILEKSRL--DHWVLGKTKVFLK 1055
Cdd:cd01383   593 PTRMTHQEFARRYGFLlpeDVSASQDPLS---TSVAILQQFNIlpEMYQVGYTKLFFR 647
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
368-1055 0e+00

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 571.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd01384     3 VLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQ---TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEY 523
Cdd:cd01384    83 SGAGKTETTKMLMQYLAYMGGRAVTegrSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  524 LLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKESYRRQFEAIqhcfRIIGF 603
Cdd:cd01384   163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDR-EKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAM----DVVGI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  604 TDKEVHSVYRILAGILNIGNIEFAAI----SSQHQTDKSEvpnaEALQNAASVLCISPEELQEALTSHCVVTRGETIIRA 679
Cdd:cd01384   238 SEEEQDAIFRVVAAILHLGNIEFSKGeeddSSVPKDEKSE----FHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  680 NTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQYYF 759
Cdd:cd01384   314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL-----IGVLDIYGFESFKTNSFEQFCINLANEKLQQHF 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  760 NQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRC-KYFWRPKGVE 838
Cdd:cd01384   389 NQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDhKRFSKPKLSR 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  839 LCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFsipltktgnlaqtraritvassslPPHFSAGKA 918
Cdd:cd01384   469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF------------------------PPLPREGTS 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  919 KvdtlevirhpeettNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIR 998
Cdd:cd01384   525 S--------------SSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRIS 590
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  999 RQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd01384   591 CAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIGKTKVFLR 647
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
367-1055 0e+00

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 554.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14873     2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFL--------GKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMG 517
Cdd:cd14873    82 ESGAGKTESTKLILKFLSVIsqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  518 ARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIaDETGRVMHD-ITSKESYRRQFEAiqh 596
Cdd:cd14873   162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEER-EEFYLSTPENYHYL-NQSGCVEDKtISDQESFREVITA--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  597 cFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSevpnaeALQNAASVLCISPEELQEALTSHCVVTRGETI 676
Cdd:cd14873   237 -MEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKT------ALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  677 IRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSagggmnVGILDIFGFENFQRNSFEQLCINIANEQIQ 756
Cdd:cd14873   310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS------IGILDIFGFENFEVNHFEQFNINYANEKLQ 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  757 YYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFW-RPK 835
Cdd:cd14873   384 EYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDL-IEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYvKPR 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  836 GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtrariTVASSSlpphfsa 915
Cdd:cd14873   463 VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE----------------HVSSRN------- 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  916 gkaKVDTLEVirhpeeTTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETV 995
Cdd:cd14873   520 ---NQDTLKC------GSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETV 590
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  996 SIRRQGYSHRILFEEFVKRYYYLAfTAHQTPLASKESCVAILEK--SRLDHWVLGKTKVFLK 1055
Cdd:cd14873   591 RIRKAGYAVRRPFQDFYKRYKVLM-RNLALPEDVRGKCTSLLQLydASNSEWQLGKTKVFLR 651
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
29-302 1.29e-180

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 534.57  E-value: 1.29e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   29 LPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADH-CV 107
Cdd:cd06608     1 LPDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKDPpGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06608    81 DDQLWLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd06608   161 AQLDSTLGRRNTFIGTPYWMAPEVIACDQQPDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKS 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06608   241 PEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
26-302 2.84e-176

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 523.81  E-value: 2.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   26 LESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADH 105
Cdd:cd06638    10 FDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYKKDV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 CVGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd06638    90 KNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTL 265
Cdd:cd06638   170 VSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTL 249
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 LHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06638   250 HQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
368-1052 5.46e-172

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 526.65  E-value: 5.46e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYH--GVKRAsnPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14872     3 IVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMhkGPKEM--PPHTYNIADDAYRAMIVDAMNQSILISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHlivQHLTFL----GKANNqtLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARIS 521
Cdd:cd14872    81 ESGAGKTEATK---QCLSFFaevaGSTNG--VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  522 EYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQkklSDFRLPEEKPPRYI----ADETgRVMHDItskesyrRQFEAIQHC 597
Cdd:cd14872   156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPA---SRGGWGSSAAYGYLslsgCIEV-EGVDDV-------ADFEEVVLA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  598 FRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRG--ET 675
Cdd:cd14872   225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPT 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  676 IIRANTVdRAADVRDAMSKALYGRLFSWIVNRINTLLQPDenicSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQI 755
Cdd:cd14872   305 RIPLTPA-QATDACDALAKAAYSRLFDWLVKKINESMRPQ----KGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  756 QYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPK 835
Cdd:cd14872   380 QQHFNQYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYA 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  836 GV---ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFsipltktgnlaqtraritvassslPPh 912
Cdd:cd14872   460 EVrtsRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF------------------------PP- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 fSAGKAKVdtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGIL 992
Cdd:cd14872   515 -SEGDQKT---------------SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVF 578
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  993 ETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHW---VLGKTKV 1052
Cdd:cd14872   579 EAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVGPDDRQRCDLLLKSLKQDFskvQVGKTRV 641
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
368-1055 3.50e-160

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 496.22  E-value: 3.50e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNL-SIYSPQFSRLYHGVKRASNPPHIFASADAAY----QCMVTLSKDQCIV 442
Cdd:cd14890     3 LLHTLRLRYERDEIYTYVGPILISINPYKSIpDLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQSII 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  443 ISGESGSGKTESAHLIVQHLT---------------FLGKANNQT---LREKILQVNSLVEAFGNSCTAINDNSSRFGKY 504
Cdd:cd14890    83 ISGESGAGKTEATKIIMQYLAritsgfaqgasgegeAASEAIEQTlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  505 LEMMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLsdfRLPEEKPPRYIadetgRVMHDITSK 584
Cdd:cd14890   163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRE---RLKLQTPVEYF-----YLRGECSSI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  585 ESYR--RQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQE 662
Cdd:cd14890   235 PSCDdaKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFE--SENDTTVLEDATTLQSLKLAAELLGVNEDALEK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  663 ALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRIN-TLLQPDENICSagggmnVGILDIFGFENFQRN 741
Cdd:cd14890   313 ALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNrTISSPDDKWGF------IGVLDIYGFEKFEWN 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  742 SFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKP---LGLLALLDEESRFPQATDQTl 818
Cdd:cd14890   387 TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkPGIFITLDDCWRFKGEEANK- 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  819 vdKFEDNLRCKY------------------FWRPK-GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSenk 879
Cdd:cd14890   466 --KFVSQLHASFgrksgsggtrrgssqhphFVHPKfDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS--- 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  880 llqqlfsipltktgnlaqtraritvassslpphfsagkakvdtlevirhpeeTTNMKRQTVASYFRYSLMDLLSKMVVGQ 959
Cdd:cd14890   541 ----------------------------------------------------RRSIREVSVGAQFRTQLQELMAKISLTN 568
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  960 PHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHqtplaSKESCVAILEK 1039
Cdd:cd14890   569 PRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAE-----NIEQLVAVLSK 643
                         730       740
                  ....*....|....*....|
gi 578803747 1040 sRL----DHWVLGKTKVFLK 1055
Cdd:cd14890   644 -MLglgkADWQIGSSKIFLK 662
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
368-1055 1.45e-156

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 486.89  E-value: 1.45e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNL-SIYSPQFsRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14888     3 ILHSLNLRFDIDEIYTFTGPILIAVNPFKTIpGLYSDEM-LLKFIQPSISKSPHVFSTASSAYQGMCNNKKSQTILISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQ---TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT---------GV 514
Cdd:cd14888    82 SGAGKTESTKYVMKFLACAGSEDIKkrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskrmsgdrGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  515 VMGARISEYLLEKSRVIKQAAREKNFHIFY--------YIYAGLHHQKKLSDFRLPEEKPPRYIADE-----------TG 575
Cdd:cd14888   162 LCGAKIQTYLLEKVRVCDQQEGERNYHIFYqlcaaareAKNTGLSYEENDEKLAKGADAKPISIDMSsfephlkfrylTK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  576 RVMHDITSKESYRrQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCI 655
Cdd:cd14888   242 SSCHELPDVDDLE-EFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  656 SPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL--QPDENICSAGggmnvgILDIF 733
Cdd:cd14888   321 DAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgySKDNSLLFCG------VLDIF 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  734 GFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQA 813
Cdd:cd14888   395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGG 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  814 TDQTL----VDKFEDNLRckyFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFsipl 889
Cdd:cd14888   475 KDQGLcnklCQKHKGHKR---FDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF---- 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  890 tktgnlaqtraritvassslpphfsagKAKVDtleviRHPEETTNMKR-QTVASYFRYSLMDLLSKMVVGQPHFVRCIKP 968
Cdd:cd14888   548 ---------------------------SAYLR-----RGTDGNTKKKKfVTVSSEFRNQLDVLMETIDKTEPHFIRCIKP 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  969 NDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYlaftahqtpLASKEscvailEKSRLDHWVLG 1048
Cdd:cd14888   596 NSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRI---------LLNGE------GKKQLSIWAVG 660

                  ....*..
gi 578803747 1049 KTKVFLK 1055
Cdd:cd14888   661 KTLCFFK 667
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
368-1055 2.58e-155

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 483.51  E-value: 2.58e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNL-SIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14903     3 ILYNVKKRFLRKLPYTYTGDICIAVNPYQWLpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHL-TFLGKANNQTLReKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd14903    83 SGAGKTETTKILMNHLaTIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSdfrLPEEKPPRYIADETGRVMHDITSKESYRRQFEAIQhcfrIIGFTD 605
Cdd:cd14903   162 EKTRVISHERPERNYHIFYQLLASPDVEERLF---LDSANECAYTGANKTIKIEGMSDRKHFARTKEALS----LIGVSE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEvPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRA 685
Cdd:cd14903   235 EKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIA-PGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  686 ADVRDAMSKALYGRLFSWIVNRINTLLQPDENIcsaggGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFA 765
Cdd:cd14903   314 EDCRDALAKAIYSNVFDWLVATINASLGNDAKM-----ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  766 LEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKpLGLLALLDEESRFPQATDQTLVDK----FEDNLRCKYFwrPKGVELCF 841
Cdd:cd14903   389 TVQIEYEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKlssiHKDEQDVIEF--PRTSRTQF 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  842 GIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARitvassslpphfSAGKAKVD 921
Cdd:cd14903   466 TIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLAR------------GARRRRGG 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  922 TLEVirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQG 1001
Cdd:cd14903   534 ALTT------------TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAA 601
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747 1002 YSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLD---HWVLGKTKVFLK 1055
Cdd:cd14903   602 YPNRLLHEEFLDKFWLFLPEGRNTDVPVAERCEALMKKLKLEspeQYQMGLTRIYFQ 658
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
367-1055 7.19e-152

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 474.30  E-value: 7.19e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLY---HGVKRASNPPHIFASADAAYQCMVTLSKDQCIVI 443
Cdd:cd14878     2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  444 SGESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTP-TGVVMGARISE 522
Cdd:cd14878    82 SGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCErKKHLTGARIYT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  523 YLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADEtgrVMHDITSKESY--RRQFEAIQHCFRI 600
Cdd:cd14878   162 YMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEK-YGLHLNNLCAHRYLNQT---MREDVSTAERSlnREKLAVLKQALNV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  601 IGFTDKEVHSVYRILAGILNIGNIEFAAISsqhQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRAN 680
Cdd:cd14878   238 VGFSSLEVENLFVILSAILHLGDIRFTALT---EADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  681 TVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFN 760
Cdd:cd14878   315 TIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSM-QTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  761 QHVFALEQMEYQNEGIDAVPVEYEDNRP-LLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFE-----DNLRCKYF--- 831
Cdd:cd14878   394 EVLFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllesSNTNAVYSpmk 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  832 -----WRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTktgnlaqtraritvas 906
Cdd:cd14878   474 dgngnVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV---------------- 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  907 sslpphfsagkakvdtlevirhpeettnmkrqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQL 986
Cdd:cd14878   538 --------------------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQL 585
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  987 RSTGILETVSIRRQGYSHRILFEEFVKRYYYLA--FTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd14878   586 QYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
367-1055 7.88e-151

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 470.80  E-value: 7.88e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14896     2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTpTGVVMGARISEYLLE 526
Cdd:cd14896    82 SGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  527 KSRVIKQAAREKNFHIFYYIYAGLHHQKKLsdfRLPEEKPPRYIADETGRVMhDITSKESyRRQFEAIQHCFRIIGFTDK 606
Cdd:cd14896   161 TSRVVFQAQAERSFHVFYELLAGLDPEERE---QLSLQGPETYYYLNQGGAC-RLQGKED-AQDFEGLLKALQGLGLCAE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  607 EVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEAlQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAA 686
Cdd:cd14896   236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEI-HTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  687 DVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGggmNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFAL 766
Cdd:cd14896   315 DARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDA---TIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQ 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  767 EQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKfednlrCKY-------FWRPKGVEL 839
Cdd:cd14896   392 EEEECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQK------CHYhhgdhpsYAKPQLPLP 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  840 CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraritvassslpphfsagKAK 919
Cdd:cd14896   466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ------------------------------EAE 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  920 vdtlevirhPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRR 999
Cdd:cd14896   516 ---------PQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRS 586
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747 1000 QGYSHRILFEEFVKRYYYLAfTAHQTPLASKESCVAILEK---SRLDHWVLGKTKVFLK 1055
Cdd:cd14896   587 EGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQvlgAESPLYHLGATKVLLK 644
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
367-1054 1.16e-148

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 465.80  E-value: 1.16e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLY--HGVKRASN----PPHIFASADAAYQCMVTLSK--- 437
Cdd:cd14901     2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyeHGERRAAGerklPPHVYAVADKAFRAMLFASRgqk 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  438 -DQCIVISGESGSGKTESAHLIVQHLTFLGKANNQ--------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMM 508
Cdd:cd14901    82 cDQSILVSGESGAGKTETTKIIMNYLASVSSATTHgqnatereNVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  509 FTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGlHHQKKLSDFRLPEEKPPRYiadetgrvmhdITSKESYR 588
Cdd:cd14901   162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRG-ASSDELHALGLTHVEEYKY-----------LNSSQCYD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  589 R--------QFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaISSQHQTDKSEVPNAEALQNAASVLCISPEEL 660
Cdd:cd14901   230 RrdgvddsvQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCF--VKKDGEGGTFSMSSLANVRAACDLLGLDMDVL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  661 QEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDEnicSAGGGMNVGILDIFGFENFQR 740
Cdd:cd14901   308 EKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSE---STGASRFIGIVDIFGFEIFAT 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  741 NSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVD 820
Cdd:cd14901   385 NSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLAN 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  821 KFEDNLRCK-YFWRPK--GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQqlfsipltktgnlaq 897
Cdd:cd14901   465 KYYDLLAKHaSFSVSKlqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS--------------- 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  898 traritvassslpphfsagkakvdtlevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQF 977
Cdd:cd14901   530 ----------------------------------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEF 569
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  978 SRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLA-----------FTAHQTPLASKESCVAIlekSRLDHWV 1046
Cdd:cd14901   570 DAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLApdgasdtwkvnELAERLMSQLQHSELNI---EHLPPFQ 646

                  ....*...
gi 578803747 1047 LGKTKVFL 1054
Cdd:cd14901   647 VGKTKVFL 654
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
372-1055 1.54e-148

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 465.39  E-value: 1.54e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  372 LQKRYADLLIYTYVGDILIALNPFQNLS-IYS-PQFSRLYHGVKRASN-PPHIFASADAAYQCM----VTLSKDQCIVIS 444
Cdd:cd14892     7 LRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKEEATASSpPPHVFSIAERAYRAMkgvgKGQGTPQSIVVS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  445 GESGSGKTESAHLIVQHLTFLGKANNQT------------LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT 512
Cdd:cd14892    87 GESGAGKTEASKYIMKYLATASKLAKGAstskgaanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  513 GVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADETGRV--MHDITskesyrrQ 590
Cdd:cd14892   167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVdgVDDAT-------E 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  591 FEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDkSEVPNAEALQNAASVLCISPEELQEALTSHCVV 670
Cdd:cd14892   240 FKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVF-AQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  671 T-RGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQpdENICSAGGGMN-------VGILDIFGFENFQRNS 742
Cdd:cd14892   319 TaRGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHK--QQTSGVTGGAAsptfspfIGILDIFGFEIMPTNS 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  743 FEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFP-QATDQTLVDK 821
Cdd:cd14892   397 FEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTI 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  822 FEDN--LRCKYFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSenkllqqlfsipltktgnlaqtr 899
Cdd:cd14892   477 YHQThlDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------------------- 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  900 aritvassslpphfsagkakvdtlevirhpeettnmkrqtvaSYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSR 979
Cdd:cd14892   534 ------------------------------------------SKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSC 571
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  980 ERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLA---------FTAHQTPLASKESCVAILEKSRLDHWVLGKT 1050
Cdd:cd14892   572 ELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvaasPDACDATTARKKCEEIVARALERENFQLGRT 651

                  ....*
gi 578803747 1051 KVFLK 1055
Cdd:cd14892   652 KVFLR 656
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
367-1015 1.84e-146

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 459.41  E-value: 1.84e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd01382     2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd01382    82 ESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGlhhqkklsdfrLPEekppryiaDETGRVMHDITSKESyrRQFEAIQHCFRIIGFTD 605
Cdd:cd01382   162 EKSRICVQSKEERNYHIFYRLCAG-----------APE--------DLREKLLKDPLLDDV--GDFIRMDKAMKKIGLSD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAAISSQhQTDKSEVPN--AEALQNAASVLCISPEELQEALTSHCVVTRGE----TIIRA 679
Cdd:cd01382   221 EEKLDIFRVVAAVLHLGNIEFEENGSD-SGGGCNVKPksEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKV 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  680 N-TVDRAADVRDAMSKALYGRLFSWIVNRINTLLqPDENicSAGggmNVGILDIFGFENFQRNSFEQLCINIANEQIQYY 758
Cdd:cd01382   300 PlKVEEANNARDALAKAIYSKLFDHIVNRINQCI-PFET--SSY---FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQF 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  759 FNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQ----TLVDKFEDNLRckyFWRP 834
Cdd:cd01382   374 FNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQhftsAVHQKHKNHFR---LSIP 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 KGVEL----------CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARITV 904
Cdd:cd01382   451 RKSKLkihrnlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAGKLSF 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  905 ASsslpphfsagkakvdtlevirhpeettnmkrqtVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLA 984
Cdd:cd01382   531 IS---------------------------------VGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILS 577
                         650       660       670
                  ....*....|....*....|....*....|.
gi 578803747  985 QLRSTGILETVSIRRQGYSHRILFEEFVKRY 1015
Cdd:cd01382   578 QLQCSGMVSVLDLMQGGFPSRTSFHDLYNMY 608
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
367-1055 8.32e-143

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 450.62  E-value: 8.32e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14920     2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQT--------LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGA 518
Cdd:cd14920    82 SGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  519 RISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVmhditSKESYRRQFEAIQHCF 598
Cdd:cd14920   162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLK-SDLLLEGFNNYRFLSNGYIPI-----PGQQDKDNFQETMEAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  599 RIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEA-LTSHCVVTRgETII 677
Cdd:cd14920   236 HIMGFSHEEILSMLKVVSSVLQFGNISF---KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR-DYVQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  678 RANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQY 757
Cdd:cd14920   312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR----QGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  758 YFNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMFLQ--KPLGLLALLDEESRFPQATDQTLVDKF--EDNLRCKYFw 832
Cdd:cd14920   388 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLvqEQGSHSKFQ- 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  833 RPKGV--ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSiPLTKTGNLAQTraritvasSSLP 910
Cdd:cd14920   467 KPRQLkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWK-DVDRIVGLDQV--------TGMT 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  911 PHFSAGKAKvdtlevirhpeeTTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTG 990
Cdd:cd14920   538 ETAFGSAYK------------TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 605
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  991 ILETVSIRRQGYSHRILFEEFVKRYYYLAFTA-HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14920   606 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 673
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
367-1055 2.11e-142

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276869  Cd Length: 653  Bit Score: 449.01  E-value: 2.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNL-SIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14904     2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIdNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd14904    82 ESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKkLSDFRLPEEKPPRYIADETGRVMHDITSKESYrrqFEAIQHCFRIIGFTD 605
Cdd:cd14904   162 EKSRVVSIAEGERNYHIFYQLLAGLSSEE-RKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKL---FASTQKSLSLIGLDN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEVHSVYRILAGILNIGNIEFAaissQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRA 685
Cdd:cd14904   238 DAQRTLFKILSGVLHLGEVMFD----KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  686 ADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFA 765
Cdd:cd14904   314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKG----QIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  766 LEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKpLGLLALLDEESRFPQATDQTLVDKFEDNLR------CKYFwrPKGVEL 839
Cdd:cd14904   390 TVEEEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdneSIDF--PKVKRT 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  840 CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraritvaSSSLPPHFSAGKAK 919
Cdd:cd14904   467 QFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG-------------------SSEAPSETKEGKSG 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  920 vdtlevirhpeETTNMKRqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRR 999
Cdd:cd14904   528 -----------KGTKAPK-SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITR 595
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747 1000 QGYSHRILFEEFVKRYYYLaFTAHQTPLASKESC----VAILEKSRLDHWVlGKTKVFLK 1055
Cdd:cd14904   596 SGYPSRLTPKELATRYAIM-FPPSMHSKDVRRTCsvfmTAIGRKSPLEYQI-GKSLIYFK 653
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
367-1055 3.28e-142

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 449.10  E-value: 3.28e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYH--------GVKRASNPPHIFASADAAYQCMVTLSK 437
Cdd:cd14907     2 ELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKeqiiqngeYFDIKKEPPHIYAIAALAFKQLFENNK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  438 DQCIVISGESGSGKTESAHLIVQHLTFLGKANNQ-------------------TLREKILQVNSLVEAFGNSCTAINDNS 498
Cdd:cd14907    82 KQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNseevltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDNS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  499 SRFGKYLEMMFT-PTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKkLSDFRLpEEKPPRYIADE---- 573
Cdd:cd14907   162 SRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQL-LQQLGL-KNQLSGDRYDYlkks 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  574 ---TGRVMHDITSkesyrrqFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaisSQHQTDKSEVP---NAEALQ 647
Cdd:cd14907   240 ncyEVDTINDEKL-------FKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQF----DDSTLDDNSPCcvkNKETLQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  648 NAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRIN-TLLQPDENICSAGGG-- 724
Cdd:cd14907   309 IIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNdTIMPKDEKDQQLFQNky 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  725 MNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGID--AVPVEYEDNRPLLDMFLQKPLGLLA 802
Cdd:cd14907   389 LSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIFN 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  803 LLDEESRFPQATDQTLVDKFED--NLRCKYFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKL 880
Cdd:cd14907   469 LLDDSCKLATGTDEKLLNKIKKqhKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRI 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  881 LQQLFSiplTKTGNLAQTRARITVassslpphfsagkakvdtlevirhpeetTNMKRQTVASYFRYSLMDLLSKMVVGQP 960
Cdd:cd14907   549 ISSIFS---GEDGSQQQNQSKQKK----------------------------SQKKDKFLGSKFRNQMKQLMNELMQCDV 597
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  961 HFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYylaftahqtplaskescvaILEKS 1040
Cdd:cd14907   598 HFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYS-------------------LLKKN 658
                         730
                  ....*....|....*
gi 578803747 1041 RLdhwvLGKTKVFLK 1055
Cdd:cd14907   659 VL----FGKTKIFMK 669
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
367-1055 2.27e-141

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 446.73  E-value: 2.27e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14929     2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLG-----KANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARIS 521
Cdd:cd14929    82 SGAGKTVNTKHIIQYFATIAamiesKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADID 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  522 EYLLEKSRVIKQAAREKNFHIFYYIYAGlhhQKKLSDFRLPEEKPPRYIADETGRVmhditSKESY--RRQFEAIQHCFR 599
Cdd:cd14929   162 IYLLEKSRVIFQQPGERNYHIFYQILSG---KKELRDLLLVSANPSDFHFCSCGAV-----AVESLddAEELLATEQAMD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  600 IIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEalqNAASVLCISPEELQEALTSHCVVTRGETIIRA 679
Cdd:cd14929   234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  680 NTVDRAADVRDAMSKALYGRLFSWIVNRINTLLqpDENICSAgggMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYF 759
Cdd:cd14929   311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVL--DAKLSRQ---FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  760 NQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDmFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCK--YFWRP-- 834
Cdd:cd14929   386 NQHMFVLEQEEYRKEGIDWVSIDFGlDLQACID-LIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKsvHFQKPkp 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 --KGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraRITVASSSLPph 912
Cdd:cd14929   465 dkKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------------NYISTDSAIQ-- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 FSAGKAKVDTlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGIL 992
Cdd:cd14929   529 FGEKKRKKGA-------------SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVL 595
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  993 ETVSIRRQGYSHRILFEEFVKRYYYL---AFTAHQTpLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14929   596 EGIRICREGFPNRLLYADFKQRYCILnprTFPKSKF-VSSRKAAEELLGSLEIDHtqYRFGITKVFFK 662
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
366-1055 2.34e-141

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 445.72  E-value: 2.34e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14882     1 ENILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQTlREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd14882    81 ESYSGKTTNARLLIKHLCYLGDGNRGA-TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIadetgRVMHDIT-SKESYRR--------QFEAIQH 596
Cdd:cd14882   160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLKEYNLKAGRNYRYL-----RIPPEVPpSKLKYRRddpegnveRYKEFEE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  597 CFRIIGFTDKEVHSVYRILAGILNIGNIEFAaissqhQTDKS-EVPNAEALQNAASVLCISPEELQEALTSHCVVTRGET 675
Cdd:cd14882   235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFR------QNGGYaELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  676 IIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENIcsAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQI 755
Cdd:cd14882   309 ERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAV--FGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  756 QYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRfpQATDQTLV-DKFEDNlRCKYFWRP 834
Cdd:cd14882   387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASR--SCQDQNYImDRIKEK-HSQFVKKH 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 KGVElcFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgNlAQTRaritvassslpphfs 914
Cdd:cd14882   464 SAHE--FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFT-------N-SQVR--------------- 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  915 agkakvdtlevirhpeettNMKrqTVASYFRYSLMDLLSKMVVGQ----PHFVRCIKPNDDREALQFSRERVLAQLRSTG 990
Cdd:cd14882   519 -------------------NMR--TLAATFRATSLELLKMLSIGAnsggTHFVRCIRSDLEYKPRGFHSEVVRQQMRALA 577
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  991 ILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd14882   578 VLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLLLIRLKMEGWAIGKTKVFLK 642
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
368-1015 4.21e-140

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 445.11  E-value: 4.21e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPF---------QNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMV-TLSK 437
Cdd:cd14902     3 LLQALSERFEHDQIYTSIGDILVALNPLkplpdlyseSQLNAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPERR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  438 DQCIVISGESGSGKTESAHLIVQHLTFLGKANNQTLRE---------KILQVNSLVEAFGNSCTAINDNSSRFGKYLEMM 508
Cdd:cd14902    83 NQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigkRILQTNPILESFGNAQTIRNDNSSRFGKFIKIQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  509 FTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQK-------KLSDFRL-----PEEKPPRYIADEtgr 576
Cdd:cd14902   163 FGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLldllglqKGGKYELlnsygPSFARKRAVADK--- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  577 vmhditskesYRRQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCIS 656
Cdd:cd14902   240 ----------YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLAKCAELMGVD 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  657 PEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGMN----VGILDI 732
Cdd:cd14902   310 VDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISDEDEelatIGILDI 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  733 FGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQ 812
Cdd:cd14902   390 FGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  813 ATDQTLVDKfednlrckyFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIP---- 888
Cdd:cd14902   470 GSNQALSTK---------FYRYHGGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADEnrds 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  889 LTKTGNLAQTRARITVASSSlpphfsagkakvdtlevirhpeettnmkrqtVASYFRYSLMDLLSKMVVGQPHFVRCIKP 968
Cdd:cd14902   541 PGADNGAAGRRRYSMLRAPS-------------------------------VSAQFKSQLDRLIVQIGRTEAHYVRCLKP 589
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  969 NDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRY 1015
Cdd:cd14902   590 NEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELF 636
PTZ00014 PTZ00014
myosin-A; Provisional
361-1108 1.35e-136

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 439.08  E-value: 1.35e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  361 EVLDedtiihQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASN-PPHIFASADAAYQCMVTLSKDQ 439
Cdd:PTZ00014  111 CVLD------FLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQ 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  440 CIVISGESGSGKTESAHLIVQH-LTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGA 518
Cdd:PTZ00014  185 TIIVSGESGAGKTEATKQIMRYfASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  519 RISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrqFEAIQHCF 598
Cdd:PTZ00014  265 SIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMK-EKYKLKSLEEYKYINPKCLDVPGIDDVKD-----FEEVMESF 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  599 RIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEV--PNAEALQNAASVLCISPEELQEALTSHCVVTRGETI 676
Cdd:PTZ00014  339 DSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIsdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKI 418
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  677 IRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDenicsagGGMNV--GILDIFGFENFQRNSFEQLCINIANEQ 754
Cdd:PTZ00014  419 EGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP-------GGFKVfiGMLDIFGFEVFKNNSLEQLFINITNEM 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  755 IQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRP 834
Cdd:PTZ00014  492 LQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKP 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 --KGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAqtraritvassslpph 912
Cdd:PTZ00014  572 akVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA---------------- 635
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 fsagkakvdtlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGIL 992
Cdd:PTZ00014  636 -----------------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSIL 692
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  993 ETVSIRRQGYSHRILFEEFVKRYYYLAF-TAHQTPLASKESCVAILEKSRL--DHWVLGKTKVFLKYYHVEQLNLLLREV 1069
Cdd:PTZ00014  693 EALQLRQLGFSYRRTFAEFLSQFKYLDLaVSNDSSLDPKEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELTQIQREK 772
                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 578803747 1070 IGRVVVLQAYTKGWLGARRYKRVREKREKGAIAIQSAWR 1108
Cdd:PTZ00014  773 LAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
367-1055 3.38e-136

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 433.23  E-value: 3.38e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14927     2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLT--------------FLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT 512
Cdd:cd14927    82 SGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  513 GVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGlhHQKKLSDFRLPEEKPPRYIADETGrvmhdITSKESYR--RQ 590
Cdd:cd14927   162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG--KKPELQDMLLVSMNPYDYHFCSQG-----VTTVDNMDdgEE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  591 FEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVV 670
Cdd:cd14927   235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKF---KQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  671 TRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQpdeniCSAGGGMNVGILDIFGFENFQRNSFEQLCINI 750
Cdd:cd14927   312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-----TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  751 ANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCK 829
Cdd:cd14927   387 TNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGlDLQACIDL-IEKPLGILSILEEECMFPKASDASFKAKLYDNHLGK 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  830 Y--FWRP-----KGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgNLaqtrari 902
Cdd:cd14927   466 SpnFQKPrpdkkRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYE-------NY------- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  903 tVASSSLPPHFSAGKAKvdtlevirhpeETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERV 982
Cdd:cd14927   532 -VGSDSTEDPKSGVKEK-----------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLV 599
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  983 LAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14927   600 LHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAipDDKFVDSRKATEKLLGSLDIDHtqYQFGHTKVFFK 676
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
367-1055 7.47e-136

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 432.10  E-value: 7.47e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14911     2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQT-----------------LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMF 509
Cdd:cd14911    82 SGAGKTENTKKVIQFLAYVAASKPKGsgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  510 TPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLpeEKPPRYIADETGrvMHDITSKESYrR 589
Cdd:cd14911   162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQR-EKFIL--DDVKSYAFLSNG--SLPVPGVDDY-A 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  590 QFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEA-LTSHC 668
Cdd:cd14911   236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF---RQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  669 VVTRgETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCI 748
Cdd:cd14911   313 KVGR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKR----QGASFIGILDMAGFEIFELNSFEQLCI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  749 NIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKF--EDN 825
Cdd:cd14911   388 NYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDL-IDKPGGIMALLDEECWFPKATDKTFVDKLvsAHS 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  826 LRCKYFWRP-KGVElCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtRARITV 904
Cdd:cd14911   467 MHPKFMKTDfRGVA-DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWK------------DAEIVG 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  905 AssslpphfsAGKAKVDTLEVIRhpeeTTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLA 984
Cdd:cd14911   534 M---------AQQALTDTQFGAR----TRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLD 600
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  985 QLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLafTAHQTP---LASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14911   601 QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL--TPNVIPkgfMDGKKACEKMIQALELDSnlYRVGQSKIFFR 674
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
366-1044 2.13e-135

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276865  Cd Length: 627  Bit Score: 429.34  E-value: 2.13e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLS---------IYSPQFSRLYHGVK---RASNPPHIFASADAAYQCMV 433
Cdd:cd14900     1 TTILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmaKYLLSFEARSSSTRnkgSDPMPPHIYQVAGEAYKAMM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  434 ----TLSKDQCIVISGESGSGKTESAHLIVQHLTFLGKANN----------QTLREKILQVNSLVEAFGNSCTAINDNSS 499
Cdd:cd14900    81 lglnGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLaasvsmgkstSGIAAKVLQTNILLESFGNARTLRNDNSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  500 RFGKYLEMMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGlhhqkklsdfrlpeekppryiADETGRVMH 579
Cdd:cd14900   161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG---------------------ASEAARKRD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  580 ditskeSYRRQFEAIQhcfrIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQH--QTDKSEV-PNA-EALQNAASVLCI 655
Cdd:cd14900   220 ------MYRRVMDAMD----IIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLaPSSiWSRDAAATLLSV 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  656 SPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGMNVGILDIFGF 735
Cdd:cd14900   290 DATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHFIGILDIFGF 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  736 ENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATD 815
Cdd:cd14900   370 EVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSD 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  816 QTLVDKF----EDNLR--CKYFWRPKGVelcFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSenklLQqlfsipl 889
Cdd:cd14900   450 TTLASKLyracGSHPRfsASRIQRARGL---FTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG----LQ------- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  890 tktgnlaqtraritvassslpphfsagkakvdtlevirhpeettnmkrqtvasyFRYSLMDLLSKMVVGQPHFVRCIKPN 969
Cdd:cd14900   516 ------------------------------------------------------FKEQLTTLLETLQQTNPHYVRCLKPN 541
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  970 DDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTahQTPLASKESCVAILEkSRLDH 1044
Cdd:cd14900   542 DLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARA--KNRLLAKKQGTSLPD-TDSDH 613
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
367-1055 5.47e-134

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 427.52  E-value: 5.47e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14932     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKA------------NNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGV 514
Cdd:cd14932    82 SGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  515 VMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLhHQKKLSDFRLPEEKPPRYIADetGRV-MHDITSKESYRRQFEA 593
Cdd:cd14932   162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGA-GDKLRSELCLEDYSKYRFLSN--GNVtIPGQQDKELFAETMEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  594 iqhcFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRG 673
Cdd:cd14932   239 ----FRIMSIPEEEQTGLLKVVSAVLQLGNMSF---KKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  674 ETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCINIANE 753
Cdd:cd14932   312 DYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKR----QGASFIGILDIAGFEIFELNSFEQLCINYTNE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  754 QIQYYFNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMFLQK--PLGLLALLDEESRFPQATDQTLVDKFEDNLRCK- 829
Cdd:cd14932   388 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNp 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  830 YFWRPKGV--ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLlqqlfsipltkTGNLAQTRARITvass 907
Cdd:cd14932   468 KFQKPKKLkdDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKF-----------VSELWKDVDRIV---- 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  908 slpphfsaGKAKVDTL-EVIRHPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQL 986
Cdd:cd14932   533 --------GLDKVAGMgESLHGAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQL 604
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  987 RSTGILETVSIRRQGYSHRILFEEFVKRYYYLafTAHQTP---LASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14932   605 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNAIPkgfMDGKQACVLMVKALELDPnlYRIGQSKVFFR 676
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
368-1055 8.37e-133

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 424.08  E-value: 8.37e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14913     3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANN----------QTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMG 517
Cdd:cd14913    83 GAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  518 ARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRVMhdITSKESyRRQFEAIQHC 597
Cdd:cd14913   163 ADIETYLLEKSRVTFQLKAERSYHIFYQILS--NKKPELIELLLITTNPYDYPFISQGEIL--VASIDD-AEELLATDSA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  598 FRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETII 677
Cdd:cd14913   238 IDILGFTPEEKSGLYKLTGAVMHYGNMKF---KQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  678 RANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQ---PDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIANEQ 754
Cdd:cd14913   315 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtklPRQHF--------IGVLDIAGFEIFEYNSLEQLCINFTNEK 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  755 IQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKYFW 832
Cdd:cd14913   387 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  833 RPKGV----ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtrariTVASSS 908
Cdd:cd14913   467 KPKVVkgraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYA----------------TFATAD 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  909 LPPHFSAGKAKVDTlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRS 988
Cdd:cd14913   531 ADSGKKKVAKKKGS-------------SFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRC 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  989 TGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14913   598 NGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAipEGQFIDSKKACEKLLASIDIDHtqYKFGHTKVFFK 668
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
367-1055 6.28e-132

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 421.81  E-value: 6.28e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14919     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLG-----KANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARIS 521
Cdd:cd14919    82 SGAGKTENTKKVIQYLAHVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  522 EYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADEtgrvmHDITSKESYRRQFEAIQHCFRII 601
Cdd:cd14919   162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK-TDLLLEPYNKYRFLSNG-----HVTIPGQQDKDMFQETMEAMRIM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  602 GFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANT 681
Cdd:cd14919   236 GIPEEEQMGLLRVISGVLQLGNIVF---KKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  682 VDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQ 761
Cdd:cd14919   313 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKR----QGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  762 HVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMfLQKPL---GLLALLDEESRFPQATDQTLVDK-FEDNLRCKYFWRPKG 836
Cdd:cd14919   389 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDL-IEKPAgppGILALLDEECWFPKATDKSFVEKvVQEQGTHPKFQKPKQ 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  837 V--ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFS-----IPLTKTGNLAQTraritvassSL 909
Cdd:cd14919   468 LkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriIGLDQVAGMSET---------AL 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  910 PPHFSAGKAKVdtlevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRST 989
Cdd:cd14919   539 PGAFKTRKGMF-----------------RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCN 601
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  990 GILETVSIRRQGYSHRILFEEFVKRYYYLafTAHQTP---LASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14919   602 GVLEGIRICRQGFPNRVVFQEFRQRYEIL--TPNSIPkgfMDGKQACVLMIKALELDSnlYRIGQSKVFFR 670
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
367-1055 2.14e-131

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 421.28  E-value: 2.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQfsrLYHGVKRASN--PPHIFASADAAYQCMVTL-------S 436
Cdd:cd14895     2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYDLH---KYREEMPGWTalPPHVFSIAEGAYRSLRRRlhepgasK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  437 KDQCIVISGESGSGKTESAHLIVQHLTFLGKANNQTLREK---------ILQVNSLVEAFGNSCTAINDNSSRFGKYLEM 507
Cdd:cd14895    79 KNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraisgseLLSANPILESFGNARTLRNDNSSRFGKFVRM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  508 MFTP-----TGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLsDFRLPEEKPP--RYIADETGRVMHD 580
Cdd:cd14895   159 FFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKL-ELQLELLSAQefQYISGGQCYQRND 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  581 ITSKEsyrRQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDK---------------SEVPNAEA 645
Cdd:cd14895   238 GVRDD---KQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDngaasapcrlasaspSSLTVQQH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  646 LQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGM 725
Cdd:cd14895   315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNPNKAA 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  726 N------VGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLG 799
Cdd:cd14895   395 NkdttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSG 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  800 LLALLDEESRFPQATDQTLVDKFEDNLRCKYFW---RPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTS 876
Cdd:cd14895   475 IFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFsasRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKT 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  877 ENKLLQQLFS-IPLTKTGNLAQTRARITVASSSLPphfSAGkakvdtlevirhpeettnmkrqtVASYFRYSLMDLLSKM 955
Cdd:cd14895   555 SDAHLRELFEfFKASESAELSLGQPKLRRRSSVLS---SVG-----------------------IGSQFKQQLASLLDVV 608
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  956 VVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAftahQTPLASKESCVA 1035
Cdd:cd14895   609 QQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV----AAKNASDATASA 684
                         730       740
                  ....*....|....*....|
gi 578803747 1036 ILEKSRLDHWVLGKTKVFLK 1055
Cdd:cd14895   685 LIETLKVDHAELGKTRVFLR 704
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
368-1055 3.63e-131

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 418.68  E-value: 3.63e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYA--DLLIYTYVGDILIALNPFQNLSiySPQFSrLYhgVKRASN--PPHIFASADAAYQCMVTLSKDQC--- 440
Cdd:cd14891     3 ILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPDKS-DY--INTPLDpcPPHPYAIAEMAYQQMCLGSGRMQnqs 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  441 IVISGESGSGKTESAHLIVQHLT------------------FLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFG 502
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLTtravggkkasgqdieqssKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  503 KYLEMMFTPTGV-VMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGlHHQKKLSDFRLPEEKPPRYIADETGRVMHDI 581
Cdd:cd14891   158 KFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAG-ASAELLKELLLLSPEDFIYLNQSGCVSDDNI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  582 TSKEsyrrQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEF-AAISSQHQTDKSEVPNAEALQNAASVLCISPEEL 660
Cdd:cd14891   237 DDAA----NFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdEEDTSEGEAEIASESDKEALATAAELLGVDEEAL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  661 QEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQR 740
Cdd:cd14891   313 EKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPY-----IGVLDIFGFESFET 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  741 -NSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDqtlv 819
Cdd:cd14891   388 kNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSD---- 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  820 DKFEDNL-----RCKYFWRP--KGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSeNKLLQQLfsipltkt 892
Cdd:cd14891   464 AKLNETLhkthkRHPCFPRPhpKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKFSDQM-------- 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  893 gnlaqtraritvassslpphfsagKAKVDTLEVIRhpeettnmkrqtvasyfryslmdllskmvvgqPHFVRCIKPNDDR 972
Cdd:cd14891   535 ------------------------QELVDTLEATR--------------------------------CNFIRCIKPNAAM 558
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  973 EALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCV--AILEKSR--LDHWVLG 1048
Cdd:cd14891   559 KVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLtqAILWAFRvpSDAYRLG 638

                  ....*..
gi 578803747 1049 KTKVFLK 1055
Cdd:cd14891   639 RTRVFFR 645
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
367-1055 3.98e-131

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 419.42  E-value: 3.98e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14921     2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFL-----GKANNQT---LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGA 518
Cdd:cd14921    82 SGAGKTENTKKVIQYLAVVasshkGKKDTSItgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  519 RISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLpeEKPPRYIADETGRV-MHDITSKESYRRQFEAIQhc 597
Cdd:cd14921   162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMR-SDLLL--EGFNNYTFLSNGFVpIPAAQDDEMFQETLEAMS-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  598 frIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETII 677
Cdd:cd14921   237 --IMGFSEEEQLSILKVVSSVLQLGNIVF---KKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  678 RANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQY 757
Cdd:cd14921   312 KAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHR----QGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  758 YFNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMFLQ--KPLGLLALLDEESRFPQATDQTLVDK-FEDNLRCKYFWR 833
Cdd:cd14921   388 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKlCTEQGNHPKFQK 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  834 PKGV--ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSiPLTKTGNLAQTrARITvaSSSLPp 911
Cdd:cd14921   468 PKQLkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQM-AKMT--ESSLP- 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  912 hfSAGKAKvdtlevirhpeetTNMKRqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGI 991
Cdd:cd14921   543 --SASKTK-------------KGMFR-TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGV 606
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  992 LETVSIRRQGYSHRILFEEFVKRYYYLAftAHQTP---LASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14921   607 LEGIRICRQGFPNRIVFQEFRQRYEILA--ANAIPkgfMDGKQACILMIKALELDPnlYRIGQSKIFFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
367-1055 4.10e-131

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 419.24  E-value: 4.10e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14909     2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQ--------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGA 518
Cdd:cd14909    82 SGAGKTENTKKVIAYFATVGASKKTdeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  519 RISEYLLEKSRVIKQAAREKNFHIFYYIYAGlhHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAIQHC 597
Cdd:cd14909   162 DIETYLLEKARVISQQSLERSYHIFYQIMSG--SVPGVKEMCLLSDNIYDYYIVSQGKVtVPNVDDGE----EFSLTDQA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  598 FRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQtdkSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETII 677
Cdd:cd14909   236 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQ---AEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  678 RANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQY 757
Cdd:cd14909   313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF-----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  758 YFNQHVFALEQMEYQNEGIDAVPVEY-EDNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKY--FWRP 834
Cdd:cd14909   388 FFNHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDL-IEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSapFQKP 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 K----GVELC-FGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRaritvasssl 909
Cdd:cd14909   467 KppkpGQQAAhFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAK---------- 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  910 pphfsAGKAKvdtlevirhpeetTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRST 989
Cdd:cd14909   537 -----GGRGK-------------KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCN 598
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  990 GILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLD--HWVLGKTKVFLK 1055
Cdd:cd14909   599 GVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDPKKAAEIILESIALDpdQYRLGHTKVFFR 666
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
368-1055 1.29e-130

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 418.54  E-value: 1.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYH--GVKRASN-------PPHIFASADAAY-QCMVTLSK 437
Cdd:cd14908     3 ILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQGiespqalGPHVFAIADRSYrQMMSEIRA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  438 DQCIVISGESGSGKTESAHLIVQHLTFLGKANNQ-----------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLE 506
Cdd:cd14908    83 SQSILISGESGAGKTESTKIVMLYLTTLGNGEEGapnegeelgklSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  507 MMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGL----HHQKKLSD-----FRLPEEKppRYIADETGRV 577
Cdd:cd14908   163 LGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGdeeeHEKYEFHDgitggLQLPNEF--HYTGQGGAPD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  578 MHDITSKESYRRQFEAIqhcfRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISP 657
Cdd:cd14908   241 LREFTDEDGLVYTLKAM----RTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  658 EELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL--QPDENICSAgggmnVGILDIFGF 735
Cdd:cd14908   317 DKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-----VGVLDIFGF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  736 ENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQ-AT 814
Cdd:cd14908   392 ECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGIrGS 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  815 D----QTLVDKF--------EDNLRCKYFWRPKGvELCFGIQHYAGKVLYDA-SGVLEKNRDTLPadvvvvlRTSEnkll 881
Cdd:cd14908   472 DanyaSRLYETYlpeknqthSENTRFEATSIQKT-KLIFAVRHFAGQVQYTVeTTFCEKNKDEIP-------LTAD---- 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  882 qQLFsipltktgnlaqtraritvassslpphfsagkakvdtlevirhpEETTNMKRQTvasyfrYSLMDLLSKMvvgQPH 961
Cdd:cd14908   540 -SLF--------------------------------------------ESGQQFKAQL------HSLIEMIEDT---DPH 565
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  962 FVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQ------------TPLAS 1029
Cdd:cd14908   566 YIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLIPEvvlswsmerldpQKLCV 645
                         730       740       750
                  ....*....|....*....|....*....|....*..
gi 578803747 1030 KESCVAILEKSRLDHWV-----------LGKTKVFLK 1055
Cdd:cd14908   646 KKMCKDLVKGVLSPAMVsmknipedtmqLGKSKVFMR 682
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
368-1015 1.05e-127

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 411.68  E-value: 1.05e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHGVKR-ASNPPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14906     3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKA----------NNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT-GV 514
Cdd:cd14906    83 ESGSGKTEASKTILQYLINTSSSnqqqnnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  515 VMGARISEYLLEKSRVIKQAAREK-NFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADETGRVmhDITSKESYRRQ--- 590
Cdd:cd14906   163 IDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVI--SSFKSQSSNKNsnh 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  591 ---------FEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQ 661
Cdd:cd14906   241 nnktesiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  662 EALTSHCVVT--RGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGMN------VGILDIF 733
Cdd:cd14906   321 QALLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAGGSNkknnlfIGVLDIF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  734 GFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQA 813
Cdd:cd14906   401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  814 TDQTLVDKFEDNLRC--KYFWRPKGvELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTK 891
Cdd:cd14906   481 SEQSLLEKYNKQYHNtnQYYQRTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  892 TGNlaqtraritvassslpphfsagkakvdtlevirhpeeTTNMKRQ--TVASYFRYSLMDLLSKMVVGQPHFVRCIKPN 969
Cdd:cd14906   560 TTN-------------------------------------TTKKQTQsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPN 602
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  970 DDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRY 1015
Cdd:cd14906   603 QTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRY 648
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
368-1055 4.88e-127

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 408.74  E-value: 4.88e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14912     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQ------------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVV 515
Cdd:cd14912    83 GAGKTVNTKRVIQYFATIAVTGEKkkeeitsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  516 MGARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAI 594
Cdd:cd14912   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITS--NKKPELIEMLLITTNPYDYPFVSQGEIsVASIDDQE----ELMAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  595 QHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGE 674
Cdd:cd14912   237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKF---KQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  675 TIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIA 751
Cdd:cd14912   314 YVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLdtkQPRQYF--------IGVLDIAGFEIFDFNSLEQLCINFT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  752 NEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCK 829
Cdd:cd14912   386 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSA 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  830 YFWRPKGV----ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARitva 905
Cdd:cd14912   466 NFQKPKVVkgkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAK---- 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  906 ssslpphfSAGKAKVDTLevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQ 985
Cdd:cd14912   542 --------KGGKKKGSSF--------------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQ 599
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  986 LRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14912   600 LRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAipEGQFIDSKKASEKLLASIDIDHtqYKFGHTKVFFK 673
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
372-1055 2.72e-126

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 405.53  E-value: 2.72e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  372 LQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASN-PPHIFASADAAYQCMVTLSKDQCIVISGESGSG 450
Cdd:cd14876     7 LKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLTKlPPHVFYTARRALENLHGVNKSQTIIVSGESGAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  451 KTESAHLIVQHLTFlGKANNQTLR--EKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLEKS 528
Cdd:cd14876    87 KTEATKQIMRYFAS-AKSGNMDLRiqTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  529 RVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIadeTGRVmHDITSKESyRRQFEAIQHCFRIIGFTDKEV 608
Cdd:cd14876   166 RIVTQDDNERSYHIFYQLLKGADSEMK-SKYHLLGLKEYKFL---NPKC-LDVPGIDD-VADFEEVLESLKSMGLTEEQI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  609 HSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNA--EALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAA 686
Cdd:cd14876   240 DTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNEslEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  687 DVRDAMSKALYGRLFSWIVNRINTLLQPDenicsagGGMNV--GILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVF 764
Cdd:cd14876   320 MLKLSLAKAMYDKLFLWIIRNLNSTIEPP-------GGFKNfmGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  765 ALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPKGV--ELCFG 842
Cdd:cd14876   393 ERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVdsNINFI 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  843 IQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAqtraritvassslpphfsagkakvdt 922
Cdd:cd14876   473 VVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIA-------------------------- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  923 levirhpeettnmKRQTVASYFRY---SLMDLLSKMvvgQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRR 999
Cdd:cd14876   527 -------------KGSLIGSQFLKqleSLMGLINST---EPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQ 590
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747 1000 QGYSHRILFEEFVKRYYYLAFTAHQTP-LASKESCVAILEKSRL--DHWVLGKTKVFLK 1055
Cdd:cd14876   591 LGYSYRRPFEEFLYQFKFLDLGIANDKsLDPKVAALKLLESSGLseDEYAIGKTMVFLK 649
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
367-1055 1.56e-125

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 404.45  E-value: 1.56e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd15896     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQT------------LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGV 514
Cdd:cd15896    82 SGAGKTENTKKVIQYLAHVASSHKTKkdqnslalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  515 VMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADetGRVMhdiTSKESYRRQFEAI 594
Cdd:cd15896   162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLR-SELLLENYNNYRFLSN--GNVT---IPGQQDKDLFTET 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  595 QHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGE 674
Cdd:cd15896   236 MEAFRIMGIPEDEQIGMLKVVASVLQLGNMSF---KKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  675 TIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQ 754
Cdd:cd15896   313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKR----QGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  755 IQYYFNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMFLQ--KPLGLLALLDEESRFPQATDQTLVDK-FEDNLRCKY 830
Cdd:cd15896   389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKvLQEQGTHPK 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  831 FWRPKGV--ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFS-----IPLTKTGNLaqtrarit 903
Cdd:cd15896   469 FFKPKKLkdEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvdriVGLDKVSGM-------- 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  904 vasSSLPPHFSAGKAKVdtlevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVL 983
Cdd:cd15896   541 ---SEMPGAFKTRKGMF-----------------RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 600
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  984 AQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLafTAHQTP---LASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd15896   601 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNAIPkgfMDGKQACVLMIKSLELDPnlYRIGQSKVFFR 675
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
368-1055 1.94e-124

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 401.40  E-value: 1.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14917     3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQ----------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMG 517
Cdd:cd14917    83 GAGKTVNTKRVIQYFAVIAAIGDRskkdqtpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  518 ARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGR-VMHDITSKEsyrrQFEAIQH 596
Cdd:cd14917   163 ADIETYLLEKSRVIFQLKAERDYHIFYQILS--NKKPELLDMLLITNNPYDYAFISQGEtTVASIDDAE----ELMATDN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  597 CFRIIGFTDKEVHSVYRILAGILNIGNIEFAAissQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETI 676
Cdd:cd14917   237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQ---KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  677 IRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIANE 753
Cdd:cd14917   314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLetkQPRQYF--------IGVLDIAGFEIFDFNSFEQLCINFTNE 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  754 QIQYYFNQHVFALEQMEYQNEGIDAVPVEY-EDNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKY 830
Cdd:cd14917   386 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgKSNN 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  831 FWRPKGV----ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtrariTVAS 906
Cdd:cd14917   465 FQKPRNIkgkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFA----------------NYAG 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  907 SSLPPHFSAGKAKVDTlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQL 986
Cdd:cd14917   529 ADAPIEKGKGKAKKGS-------------SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQL 595
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  987 RSTGILETVSIRRQGYSHRILFEEFVKRYYYL--AFTAHQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14917   596 RCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAAIPEGQFIDSRKGAEKLLSSLDIDHnqYKFGHTKVFFK 668
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
367-1055 1.08e-123

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 399.47  E-value: 1.08e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14930     2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANN--------QTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGA 518
Cdd:cd14930    82 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  519 RISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGrvmhdiTSKESYRRQFEAIQHCF 598
Cdd:cd14930   162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPS------SSPGQERELFQETLESL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  599 RIIGFTDKEVHSVYRILAGILNIGNIefaAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIR 678
Cdd:cd14930   235 RVLGFSHEEITSMLRMVSAVLQFGNI---VLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  679 ANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYY 758
Cdd:cd14930   312 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR----QGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  759 FNQHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMFLQ--KPLGLLALLDEESRFPQATDQTLVDKF-EDNLRCKYFWRP 834
Cdd:cd14930   388 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVaQEQGGHPKFQRP 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 KGV--ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGnLAQTraritvasSSLPPH 912
Cdd:cd14930   468 RHLrdQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVG-LEQV--------SSLGDG 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 FSAGKAKVDTLevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGIL 992
Cdd:cd14930   539 PPGGRPRRGMF--------------RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVL 604
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  993 ETVSIRRQGYSHRILFEEFVKRYYYLafTAHQTP---LASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14930   605 EGIRICRQGFPNRILFQEFRQRYEIL--TPNAIPkgfMDGKQACEKMIQALELDPnlYRVGQSKIFFR 670
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
368-1055 6.15e-123

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 397.18  E-value: 6.15e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14918     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQ----------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMG 517
Cdd:cd14918    83 GAGKTVNTKRVIQYFATIAVTGEKkkeesgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  518 ARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAIQH 596
Cdd:cd14918   163 ADIETYLLEKSRVTFQLKAERSYHIFYQITS--NKKPDLIEMLLITTNPYDYAFVSQGEItVPSIDDQE----ELMATDS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  597 CFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETI 676
Cdd:cd14918   237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKF---KQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  677 IRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIANE 753
Cdd:cd14918   314 TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLdtkQPRQYF--------IGVLDIAGFEIFDFNSLEQLCINFTNE 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  754 QIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKYF 831
Cdd:cd14918   386 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlgKSANF 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  832 WRPKGV----ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtrariTVASS 907
Cdd:cd14918   466 QKPKVVkgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS----------------TYASA 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  908 SLPPHFSAGKAKVDTlevirhpeettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLR 987
Cdd:cd14918   530 EADSGAKKGAKKKGS-------------SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLR 596
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  988 STGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14918   597 CNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAipEGQFIDSKKASEKLLASIDIDHtqYKFGHTKVFFK 668
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
367-1055 4.36e-122

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 394.78  E-value: 4.36e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGE 446
Cdd:cd14934     2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQ------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARI 520
Cdd:cd14934    82 SGAGKTENTKKVIQYFANIGGTGKQssdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  521 SEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADETgRVMHDITSKEsyrrQFEAIQHCFRI 600
Cdd:cd14934   162 ESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGV-TVVDNMDDGE----ELQITDVAFDV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  601 IGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDkseVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRAN 680
Cdd:cd14934   237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAE---VDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  681 TVDRAADVRDAMSKALYGRLFSWIVNRINTLLQpdeniCSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFN 760
Cdd:cd14934   314 NMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-----TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  761 QHVFALEQMEYQNEGIDAVPVEYE-DNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKYFWRP--- 834
Cdd:cd14934   389 HHMFVLEQEEYKREGIEWVFIDFGlDLQACIDL-LEKPMGIFSILEEQCVFPKATDATFKAALYDNHlgKSSNFLKPkgg 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  835 --KGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRAritvasSSLpph 912
Cdd:cd14934   468 kgKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKKQKRG------SSF--- 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 fsagkakvdtlevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGIL 992
Cdd:cd14934   539 -------------------------MTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVL 593
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  993 ETVSIRRQGYSHRILFEEFVKRYYYL-AFTAHQTPLASKESCVAILEKSRLD--HWVLGKTKVFLK 1055
Cdd:cd14934   594 EGIRICRKGFPNRLQYPEFKQRYQVLnPNVIPQGFVDNKKASELLLGSIDLDvnEYKIGHTKVFFR 659
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
368-1055 4.44e-121

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 392.56  E-value: 4.44e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14910     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQ------------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVV 515
Cdd:cd14910    83 GAGKTVNTKRVIQYFATIAVTGEKkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  516 MGARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAI 594
Cdd:cd14910   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMS--NKKPDLIEMLLITTNPYDYAFVSQGEItVPSIDDQE----ELMAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  595 QHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGE 674
Cdd:cd14910   237 DSAIEILGFTSDERVSIYKLTGAVMHYGNMKF---KQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  675 TIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIA 751
Cdd:cd14910   314 YVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLdtkQPRQYF--------IGVLDIAGFEIFDFNSLEQLCINFT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  752 NEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDK-FEDNL-RCK 829
Cdd:cd14910   386 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYEQHLgKSN 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  830 YFWRPK----GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraRITVA 905
Cdd:cd14910   466 NFQKPKpakgKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFS--------------GAAAA 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  906 SSSLPPHFSAGKAKVDTLevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQ 985
Cdd:cd14910   532 EAEEGGGKKGGKKKGSSF--------------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQ 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  986 LRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14910   598 LRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAipEGQFIDSKKASEKLLGSIDIDHtqYKFGHTKVFFK 671
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
367-1055 1.03e-120

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 391.10  E-value: 1.03e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADL-LIYTYVGDILIALNPFQNLSIYSPQFSRLYHGV-KRASNPPHIFASADAAY-QCMVTLSKDQCIVI 443
Cdd:cd14875     2 TLLHCIKERFEKLhQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFnAIFVQGLGNQSVVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  444 SGESGSGKTESAHLIVQHLTFL-----GKANNQTLREKILQ----VNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPT-G 513
Cdd:cd14875    82 SGESGSGKTENAKMLIAYLGQLsymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTsG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  514 VVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGL--HHQKKLSDFRLPEEKP--------PRYIADetGRVMHDitS 583
Cdd:cd14875   162 VMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLspEEKKELGGLKTAQDYKclnggntfVRRGVD--GKTLDD--A 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  584 KEsyrrqFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAissqHQTDKSEVPNAEALQNAASVLCISPEELQEa 663
Cdd:cd14875   238 HE-----FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES----DQNDKAQIADETPFLTACRLLQLDPAKLRE- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  664 ltshCVVTRGET---IIRANTVDrAADVRDAMSKALYGRLFSWIVNRINTLLQPDENiCSagGGMNVGILDIFGFENFQR 740
Cdd:cd14875   308 ----CFLVKSKTslvTILANKTE-AEGFRNAFCKAIYVGLFDRLVEFVNASITPQGD-CS--GCKYIGLLDIFGFENFTR 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  741 NSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATdqtlVD 820
Cdd:cd14875   380 NSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGT----TE 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  821 KFEDNL------RCKYFWRPKG-VELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktg 893
Cdd:cd14875   456 RFTTNLwdqwanKSPYFVLPKStIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS------- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  894 nlaqtraritvassslpphfsagkakvdtlevirhPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDRE 973
Cdd:cd14875   529 -----------------------------------TEKGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEAS 573
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  974 ALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVkRYYYLAFTAHQTPLAS----KESCVAILEK-SRLDHW--- 1045
Cdd:cd14875   574 PSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFC-RYFYLIMPRSTASLFKqekySEAAKDFLAYyQRLYGWakp 652
                         730
                  ....*....|..
gi 578803747 1046 --VLGKTKVFLK 1055
Cdd:cd14875   653 nyAVGKTKVFLR 664
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
368-1055 2.01e-118

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 385.18  E-value: 2.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14916     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFL-----------GKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVM 516
Cdd:cd14916    83 GAGKTVNTKRVIQYFASIaaigdrskkenPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  517 GARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAIQ 595
Cdd:cd14916   163 SADIETYLLEKSRVIFQLKAERNYHIFYQILS--NKKPELLDMLLVTNNPYDYAFVSQGEVsVASIDDSE----ELLATD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  596 HCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGET 675
Cdd:cd14916   237 SAFDVLGFTAEEKAGVYKLTGAIMHYGNMKF---KQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  676 IIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIAN 752
Cdd:cd14916   314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLetkQPRQYF--------IGVLDIAGFEIFDFNSFEQLCINFTN 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  753 EQIQYYFNQHVFALEQMEYQNEGIDAVPVEY-EDNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCK 829
Cdd:cd14916   386 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlgKSN 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  830 YFWRPKGV----ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLT-KTGNLAQTRaritv 904
Cdd:cd14916   465 NFQKPRNVkgkqEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASaDTGDSGKGK----- 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  905 assslpphfsAGKAKVDTLevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLA 984
Cdd:cd14916   540 ----------GGKKKGSSF--------------QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMH 595
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  985 QLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14916   596 QLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipEGQFIDSRKGAEKLLGSLDIDHnqYKFGHTKVFFK 670
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
368-1055 3.38e-118

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 384.42  E-value: 3.38e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14923     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQ-----------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVM 516
Cdd:cd14923    83 GAGKTVNTKRVIQYFATIAVTGDKkkeqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  517 GARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAIQ 595
Cdd:cd14923   163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMS--NKKPELIDLLLISTNPFDFPFVSQGEVtVASIDDSE----ELLATD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  596 HCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGET 675
Cdd:cd14923   237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKF---KQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  676 IIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIAN 752
Cdd:cd14923   314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLdtkQPRQYF--------IGVLDIAGFEIFDFNSLEQLCINFTN 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  753 EQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKY 830
Cdd:cd14923   386 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNN 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  831 FWRPKGV----ELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgNLAQTRARITVAS 906
Cdd:cd14923   466 FQKPKPAkgkaEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFS-------NYAGAEAGDSGGS 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  907 SslpphfSAGKAKVDTLevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQL 986
Cdd:cd14923   539 K------KGGKKKGSSF--------------QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQL 598
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  987 RSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14923   599 RCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAipEGQFIDSKNASEKLLNSIDVDReqYRFGHTKVFFK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
368-1055 4.78e-118

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 384.08  E-value: 4.78e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd14915     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFLGKANNQ------------TLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVV 515
Cdd:cd14915    83 GAGKTVNTKRVIQYFATIAVTGEKkkeeaasgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  516 MGARISEYLLEKSRVIKQAAREKNFHIFYYIYAglHHQKKLSDFRLPEEKPPRYIADETGRV-MHDITSKEsyrrQFEAI 594
Cdd:cd14915   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMS--NKKPELIEMLLITTNPYDFAFVSQGEItVPSIDDQE----ELMAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  595 QHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaaiSSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGE 674
Cdd:cd14915   237 DSAVDILGFSADEKVAIYKLTGAVMHYGNMKF---KQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  675 TIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL---QPDENIcsagggmnVGILDIFGFENFQRNSFEQLCINIA 751
Cdd:cd14915   314 YVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLdtkQPRQYF--------IGVLDIAGFEIFDFNSLEQLCINFT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  752 NEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDK-FEDNL-RCK 829
Cdd:cd14915   386 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYEQHLgKSN 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  830 YFWRPK----GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltkTGNLAQTRAritva 905
Cdd:cd14915   466 NFQKPKpakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS-----GGQTAEAEG----- 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  906 ssslPPHFSAGKAKVDTLevirhpeettnmkrQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQ 985
Cdd:cd14915   536 ----GGGKKGGKKKGSSF--------------QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQ 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  986 LRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTA--HQTPLASKESCVAILEKSRLDH--WVLGKTKVFLK 1055
Cdd:cd14915   598 LRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAipEGQFIDSKKASEKLLGSIDIDHtqYKFGHTKVFFK 671
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
365-1056 1.42e-117

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 381.90  E-value: 1.42e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  365 EDTIIHQLQKRYADLLIYTYVGD-ILIALNPFQNLSIYSPQFSRLY-------HGVKRASNPPHIFASADAAYQCMVTLS 436
Cdd:cd14879     3 DDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  437 KDQCIVISGESGSGKTESAHLIVQHLTFLGKANNQTLR--EKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGV 514
Cdd:cd14879    83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTKlsSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  515 VMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLpEEKppryiADETGRvmhdiTSKESYRRQ---- 590
Cdd:cd14879   163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEER-QHLGL-DDP-----SDYALL-----ASYGCHPLPlgpg 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  591 ------FEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFaAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEAL 664
Cdd:cd14879   231 sddaegFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-TYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  665 TSHCVVTRGE--TIIRanTVDRAADVRDAMSKALYGRLFSWIVNRINT-LLQPDENICSagggmNVGILDIFGFENF--- 738
Cdd:cd14879   310 TYKTKLVRKElcTVFL--DPEGAAAQRDELARTLYSLLFAWVVETINQkLCAPEDDFAT-----FISLLDFPGFQNRsst 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  739 QRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEE-SRFPQATDQT 817
Cdd:cd14879   383 GGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQtRRMPKKTDEQ 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  818 LVD----KFEDNLRCKYFWRPKGVEL--CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTsenkllqqlfsipltk 891
Cdd:cd14879   463 MLEalrkRFGNHSSFIAVGNFATRSGsaSFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRG---------------- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  892 tgnlaqtraritvassslpphfsagkakvdtlevirhpeettnmkrqtvASYFRYSLMDLLSKMVVGQPHFVRCIKPNDD 971
Cdd:cd14879   527 -------------------------------------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDS 557
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  972 REALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPlaSKESCVAILEKSRLDhWVLGKTK 1051
Cdd:cd14879   558 QLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAER--IRQCARANGWWEGRD-YVLGNTK 634

                  ....*
gi 578803747 1052 VFLKY 1056
Cdd:cd14879   635 VFLSY 639
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
367-1054 5.66e-117

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 380.74  E-value: 5.66e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHGvkrASNP----PHIFASADAAYQCMVTLSK--DQ 439
Cdd:cd14880     2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHA---APQPqklkPHIFTVGEQTYRNVKSLIEpvNQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  440 CIVISGESGSGKTESAHLIVQHLTFLGKA-----NNQT---LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTP 511
Cdd:cd14880    79 SIVVSGESGAGKTWTSRCLMKFYAVVAASptsweSHKIaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  512 TGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLsDFRLPEEKPPRYIADETGRVMHDItskesyrrqF 591
Cdd:cd14880   159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERL-QWHLPEGAAFSWLPNPERNLEEDC---------F 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  592 EAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVT 671
Cdd:cd14880   229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  672 -RGETIIRANTVDRAADV-RDAMSKALYGRLFSWIVNRINtllqpdENICSAGGGMN--VGILDIFGFENFQRNSFEQLC 747
Cdd:cd14880   309 gKQQQVFKKPCSRAECDTrRDCLAKLIYARLFDWLVSVIN------SSICADTDSWTtfIGLLDVYGFESFPENSLEQLC 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  748 INIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATD----QTLVDKFE 823
Cdd:cd14880   383 INYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSaaqlQTRIESAL 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  824 DNLRC----KYFWRPKgvelcFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSI-PLTKTGNLAQT 898
Cdd:cd14880   463 AGNPClghnKLSREPS-----FIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAnPEEKTQEEPSG 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  899 RARITVAssslpphfsagkakvdtlevirhpeettnmkrqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFS 978
Cdd:cd14880   538 QSRAPVL---------------------------------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFL 584
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  979 RERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLaftAHQTPLASKESCVAILEKSRLDHWVLGKTKVFL 1054
Cdd:cd14880   585 QEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL---RRLRPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
32-302 8.82e-113

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 354.26  E-value: 8.82e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd06612     1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV-PVEEDLQEIIKEISILKQC-DSPYIVKYYGSYFK-----NTDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd06612    74 WIVMEYCGAGSVSDIMK---ITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKW 271
Cdd:cd06612   151 DTMAKRNTVIGTPFWMAPEVIQ-----EIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKW 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06612   226 SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
368-1055 1.45e-110

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 363.05  E-value: 1.45e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHG--VKR---ASNPPHIFASADAAYQCMVTLSKDQCI 441
Cdd:cd14886     3 VIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQadTSRgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  442 VISGESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARIS 521
Cdd:cd14886    83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKIT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  522 EYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLS-DFRLPE-----EKPPRYIADEtgrvMHDITSKESYRRQFEAIq 595
Cdd:cd14886   163 SYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSlGFKSLEsynflNASKCYDAPG----IDDQKEFAPVRSQLEKL- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  596 hcfriigFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGET 675
Cdd:cd14886   238 -------FSKNEIDSFYKCISGILLAGNIEFSEEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  676 IIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDenicsAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQI 755
Cdd:cd14886   311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFD-----ADARPWIGILDIYGFEFFERNTYEQLLINYANERL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  756 QYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRF----PQATDQTLVDKFEDNLrckyF 831
Cdd:cd14886   386 QQYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIqtgsSEKFTSSCKSKIKNNS----F 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  832 WRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSipltktgnlaqtraritvassslpp 911
Cdd:cd14886   462 IPGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFS------------------------- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  912 hfsagkakvdtleviRHPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGI 991
Cdd:cd14886   517 ---------------DIPNEDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSI 581
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  992 LETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAIleKSRLDH-------WVLGKTKVFLK 1055
Cdd:cd14886   582 FESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEDLVEAV--KSILENlgipcsdYRIGKTKVFLR 650
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
36-302 4.54e-108

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 341.49  E-value: 4.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKkESILNEIAILKKC-KHPNIVKYYGSYLKKD-----ELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGllrCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd05122    76 MEFCSGGSLKDLLKN---TNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 lRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWCEE 274
Cdd:cd05122   153 -TRNTFVGTPYWMAPEVIQGK-----PYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKE 226
                         250       260
                  ....*....|....*....|....*...
gi 578803747  275 FNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd05122   227 FKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
367-1015 6.67e-107

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 355.17  E-value: 6.67e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNL-SIYSPQFSRLY---HGVK-----RASNP--PHIFASADAAYQCMVTL 435
Cdd:cd14899     2 SILNALRLRYERHAIYTHIGDILISINPFQDLpQLYGDEILRGYaydHNSQfgdrvTSTDPrePHLFAVARAAYIDIVQN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  436 SKDQCIVISGESGSGKTESAHLIVQHLTFLGKANN-----------------QTLREKILQVNSLVEAFGNSCTAINDNS 498
Cdd:cd14899    82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNnnltnsesisppaspsrTTIEEQVLQSNPILEAFGNARTVRNDNS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  499 SRFGKYLEMMF-TPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAglhhqkklSDFRLPEEKPPRYIADETGRV 577
Cdd:cd14899   162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLS--------ADNNCVSKEQKQVLALSGGPQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  578 MHDITSKE--SYRR-------QFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQ----TDKSEVPNAE 644
Cdd:cd14899   234 SFRLLNQSlcSKRRdgvkdgvQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDdtvfADEARVMSST 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  645 A-----LQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQ------ 713
Cdd:cd14899   314 TgafdhFTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQrqasap 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  714 ---PDENICSAGGGMN-VGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPL 789
Cdd:cd14899   394 wgaDESDVDDEEDATDfIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRAC 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  790 LDMFLQKPLGLLALLDEESRFPQATDQTLVDK----FEDNLRCKYFWRPKGVELC--FGIQHYAGKVLYDASGVLEKNRD 863
Cdd:cd14899   474 LELFEHRPIGIFSLTDQECVFPQGTDRALVAKyyleFEKKNSHPHFRSAPLIQRTtqFVVAHYAGCVTYTIDGFLAKNKD 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  864 TLPADVVVVLRTSENKLLQQLfsipltktgnlaqtraritvaSSSLPPHFSAGKAKVDTLEVIRHPEETTNMKRQTVASY 943
Cdd:cd14899   554 SFCESAAQLLAGSSNPLIQAL---------------------AAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQ 612
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  944 FRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRY 1015
Cdd:cd14899   613 FKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
36-302 1.70e-102

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 326.57  E-value: 1.70e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMdEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWL 113
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVikLEPGDDF-EIIQQEISMLKEC-RHPNIVAYFGSYLRRD-----KLWI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd06613    75 VMEYCGGGSLQDIYQVT----GPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR--NPPPTLLHPEKW 271
Cdd:cd06613   151 IAKRKSFIGTPYWMAPEVAAVERK--GGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKsnFDPPKLKDKEKW 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06613   229 SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
26-302 1.54e-100

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 321.96  E-value: 1.54e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   26 LESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYK--- 102
Cdd:cd06636     8 LSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKksp 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 ADHcvGGQLWLVLELCNGGSVTELVKGLLrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV 182
Cdd:cd06636    88 PGH--DDQLWLVMEFCGAGSVTDLVKNTK--GNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPP 262
Cdd:cd06636   164 DFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPP 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  263 PTlLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06636   244 PK-LKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
366-1022 6.70e-100

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276863  Cd Length: 578  Bit Score: 331.48  E-value: 6.70e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHgvkRASNPPHIFASADAAYQCMVtLSKDQCIVISG 445
Cdd:cd14898     1 NATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKN---YSHVEPHVYDVAEASVQDLL-VHGNQTIVISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFlGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTptGVVMGARISEYLL 525
Cdd:cd14898    77 ESGSGKTENAKLVIKYLVE-RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGlhhqkklSDFRLPEEkpprYIadETGRVMHDITSKESYRRQFEAIQHCFRIIGFTD 605
Cdd:cd14898   154 EKSRVTHHEKGERNFHIFYQFCAS-------KRLNIKND----FI--DTSSTAGNKESIVQLSEKYKMTCSAMKSLGIAN 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 keVHSVYRILAGILNIGNIEFAaissqhQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRA 685
Cdd:cd14898   221 --FKSIEDCLLGILYLGSIQFV------NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQA 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  686 ADVRDAMSKALYGRLFSWIVNRINtllqpdeNICSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFA 765
Cdd:cd14898   293 RTIRNSMARLLYSNVFNYITASIN-------NCLEGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  766 LEQMEYQNEGIDAVPVEYEDNRPLLDMFlQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRckYFWRPKGVELCFgIQH 845
Cdd:cd14898   366 AKQGMYKEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKIKKYLN--GFINTKARDKIK-VSH 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  846 YAGKVLYDASGVLEKNRDtlpadvvvvlrtsenkllqqlfsipltkTGNlaqtraritvassslpphfsagkakvdtLEV 925
Cdd:cd14898   442 YAGDVEYDLRDFLDKNRE----------------------------KGQ----------------------------LLI 465
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  926 IRHPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHR 1005
Cdd:cd14898   466 FKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQE 545
                         650
                  ....*....|....*..
gi 578803747 1006 ILFEEFVKRYYYLAFTA 1022
Cdd:cd14898   546 IPKDRFEERYRILGITL 562
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
37-303 9.25e-99

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 316.88  E-value: 9.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD--EEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQLWLV 114
Cdd:cd06609     4 TLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDeiEDIQQEIQFLSQC-DSPYITKYYGSFLK-----GSKLWII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd06609    78 MEYCGGGSVLDLLKP-----GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIACeqqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPeKWCEE 274
Cdd:cd06609   153 SKRNTFVGTPFWMAPEVIKQ-----SGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGN-KFSKP 226
                         250       260
                  ....*....|....*....|....*....
gi 578803747  275 FNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06609   227 FKDFVELCLNKDPKERPSAKELLKHKFIK 255
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
366-1054 1.46e-97

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 326.69  E-value: 1.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQN----LSIYSPQFSRLY----HGVKRASNpphifASADAAYQcmvtlsk 437
Cdd:cd14881     1 DAVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLApqllKVVQEAVR-----QQSETGYP------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  438 dQCIVISGESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVN-SLVEAFGNSCTAINDNSSRFGKYLEMMFTpTGVVM 516
Cdd:cd14881    69 -QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAfTVLRSLGSAKTATNSESSRIGHFIEVQVT-DGALY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  517 GARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPP--RYIadETGRVMHDITskESYRRqFEAI 594
Cdd:cd14881   147 RTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEER-VKLHLDGYSPAnlRYL--SHGDTRQNEA--EDAAR-FQAW 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  595 QHCFRIIG--FTDkevhsVYRILAGILNIGNIEFaaissqHQTDKSEV-PNAEA-LQNAASVLCISPEELQEALTSHCVV 670
Cdd:cd14881   221 KACLGILGipFLD-----VVRVLAAVLLLGNVQF------IDGGGLEVdVKGETeLKSVAALLGVSGAALFRGLTTRTHN 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  671 TRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGMNVGILDIFGFENFQRNSFEQLCINI 750
Cdd:cd14881   290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLKRLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINL 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  751 ANEQIQYYFNQHVFALEQMEYQNEGID-AVPVEYEDNRPLLDMFLQKPLGLLALLDEESRfPQATDQTLVDKF----EDN 825
Cdd:cd14881   370 CAETMQHFYNTHIFKSSIESCRDEGIQcEVEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIkvqhRQN 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  826 LRckyFWRPKGVEL-CFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTsenkllqqlfsipltktgnlaqtraritv 904
Cdd:cd14881   449 PR---LFEAKPQDDrMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK----------------------------- 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  905 assslpphfsagkakvdtlevirhpeETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLA 984
Cdd:cd14881   497 --------------------------QNCNFGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVR 550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  985 QLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKE-SCVAILEKSRLDH-----------WVLGKTKV 1052
Cdd:cd14881   551 QIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKAlEDCALILQFLEAQppsklssvstsWALGKRHI 630

                  ..
gi 578803747 1053 FL 1054
Cdd:cd14881   631 FL 632
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
31-302 8.46e-97

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 311.68  E-value: 8.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDmdEEIE---AEYNILQFLpNHPNVVKFYGMFYKAdhcv 107
Cdd:cd06611     2 NPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESE--EELEdfmVEIDILSEC-KHPNIVGLYEAYFYE---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 gGQLWLVLELCNGGSVTELVkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06611    75 -NKLWILIEFCDGGALDSIM---LELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd06611   151 AKNKSTLQKRDTFIGTPYWMAPEVVACETFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQ 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06611   231 PSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFV 265
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
29-303 1.52e-93

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 303.56  E-value: 1.52e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   29 LPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADH-CV 107
Cdd:cd06637     1 LRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPpGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSVTELVKGLLrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06637    81 DDQLWLVMEFCGAGSVTDLIKNTK--GNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTlLH 267
Cdd:cd06637   159 AQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPR-LK 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06637   238 SKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
368-1055 1.11e-90

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 307.71  E-value: 1.11e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSrlyhgvKRASN--PPHIFASADAAYQCMVTLSKDQCIVISG 445
Cdd:cd14937     3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYK------NKNTNelPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  446 ESGSGKTESAHLIVQHLTFLGKANNQtLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLL 525
Cdd:cd14937    77 ESGSGKTEASKLVIKYYLSGVKEDNE-ISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYIADETGRVMHDITSKEsyrrqFEAIQHCFRIIGFTD 605
Cdd:cd14937   156 ENIRVVSQEEEERGYHIFYQIFNGMSQELK-NKYKIRSENEYKYIVNKNVVIPEIDDAKD-----FGNLMISFDKMNMHD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  606 KEvHSVYRILAGILNIGNIEFAAISSQHQTDKSEVP--NAEALQNAASVLCISPEELQEaltshCVVTRGETIirAN--- 680
Cdd:cd14937   230 MK-DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDknNLELVNEISNLLGINYENLKD-----CLVFTEKTI--ANqki 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  681 ----TVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAgggmnVGILDIFGFENFQRNSFEQLCINIANEQIQ 756
Cdd:cd14937   302 eiplSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNY-----IGILDIFGFEIFSKNSLEQLLINIANEEIH 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  757 YYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMfLQKPLGLLALLDEESRFPQATDQTLV----DKFEDNLrcKYFW 832
Cdd:cd14937   377 SIYLYIVYEKETELYKAEDILIESVKYTTNESIIDL-LRGKTSIISILEDSCLGPVKNDESIVsvytNKFSKHE--KYAS 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  833 RPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFsipltktgnlaqtraritvassslpph 912
Cdd:cd14937   454 TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLY--------------------------- 506
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  913 fsagkakvDTLEVirhpeeTTNMKRQTVASY-FRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGI 991
Cdd:cd14937   507 --------EDVEV------SESLGRKNLITFkYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSI 572
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  992 LETVSIRRqGYSHRILFEEFVKRYYYLAF-TAHQTPLASKESCVAILEKS-RLDHWVLGKTKVFLK 1055
Cdd:cd14937   573 IETLNISF-FFQYKYTFDVFLSYFEYLDYsTSKDSSLTDKEKVSMILQNTvDPDLYKVGKTMVFLK 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
381-1055 8.12e-89

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 305.03  E-value: 8.12e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  381 IYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGESGSGKTESAHLIVQ 460
Cdd:cd14887    24 IYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  461 HLTFLGK----ANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLEKSRVIKQAAR 536
Cdd:cd14887   104 YLAAVSDrrhgADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  537 EKNFHIFyyiYAGLHHQKKLSDFR-LPEEKPPryiadetgrvmhditskESYRRQFeaIQHCFRIIGFTDKEVHSVYRIL 615
Cdd:cd14887   184 EFSFHIF---YALCNAAVAAATQKsSAGEGDP-----------------ESTDLRR--ITAAMKTVGIGGGEQADIFKLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  616 AGILNIGNIEFA---------------------------AISSQHQTDKSEVPNAEA----LQNAASVLCISP-----EE 659
Cdd:cd14887   242 AAILHLGNVEFTtdqepetskkrkltsvsvgceetaadrSHSSEVKCLSSGLKVTEAsrkhLKTVARLLGLPPgvegeEM 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  660 LQEALTSHCV-VTRgetiiRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQ---------PDENICSAGGGMNVGI 729
Cdd:cd14887   322 LRLALVSRSVrETR-----SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQrsakpsesdSDEDTPSTTGTQTIGI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  730 LDIFGFENFQ---RNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDN--RPLLDMFLQKPLGLLALL 804
Cdd:cd14887   397 LDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPfsFPLASTLTSSPSSTSPFS 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  805 ---DEESRFPQATDQTLVDKF----------------EDNLRCKYFWRPKGVE----------------LCFGIQHYAGK 849
Cdd:cd14887   477 ptpSFRSSSAFATSPSLPSSLsslssslsssppvwegRDNSDLFYEKLNKNIInsakyknitpalsrenLEFTVSHFACD 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  850 VLYDASGVLEKNRDTLPADvvvvlrtsenklLQQLFSIPLTKTGNLAQTRARITVASSSlpphfsagkakvdtlevirhp 929
Cdd:cd14887   557 VTYDARDFCRANREATSDE------------LERLFLACSTYTRLVGSKKNSGVRAISS--------------------- 603
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  930 eettnmKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFE 1009
Cdd:cd14887   604 ------RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYV 677
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747 1010 EFVKRYYYLAFTAHQTPLASKESCVAILEKSRLD--HWVLGKTKVFLK 1055
Cdd:cd14887   678 ELWRRYETKLPMALREALTPKMFCKIVLMFLEINsnSYTFGKTKIFFR 725
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
368-1055 1.50e-88

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 303.08  E-value: 1.50e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGES 447
Cdd:cd01386     3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  448 GSGKTESAHLIVQHLTFL-GKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLE 526
Cdd:cd01386    83 GSGKTTNCRHILEYLVTAaGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  527 KSRVIKQAAREKNFHIFYYIYAGLhhqkklsDFRLPEEKPPRYIADETGRVMHDITSKESYRR---QFEAIQHCFRIIGF 603
Cdd:cd01386   163 RSRVARRPEGESNFNVFYYLLAGA-------DAALRTELHLNQLAESNSFGIVPLQKPEDKQKaaaAFSKLQAAMKTLGI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  604 TDKEVHSVYRILAGILNIGnieFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCV---VTRGETIIRAN 680
Cdd:cd01386   236 SEEEQRAIWSILAAIYHLG---AAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLsggPQQSTTSSGQE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  681 TVDR---------AADVRDAMSKALYGRLFSWIVNRINtllqpdENICSAGGGM-NVGILDIFGFEN-----FQRNS-FE 744
Cdd:cd01386   313 SPARsssggpkltGVEALEGFAAGLYSELFAAVVSLIN------RSLSSSHHSTsSITIVDTPGFQNpahsgSQRGAtFE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  745 QLCINIANEQIQYYFNQHVFALEQMEYQNEGIDavpVEYEDN----RPLLDMFLQKP--------------LGLLALLDE 806
Cdd:cd01386   387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelspGALVALIDQAPqqalvrsdlrdedrRGLLWLLDE 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  807 ESRFPQATDQTLVDK----FEDNLRCK--YFWRPKGVELCFGIQHYAGK--VLYDASGVLEKNRDtlpadvvvvlrtsen 878
Cdd:cd01386   464 EALYPGSSDDTFLERlfshYGDKEGGKghSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKE--------------- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  879 kllqqlfsipltktgNLAQTRARITVASSSlpphfsagkakvdtlevirhpEETTNMKRQTVASYFRYS---LMDLLSKM 955
Cdd:cd01386   529 ---------------NPSAQNATQLLQESQ---------------------KETAAVKRKSPCLQIKFQvdaLIDTLRRT 572
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  956 vvgQPHFVRCIKPN------DDREALQFSRERVL------AQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLA---- 1019
Cdd:cd01386   573 ---GLHFVHCLLPQhnagkdERSTSSPAAGDELLdvpllrSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLApplt 649
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 578803747 1020 ------FTAHQTPLASKESCVAI-LEKSRldhWVLGKTKVFLK 1055
Cdd:cd01386   650 kklglnSEVADERKAVEELLEELdLEKSS---YRIGLSQVFFR 689
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
39-303 2.15e-88

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 287.18  E-value: 2.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYkadhcVGGQLWLVLELC 118
Cdd:cd06614     5 LEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKEC-KHPNIVDYYDSYL-----VGDELWVVMEYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELVKgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRN 198
Cdd:cd06614    79 DGGSLTDIIT---QNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  199 TSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWCEEFNHF 278
Cdd:cd06614   156 SVVGTPYWMAPEVIK-----RKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDF 230
                         250       260
                  ....*....|....*....|....*
gi 578803747  279 ISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06614   231 LNKCLVKDPEKRPSAEELLQHPFLK 255
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
366-1011 1.18e-86

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 297.39  E-value: 1.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  366 DTIIHQLQKRYADLLIYTYVGDILIALNPFQNLS-IYSPQFSRLYHgvKRASNPPHIFASADAAYQCMVTLSKDQCIVIS 444
Cdd:cd14905     1 DTLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  445 GESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYL 524
Cdd:cd14905    79 GESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  525 LEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSdFRLPEEKPPRYIaDETGRVmhditSKESY--RRQFEAIQHCFRIIG 602
Cdd:cd14905   159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAA-YQLGDINSYHYL-NQGGSI-----SVESIddNRVFDRLKMSFVFFD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  603 FTDKEVHSVYRILAGILNIGNIEFAaissqHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHcvvtrgetiiRANTV 682
Cdd:cd14905   232 FPSEKIDLIFKTLSFIIILGNVTFF-----QKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  683 DRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENicsaggGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQH 762
Cdd:cd14905   297 NEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQY------SHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  763 VFALEQMEYQNEGID-AVPVEYEDNRPLLDMFLQkplgLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPKGVElcF 841
Cdd:cd14905   371 VLKQEQREYQTERIPwMTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPNK--F 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  842 GIQHYAGKVLYDASGVLEKNRDTLPADVVVVlrtSENKLLQQLFSipltkTGNLAQTRARITVASSSLPPHFSAGKAKVD 921
Cdd:cd14905   445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVL---HKNSITKYLFS-----RDGVFNINATVAELNQMFDAKNTAKKSPLS 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  922 TLEVI-----RHPEETTNMKRQT----------------VASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRE 980
Cdd:cd14905   517 IVKVLlscgsNNPNNVNNPNNNSgggggggnsgggsgsgGSTYTTYSSTNKAINNSNCDFHFIRCIKPNSKKTHLTFDVK 596
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 578803747  981 RVLAQLRSTGILETVSIRRQGYS----HRILFEEF 1011
Cdd:cd14905   597 SVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
36-302 2.85e-84

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 275.56  E-value: 2.85e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747     36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKkkKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDK-----LYL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    114 VLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:smart00220   75 VMEYCEGGDLFDL----LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    194 RlRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPE-KWC 272
Cdd:smart00220  151 E-KLTTFVGTPEYMAPEVLLGKG-----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDIS 224
                           250       260       270
                    ....*....|....*....|....*....|
gi 578803747    273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:smart00220  225 PEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
31-305 6.53e-83

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 273.45  E-value: 6.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDmdEEIE---AEYNILQFLpNHPNVVKFYGMFYKAdhcv 107
Cdd:cd06644     9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSE--EELEdymVEIEILATC-NHPYIVKLLGAFYWD---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 gGQLWLVLELCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06644    82 -GKLWIMIEFCPGGAVDAI---MLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd06644   158 AKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQ 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGV 305
Cdd:cd06644   238 PSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSV 275
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
368-1055 8.11e-83

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 284.84  E-value: 8.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  368 IIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHgvkrasnpphIFASADAAYQCMVTL-SKDQCIVISGE 446
Cdd:cd14874     3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKCH----------ISGVAENALDRIKSMsSNAESIVFGGE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  447 SGSGKTESAHLIVQHLTFLGKANNQTLREKILQvnSLVEAFGNSCTAINDNSSRFGKYLEMMFTpTGVVMGARISEYL-L 525
Cdd:cd14874    73 SGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIE--SVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLTGLNLKYTVpL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  526 EKSRVIKQAAREKNFHIFYYIYAGLHHQKKlSDFRLPEEKPPRYI--ADETGRVMHDItskesyrRQFEAIQHCFRIIGF 603
Cdd:cd14874   150 EVPRVISQKPGERNFNVFYEVYHGLNDEMK-AKFGIKGLQKFFYInqGNSTENIQSDV-------NHFKHLEDALHVLGF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  604 TDKEVHSVYRILAGILNIGNIEF-AAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTshCVVTRGETIiranTV 682
Cdd:cd14874   222 SDDHCISIYKIISTILHIGNIYFrTKRNPNVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL--PKSEDGTTI----DL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  683 DRAADVRDAMSKALYGRLFSWIVNRINTLLQpdeniCSAGGGMnVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQH 762
Cdd:cd14874   296 NAALDNRDSFAMLIYEELFKWVLNRIGLHLK-----CPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  763 VFALEQMEYQNEGIDavpVEYE-----DNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNL--RCKYFWRPK 835
Cdd:cd14874   370 SFHDQLVDYAKDGIS---VDYKvpnsiENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHtdRSSYGKARN 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  836 GVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSiplTKTGNlaqtraritvassslpphfsa 915
Cdd:cd14874   447 KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE---SYSSN--------------------- 502
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  916 gkakvdtlevirhpeetTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETV 995
Cdd:cd14874   503 -----------------TSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELL 565
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  996 SIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRL---DHWVLGKTKVFLK 1055
Cdd:cd14874   566 SFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQGQGVkyeNDFKIGTEYVFLR 628
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
31-302 4.58e-81

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 268.05  E-value: 4.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDmdEEIE---AEYNILQFLpNHPNVVKFYGMFYKADhcv 107
Cdd:cd06643     2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSE--EELEdymVEIDILASC-DHPNIVKLLDAFYYEN--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 ggQLWLVLELCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06643    76 --NLWILIEFCAGGAVDAV---MLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd06643   151 AKNTRTLQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQ 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06643   231 PSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
40-302 1.12e-74

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 248.68  E-value: 1.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVK---ILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd06627     6 DLIGRGAFGSVYKGLNLNTGEFVAIKqisLEKIPKSDLKSVMGEIDLLKKL-NHPNIVKYIGSVKTKDS-----LYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGLLRCGQRLdeaMISYIlYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd06627    80 YVENGSLASIIKKFGKFPESL---VAVYI-YQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIacEQqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLlhPEKWCEEFN 276
Cdd:cd06627   156 ENSVVGTPYWMAPEVI--EM---SGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPL--PENISPELR 228
                         250       260
                  ....*....|....*....|....*.
gi 578803747  277 HFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06627   229 DFLLQCFQKDPTLRPSAKELLKHPWL 254
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
369-1054 7.95e-74

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 262.21  E-value: 7.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  369 IHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHG--------VKRASN--PPHIFASADAAYQCMVTLSKD 438
Cdd:cd14893     4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKsreqtplyEKDTVNdaPPHVFALAQNALRCMQDAGED 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  439 QCIVISGESGSGKTESAHLIVQHLTFLGKANN------------QTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLE 506
Cdd:cd14893    84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEprpdsegasgvlHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  507 MMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHH----------QKKLSDFRLPEEKPPryiadetgr 576
Cdd:cd14893   164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdptlrdslemNKCVNEFVMLKQADP--------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  577 vmhDITSKESYRRQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFA----AISSQHQTDKSEVPNAE--ALQNAA 650
Cdd:cd14893   235 ---LATNFALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVpdpeGGKSVGGANSTTVSDAQscALKDPA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  651 SVLCISP-EELQEALTSHCVVTR-------GETI--IRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLL------QP 714
Cdd:cd14893   312 QILLAAKlLEVEPVVLDNYFRTRqffskdgNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdrYE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  715 DENICSAGGGmnVGILDIFGFENF--QRNSFEQLCINIANEQIQYYFNQHVFAL-------EQMEYQNEGID--AVPVEY 783
Cdd:cd14893   392 KSNIVINSQG--VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYVQNTLAInfsfledESQQVENRLTVnsNVDITS 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  784 EDNRpLLDMFLQKPLGLLALLDEESRFPQATDQTLVDK-FEDNLRCKYFWRP--------------KGVELCFGIQHYAG 848
Cdd:cd14893   470 EQEK-CLQLFEDKPFGIFDLLTENCKVRLPNDEDFVNKlFSGNEAVGGLSRPnmgadttneylapsKDWRLLFIVQHHCG 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  849 KVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQ-----QLFSIPLTKTGNLAQTRARITVASSSLPPHFSAGKAKVDTl 923
Cdd:cd14893   549 KVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHavgaaQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNITDS- 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  924 evirhpeETTNMKRQTVAsyfryslmdLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYS 1003
Cdd:cd14893   628 -------AATDVYNQADA---------LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFT 691
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747 1004 HRILFEEFVKRYYYLAftAHQTPLAS---KESCVAILEKSRldhWVLGKTKVFL 1054
Cdd:cd14893   692 VHLTYGHFFRRYKNVC--GHRGTLESllrSLSAIGVLEEEK---FVVGKTKVYL 740
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
34-302 3.55e-73

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 244.96  E-value: 3.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD------PVSDMDEEIEAEYNIlqflpNHPNVVKFYGMFykadhCV 107
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDlekcqtSMDELRKEIQAMSQC-----NHPNVVSYYTSF-----VV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSVTELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06610    71 GDELWLVMPLLSGGSLLDIMKSSYPRGG-LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQL----TSTRLRRNTSVGTPFWMAPEVIacEQqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPP 263
Cdd:cd06610   150 ASLatggDRTRKVRKTFVGTPCWMAPEVM--EQ--VRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPP 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  264 TLLH---PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06610   226 SLETgadYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
36-302 3.84e-72

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 241.66  E-value: 3.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK---ILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd06606     2 WKKGELLGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEELEALEREIRILSSL-KHPNIVRYLGTERTENT-----LN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKgllRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL-- 190
Cdd:cd06606    76 IFLEYVPGGSLASLLK---KFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLae 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMH-PVKTLFKIPRNPPPTLLhPE 269
Cdd:cd06606   152 IATGEGTKSLRGTPYWMAPEVIRGEG-----YGRAADIWSLGCTVIEMATGKPPWSELGnPVAALFKIGSSGEPPPI-PE 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  270 KWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06606   226 HLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
367-1010 8.29e-71

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 251.75  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNL---------SIYSPQFSRlYHGVKRASNPPHIFASADAAYQCMVTLSK 437
Cdd:cd14884     2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLkelydqdvmNVYLHKKSN-SAASAAPFPKAHIYDIANMAYKNMRGKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  438 DQCIVISGESGSGKTESAHLIVQHLTFLgkaNNQTLR----EKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMF---- 509
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---QTDSQMteriDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFeeve 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  510 -----TPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHhQKKLSDFRL------------PEEKPPRYIAD 572
Cdd:cd14884   158 ntqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLS-DEDLARRNLvrncgvygllnpDESHQKRSVKG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  573 --ETGRVMHDITSKESYR--RQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNiefaaissqhqtdksevpnaEALQN 648
Cdd:cd14884   237 tlRLGSDSLDPSEEEKAKdeKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  649 AASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRIN-TLLQPDE--NICSAGGGM 725
Cdd:cd14884   297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrNVLKCKEkdESDNEDIYS 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  726 N----VGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLdMFLQKplgLL 801
Cdd:cd14884   377 IneaiISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTL-IFIAK---IF 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  802 ALLDEESRFP----QATDQTLVDKFEDNLRcKYFWRPKGV-------------------ELCFGIQHYAGKVLYDASGVL 858
Cdd:cd14884   453 RRLDDITKLKnqgqKKTDDHFFRYLLNNER-QQQLEGKVSygfvlnhdadgtakkqnikKNIFFIRHYAGLVTYRINNWI 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  859 EKNRDTLPADVVVVLRTSENKLLQQlfsipltktgNLAQTRARitvassslppHFSagkakvdtlevirhpeettnmkrq 938
Cdd:cd14884   532 DKNSDKIETSIETLISCSSNRFLRE----------ANNGGNKG----------NFL------------------------ 567
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  939 TVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEE 1010
Cdd:cd14884   568 SVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
31-302 4.17e-70

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 236.49  E-value: 4.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvG 108
Cdd:cd06640     1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDleEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLK-----G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVTELvkglLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd06640    75 TKLWIIMEYLGGGSALDL----LRAGP-FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIaceQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHp 268
Cdd:cd06640   150 QLTDTQIKRNTFVGTPFWMAPEVI---QQ--SAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVG- 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  269 eKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06640   224 -DFSKPFKEFIDACLNKDPSFRPTAKELLKHKFI 256
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
31-312 1.37e-69

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 234.95  E-value: 1.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvG 108
Cdd:cd06642     1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDleEAEDEIEDIQQEITVLSQC-DSPYITRYYGSYLK-----G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd06642    75 TKLWIIMEYLGGGSALDLLKP-----GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLlhP 268
Cdd:cd06642   150 QLTDTQIKRNTFVGTPFWMAPEVIK-----QSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTL--E 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFL 312
Cdd:cd06642   223 GQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFL 266
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
31-302 2.77e-68

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 231.09  E-value: 2.77e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDeeIEAEYNILQFLPNHPNVVKFYGMFYKADhcvg 108
Cdd:cd06645     8 NPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVikLEPGEDFA--VVQQEIIMMKDCKHSNIVAYFGSYLRRD---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCNGGSVTEL--VKGllrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd06645    82 -KLWICMEFCGGGSLQDIyhVTG------PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN--PPPT 264
Cdd:cd06645   155 SAQITATIAKRKSFIGTPYWMAPEVAAVERK--GGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSnfQPPK 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  265 LLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06645   233 LKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
37-307 5.09e-67

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 227.09  E-value: 5.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSD--MDEEIEAEYNILqFLPNHPNVVKFYGMFYKadhcvGGQLWLV 114
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDeeFRKQLLRELKTL-RSCESPYVVKCYGAFYK-----EGEISIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKgllRCGqRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd06623    78 LEYMDGGSLADLLK---KVG-KIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLENT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFD---MHPVKTLFKIPRNPPPtLLHPEK 270
Cdd:cd06623   154 LDQCNTFVGTVTYMSPERIQGE-----SYSYAADIWSLGLTLLECALGKFPFLPpgqPSFFELMQAICDGPPP-SLPAEE 227
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHG 307
Cdd:cd06623   228 FSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
31-302 1.08e-65

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 223.37  E-value: 1.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMdEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvg 108
Cdd:cd06646     6 NPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIikLEPGDDF-SLIQQEIFMVKEC-KHCNIVAYFGSYLSRE---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCNGGSVTEL--VKGllrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd06646    80 -KLWICMEYCGGGSLQDIyhVTG------PLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIACEQqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN--PPPT 264
Cdd:cd06646   153 AAKITATIAKRKSFIGTPYWMAPEVAAVEK--NGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSnfQPPK 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  265 LLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06646   231 LKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
37-302 1.11e-65

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 223.11  E-value: 1.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMDE----EIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd08215     3 EKIRVIGKGSFGSAYLVRRKSDGKLYVLKEID-LSNMSEkereEALNEVKLLSKL-KHPNIVKYYESFEENGK-----LC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd08215    76 IVMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEViaCEQQydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLF-KIPRNPPPTLlhPEKW 271
Cdd:cd08215   156 TTDLAKTVVGTPYYLSPEL--CENK---PYNYKSDIWALGCVLYELCTLKHP-FEANNLPALVyKIVKGQYPPI--PSQY 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08215   228 SSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
31-314 1.54e-65

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 223.41  E-value: 1.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvg 108
Cdd:cd06641     1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDleEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKDT---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd06641    76 -KLWIIMEYLGGGSALDLLEP-----GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLlhP 268
Cdd:cd06641   150 QLTDTQIKRN*FVGTPFWMAPEVIK-----QSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTL--E 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd06641   223 GNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTE 268
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
39-303 2.67e-64

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 220.04  E-value: 2.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDE--EIEAEYNILQFLPNH--PNVVKFYGMFYKadhcvGGQLWLV 114
Cdd:cd06917     6 LELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsDIQKEVALLSQLKLGqpKNIIKYYGSYLK-----GPSLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd06917    81 MDYCEGGSIRTLMRA-----GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIAcEQQYdssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTlLHPEKWCEE 274
Cdd:cd06917   156 SKRSTFVGTPYWMAPEVIT-EGKY---YDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPR-LEGNGYSPL 230
                         250       260
                  ....*....|....*....|....*....
gi 578803747  275 FNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06917   231 LKEFVAACLDEEPKDRLSADELLKSKWIK 259
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
36-302 2.97e-63

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 216.16  E-value: 2.97e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKADHCvggql 111
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEkwqdIIKEVKFLRQL-RHPNTIEYKGCYLREHTA----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGS--VTELVKGLLRcgqrldEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGvSAQ 189
Cdd:cd06607    77 WLVMEYCLGSAsdIVEVHKKPLQ------EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SAS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTrlrRNTSVGTPFWMAPEVIAC--EQQydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTlLH 267
Cdd:cd06607   150 LVCP---ANSFVGTPYWMAPEVILAmdEGQ----YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPT-LS 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06607   222 SGEWSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
31-303 5.24e-62

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 212.69  E-value: 5.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIET---IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIE-AEYNILQFLPnHPNVVKFYGmfykaDHC 106
Cdd:cd06648     1 SPGDPRSDLDNfvkIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLfNEVVIMRDYQ-HPNIVEMYS-----SYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VGGQLWLVLELCNGGSVTELVKGLlrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd06648    75 VGDELWVVMEFLEGGALTDIVTHT-----RMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLL 266
Cdd:cd06648   150 CAQVSKEVPRRKSLVGTPYWMAPEVISRL-----PYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLK 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  267 HPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06648   225 NLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
28-303 2.03e-61

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 210.94  E-value: 2.03e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   28 SLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEAEYNILQFL----PNHPNVVKfygmfYKA 103
Cdd:cd06647     1 SVGDPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMN----LQQQPKKELIINEILvmreNKNPNIVN-----YLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  104 DHCVGGQLWLVLELCNGGSVTELVKGLlrCgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd06647    72 SYLVGDELWVVMEYLAGGSLTDVVTET--C---MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPP 263
Cdd:cd06647   147 FGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKA-----YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTP 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  264 TLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06647   222 ELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
35-302 6.35e-61

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 209.57  E-value: 6.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD------EEIEAEYNILQFLpNHPNVVKFYGMfykadHCVG 108
Cdd:cd06632     1 RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKksresvKQLEQEIALLSKL-RHPNIVQYYGT-----EREE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd06632    75 DNLYIFLEYVPGGSIHKLLQRY----GAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRnTSVGTPFWMAPEVIAceqQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNP--PPTll 266
Cdd:cd06632   151 HVEAFSFAK-SFKGSPYWMAPEVIM---QKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGelPPI-- 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  267 hPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06632   225 -PDHLSPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
37-303 1.41e-58

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 202.96  E-value: 1.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYkadhcVGGQLWLV 114
Cdd:cd06605     4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVirLEIDEALQKQILRELDVLHKC-NSPYIVGFYGAFY-----SEGDISIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd06605    78 MEYMDGGSLDKI----LKEVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RlrRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDG----DPPLFD--MHPVKTLFKIPRNPPPtLLH 267
Cdd:cd06605   154 L--AKTFVGTRSYMAPERISGGK-----YTVKSDIWSLGLSLVELATGrfpyPPPNAKpsMMIFELLSYIVDEPPP-LLP 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06605   226 SGKFSPDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
31-303 1.80e-57

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 201.80  E-value: 1.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD----PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKaDHC 106
Cdd:cd06633    18 DPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSysgkQTNEKWQDIIKEVKFLQQL-KHPNTIEYKGCYLK-DHT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VggqlWLVLELCNGGSvtelvKGLLRCGQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd06633    96 A----WLVMEYCLGSA-----SDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 vSAQLTSTrlrRNTSVGTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTL 265
Cdd:cd06633   167 -SASIASP---ANSFVGTPYWMAPEVILAMDE--GQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTL 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  266 LHPEkWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06633   241 QSNE-WTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR 277
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
39-320 3.98e-57

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 199.57  E-value: 3.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCvggQLWLVLE 116
Cdd:cd06621     6 LSSLGEGAGGSVTKCRLRNTKTIFALKTIttDPNPDVQKQILRELEINKSC-ASPYIVKYYGAFLDEQDS---SIGIAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTrlR 196
Cdd:cd06621    82 YCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNS--L 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELG--------DGDPPLFdmhPVKTLFKIPRNPPPTLLHP 268
Cdd:cd06621   160 AGTFTGTSYYMAPERIQGG-----PYSITSDVWSLGLTLLEVAqnrfpfppEGEPPLG---PIELLSYIVNMPNPELKDE 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  269 E----KWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFLQKQLAKVL 320
Cdd:cd06621   232 PengiKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAKFVKQVW 287
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
28-303 8.31e-57

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 199.18  E-value: 8.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   28 SLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE-IEAEYNILQFLPNhPNVVKFYGMFYkadhc 106
Cdd:cd06655    13 SIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKElIINEILVMKELKN-PNIVNFLDSFL----- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VGGQLWLVLELCNGGSVTELVKGLLrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd06655    87 VGDELFVVMEYLAGGSLTDVVTETC-----MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLL 266
Cdd:cd06655   162 CAQITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQ 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  267 HPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06655   237 NPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
28-303 1.12e-56

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 198.79  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   28 SLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKfygmfYKADHCV 107
Cdd:cd06656    13 SVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN-----YLDSYLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSVTELVKGLLrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06656    88 GDELWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd06656   163 AQITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQN 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06656   238 PERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
28-303 9.47e-56

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 196.10  E-value: 9.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   28 SLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKfygmfYKADHCV 107
Cdd:cd06654    14 SVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVN-----YLDSYLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSVTELVKGLLrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd06654    89 GDELWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd06654   164 AQITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQN 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06654   239 PEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
36-301 9.94e-56

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 194.62  E-value: 9.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD---PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDkkkLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKN-----LY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVSAQ 189
Cdd:cd05117    76 LVMELCTGG---ELFDRIVKKG-SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspIKIIDFGLAKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRnTSVGTPFWMAPEVIACeqqydSSYDARCDVWSLG-ITAIELGdGDPPlFDMHPVKTLF-KIPRNPPPtlLH 267
Cdd:cd05117   152 FEEGEKLK-TVCGTPYYVAPEVLKG-----KGYGKKCDIWSLGvILYILLC-GYPP-FYGETEQELFeKILKGKYS--FD 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  268 PEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd05117   222 SPEWknvSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
367-1054 5.04e-55

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 205.46  E-value: 5.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  367 TIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLY---HGVKRAS-NPPHIFASAdaaYQCMVTLSKDQCIV 442
Cdd:cd14938     2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYkciDCIEDLSlNEYHVVHNA---LKNLNELKRNQSII 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  443 ISGESGSGKTESAHLIVQHLTFLGKAN-----------------------NQTLREKILQVNSLVEAFGNSCTAINDNSS 499
Cdd:cd14938    79 ISGESGSGKSEIAKNIINFIAYQVKGSrrlptnlndqeednihneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  500 RFGKYLeMMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAG-------LHHQKKLSDFR-LPEEKPPRYIA 571
Cdd:cd14938   159 RFSKFC-TIHIENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGssdkfkkMYFLKNIENYSmLNNEKGFEKFS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  572 DETGRVMHDITSkesyrrqfeaiqhcFRIIGFTDKEVHSVYRILAGILNIGNIE----FAAISS-----------QHQTD 636
Cdd:cd14938   238 DYSGKILELLKS--------------LNYIFDDDKEIDFIFSVLSALLLLGNTEivkaFRKKSLlmgknqcgqniNYETI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  637 KSEVPNAE--ALQN-------AASVLCISPEELQEALTSHCVVTRgETIIRANTVDRAADVRDAMSKALYGRLFSWIVNR 707
Cdd:cd14938   304 LSELENSEdiGLDEnvknlllACKLLSFDIETFVKYFTTNYIFND-SILIKVHNETKIQKKLENFIKTCYEELFNWIIYK 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  708 INTLLQPDENICSAGGGMNVgiLDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGID-AVPVEYEDN 786
Cdd:cd14938   383 INEKCTQLQNININTNYINV--LDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFcEYNSENIDN 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  787 RPLLDMFLQKPLGLLALLDEESRFPQATDQ-----TLVDKFEDNlrCKYFWRP--KGVELCFGIQHYAGKVLYDASGVLE 859
Cdd:cd14938   461 EPLYNLLVGPTEGSLFSLLENVSTKTIFDKsnlhsSIIRKFSRN--SKYIKKDdiTGNKKTFVITHSCGDIIYNAENFVE 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  860 KNRDTLPADVVVVLRTSENKLLQQL-FSIPLTKTGNLAQTRARITVASSslpphFSAGKAKVDTlevirhpeettnmKRQ 938
Cdd:cd14938   539 KNIDILTNRFIDMVKQSENEYMRQFcMFYNYDNSGNIVEEKRRYSIQSA-----LKLFKRRYDT-------------KNQ 600
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  939 TVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREAL-QFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKryyy 1017
Cdd:cd14938   601 MAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRELcSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS---- 676
                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 578803747 1018 lAFTAHQTPLasKESCVAILEKSRLD--HWVLGKTKVFL 1054
Cdd:cd14938   677 -IFDIKNEDL--KEKVEALIKSYQISnyEWMIGNNMIFL 712
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
42-300 6.14e-55

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 190.56  E-value: 6.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP--VSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLELCN 119
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKekLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENF-----LYLVMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSVTELVKgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNT 199
Cdd:cd00180    75 GGSLKDLLK---ENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  200 SVGTPFWMAPEVIACEQQYdssYDARCDVWSLGITAIELgdgdpplfdmhpvktlfkiprnppptllhpekwcEEFNHFI 279
Cdd:cd00180   152 TGGTTPPYYAPPELLGGRY---YGPKVDIWSLGVILYEL----------------------------------EELKDLI 194
                         250       260
                  ....*....|....*....|.
gi 578803747  280 SQCLIKDFERRPSVTHLLDHP 300
Cdd:cd00180   195 RRMLQYDPKKRPSAKELLEHL 215
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
37-302 1.39e-54

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 191.60  E-value: 1.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMDE----EIEAEYNILQFLpNHPNVVKFYGMFY-KADHcvggQL 111
Cdd:cd08217     3 EVLETIGKGSFGTVRKVRRKSDGKILVWKEID-YGKMSEkekqQLVSEVNILREL-KHPNIVRYYDRIVdRANT----TL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHN-----NRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd08217    77 YIVMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLF-KIPRNPPPTL 265
Cdd:cd08217   157 ARVLSHDSSFAKTYVGTPYYMSPELLN-----EQSYDEKSDIWSLGCLIYELCALHPP-FQAANQLELAkKIKEGKFPRI 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 lhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08217   231 --PSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
36-298 3.25e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 197.54  E-value: 3.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYkadhcVGGQL 111
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARErfrrEARALARL-NHPNIVRVYDVGE-----EDGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:COG0515    83 YLVMEYVEGESLADL----LRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRL-RRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEK 270
Cdd:COG0515   159 GATLtQTGTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRP 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  271 WC-EEFNHFISQCLIKDFERRP-SVTHLLD 298
Cdd:COG0515   234 DLpPALDAIVLRALAKDPEERYqSAAELAA 263
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
42-301 6.03e-54

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 188.88  E-value: 6.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP----VSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKkeiiKRKEVEHTLNERNILERV-NHPFIVKLHYAFQTEEK-----LYLVLDY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGqRLDEAMISyiLYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd05123    75 VPGG---ELFSHLSKEG-RFPEERAR--FYAAeiVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIAcEQQYDSSydarCDVWSLGITAIELGDGDPPLFDmHPVKTLF-KIPRNPPPTllhPEKWCEE 274
Cdd:cd05123   149 RTYTFCGTPEYLAPEVLL-GKGYGKA----VDWWSLGVLLYEMLTGKPPFYA-ENRKEIYeKILKSPLKF---PEYVSPE 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  275 FNHFISQCLIKDFERR---PSVTHLLDHPF 301
Cdd:cd05123   220 AKSLISGLLQKDPTKRlgsGGAEEIKAHPF 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
42-302 1.41e-53

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 188.67  E-value: 1.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKIL---DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVLELC 118
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIrfqDNDPKTIKEIADEMKVLEGL-DHPNLVRYYGVEVHRE-----EVYIFMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST----- 193
Cdd:cd06626    82 QEGTLEEL----LRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNtttma 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAceQQYDSSYDARCDVWSLGITAIELGDGDPPLFDM-HPVKTLFKIPRNPPPTLLHPEKWC 272
Cdd:cd06626   158 PGEVNSLVGTPAYMAPEVIT--GNKGEGHGRAADIWSLGCVVLEMATGKRPWSELdNEWAIMYHVGMGHKPPIPDSLQLS 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06626   236 PEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
37-303 4.46e-53

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 186.53  E-value: 4.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMDE---------EIEaeyniLQFLPNHPNVVKFYGMFYKADHcv 107
Cdd:cd14007     3 EIGKPLGKGKFGNVYLAREKKSGFIVALKVI-SKSQLQKsglehqlrrEIE-----IQSHLRHPNILRLYGYFEDKKR-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 ggqLWLVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd14007    75 ---IYLILEYAPNG---ELYKELKKQK-RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTrlRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPTLlh 267
Cdd:cd14007   148 VHAPSN--RRKTFCGTLDYLPPEMVEGK-----EYDYKVDIWSLGVLCYELLVGKPP-FESKSHQETYKRIQNVDIKF-- 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14007   218 PSSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
36-298 5.14e-53

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 186.64  E-value: 5.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEI----EAEYNILQFLpNHPNVVKFYGMFYkadhcVGGQL 111
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFrerfLREARALARL-SHPNIVRVYDVGE-----DDGRP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14014    76 YIVMEYVEGGSLADLLRE----RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRR-NTSVGTPFWMAPeviacEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI--PRNPPPTLLHP 268
Cdd:cd14014   152 DSGLTQtGSVLGTPAYMAP-----EQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHlqEAPPPPSPLNP 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  269 EKWcEEFNHFISQCLIKDFERRP-SVTHLLD 298
Cdd:cd14014   227 DVP-PALDAIILRALAKDPEERPqSAAELLA 256
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
35-302 1.95e-51

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 182.64  E-value: 1.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVY-KVTNKrdGSLAAVK--ILDPvSDMD------EEIEAEYNILQFLpNHPNVVKFYGMFYKaDH 105
Cdd:cd06631     2 QWKKGNVLGKGAYGTVYcGLTST--GQLIAVKqvELDT-SDKEkaekeyEKLQEEVDLLKTL-KHVNIVGYLGTCLE-DN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 CVGgqlwLVLELCNGGSVTELvkgLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd06631    77 VVS----IFMEFVPGGSIASI---LARFGA-LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQL-------TSTRLRRNTSvGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI- 257
Cdd:cd06631   149 CAKRLcinlssgSQSQLLKSMR-GTPYWMAPEVIN-----ETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIg 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  258 -PRNPPPTLlhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06631   223 sGRKPVPRL--PDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
26-302 2.47e-51

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 183.26  E-value: 2.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   26 LESLPDPTDTWEIIET---IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYgmfyk 102
Cdd:cd06659    10 LRMVVDQGDPRQLLENyvkIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMY----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 ADHCVGGQLWLVLELCNGGSVTELVKGLlrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV 182
Cdd:cd06659    85 KSYLVGEELWVLMEYLQGGALTDIVSQT-----RLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPP 262
Cdd:cd06659   160 DFGFCAQISKDVPKRKSLVGTPYWMAPEVIS-----RCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPP 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  263 PTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06659   235 PKLKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
42-302 7.06e-51

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 180.83  E-value: 7.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILD---------------PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFY--KAD 104
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkrregkndrgKIKNALDDVRREIAIMKKL-DHPNIVRLYEVIDdpESD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HcvggqLWLVLELCNGGSVTELvkGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd14008    80 K-----LYLVLEYCEGGPVMEL--DSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 GVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDArcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPT 264
Cdd:cd14008   153 GVSEMFEDGNDTLQKTAGTPAFLAPELCDGDSKTYSGKAA--DIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEF 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  265 LLHPEkWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14008   231 PIPPE-LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
31-302 2.99e-50

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 181.02  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKaDHC 106
Cdd:cd06635    22 DPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEkwqdIIKEVKFLQRI-KHPNSIEYKGCYLR-EHT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VggqlWLVLELCNGGSvtelvKGLLRCGQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd06635   100 A----WLVMEYCLGSA-----SDLLEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 vSAQLTSTrlrRNTSVGTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTL 265
Cdd:cd06635   171 -SASIASP---ANSFVGTPYWMAPEVILAMDE--GQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTL 244
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 LHPEkWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06635   245 QSNE-WSDYFRNFVDSCLQKIPQDRPTSEELLKHMFV 280
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
31-302 3.02e-50

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 180.60  E-value: 3.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKaDHC 106
Cdd:cd06634    12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEkwqdIIKEVKFLQKL-RHPNTIEYRGCYLR-EHT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VggqlWLVLELCNGGSvtelvKGLLRCGQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd06634    90 A----WLVMEYCLGSA-----SDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 vSAQLTSTrlrRNTSVGTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPtL 265
Cdd:cd06634   161 -SASIMAP---ANSFVGTPYWMAPEVILAMDE--GQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESP-A 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 LHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06634   234 LQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFL 270
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
36-300 6.51e-50

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 177.60  E-value: 6.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMD----EEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQID-ISRMSrkmrEEAIDEARVLSKL-NSPYVIKYYDSFVD-----KGKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd08529    75 NIVMEYAENGDLHSLIKSQR--GRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEViaCEqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLlhPEKW 271
Cdd:cd08529   153 DTTNFAQTIVGTPYYLSPEL--CE---DKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPI--SASY 225
                         250       260
                  ....*....|....*....|....*....
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd08529   226 SQDLSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
36-301 7.43e-50

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 177.32  E-value: 7.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD---PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDkskLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENK-----IY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ-LT 191
Cdd:cd14003    76 LVMEYASGG---ELFDYIVNNG-RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEfRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLrrNTSVGTPFWMAPEVIACEQqydssYDAR-CDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPtllHPEK 270
Cdd:cd14003   152 GSLL--KTFCGTPAYAAPEVLLGRK-----YDGPkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYP---IPSH 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14003   222 LSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
42-298 1.40e-49

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 176.19  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVKILDPVSDMDEEIEA---EYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLELC 118
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEfrrEVSILSKL-RHPNIVQFIGACLSPPP-----LCIVTEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRN 198
Cdd:cd13999    73 PGGSLYDL---LHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  199 TSVGTPFWMAPEVIaCEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVK-TLFKIPRNPPPTLlhPEKWCEEFNH 277
Cdd:cd13999   150 GVVGTPRWMAPEVL-RGEPYTEK----ADVYSFGIVLWELLTGEVPFKELSPIQiAAAVVQKGLRPPI--PPDCPPELSK 222
                         250       260
                  ....*....|....*....|.
gi 578803747  278 FISQCLIKDFERRPSVTHLLD 298
Cdd:cd13999   223 LIKRCWNEDPEKRPSFSEIVK 243
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
34-308 4.50e-49

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 176.46  E-value: 4.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEE-IEAEYNILQFLPNHPNVVKFYGMFYKAdhcvgGQL 111
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKrIRATVNSQEQKrLLMDLDISMRSVDCPYTVTFYGALFRE-----GDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGgSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNN-RIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd06617    76 WICMEVMDT-SLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTrLRRNTSVGTPFWMAPEVIACEQQyDSSYDARCDVWSLGITAIELGDGDPPLFDMH-PVKTLFKIPRNPPPTLlhP- 268
Cdd:cd06617   155 VDS-VAKTIDAGCKPYMAPERINPELN-QKGYDVKSDVWSLGITMIELATGRFPYDSWKtPFQQLKQVVEEPSPQL--Pa 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGK 308
Cdd:cd06617   231 EKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSK 270
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
42-302 3.20e-47

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 170.04  E-value: 3.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVS----DMDEEIEAEYNILQFLpNHPNVVKFYGMFyKADHCVggqlWLVLEL 117
Cdd:cd14099     9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSltkpKQREKLKSEIKIHRSL-KHPNIVKFHDCF-EDEENV----YILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKGllRcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd14099    83 CSNGSLMELLKR--R--KALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 NTSVGTPFWMAPEVIACEQQYdsSYDArcDVWSLGITAIELGDGDPPlFDMHPVKTLFK-IPRN-----PPPTLLHPEKw 271
Cdd:cd14099   159 KTLCGTPNYIAPEVLEKKKGH--SFEV--DIWSLGVILYTLLVGKPP-FETSDVKETYKrIKKNeysfpSHLSISDEAK- 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  272 ceefnHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14099   233 -----DLIRSMLQPDPTKRPSLDEILSHPFF 258
Pkinase pfam00069
Protein kinase domain;
36-302 4.91e-47

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 167.81  E-value: 4.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA---EYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNilrEIKILKKL-NHPNIVRLYDAFEDKDN-----LY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   113 LVLELCNGGSVTElvkgLLRCGQRLDEAMISYILYGALLGLqhlhnnriihrdvkgnnillttEGGVKLVDFgvsaqlts 192
Cdd:pfam00069   75 LVLEYVEGGSLFD----LLSEKGAFSEREAKFIMKQILEGL----------------------ESGSSLTTF-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   193 trlrrntsVGTPFWMAPEVIACeQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWC 272
Cdd:pfam00069  121 --------VGTPWYMAPEVLGG-NPYGPK----VDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLS 187
                          250       260       270
                   ....*....|....*....|....*....|
gi 578803747   273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:pfam00069  188 EEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
42-302 1.40e-46

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 168.48  E-value: 1.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVK--ILDPVS--------DMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKqvELPSVSaenkdrkkSMLDALQREIALLREL-QHENIVQYLGSSSDANH-----L 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTelvkGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL- 190
Cdd:cd06628    82 NIFLEYVPGGSVA----TLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLe 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 -----TSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTL 265
Cdd:cd06628   158 anslsTKNNGARPSLQGSVFWMAPEVVK-----QTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTI 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 lhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06628   233 --PSNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
31-303 1.99e-46

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 169.06  E-value: 1.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYgmfykADHCVGGQ 110
Cdd:cd06658    19 DPREYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMY-----NSYLVGDE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd06658    94 LWVVMEFLEGGALTDIVTH-----TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEK 270
Cdd:cd06658   169 SKEVPKRKSLVGTPYWMAPEVIS-----RLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHK 243
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06658   244 VSSVLRGFLDLMLVREPSQRATAQELLQHPFLK 276
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
36-302 3.74e-46

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 167.15  E-value: 3.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVS-DMDEEIEAEYNILQFLPN--HPNVVKFYGmfykadhCV--G 108
Cdd:cd06625     2 WKQGKLLGQGAFGQVYLCYDADTGRELAVKQveIDPINtEASKEVKALECEIQLLKNlqHERIVQYYG-------CLqdE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd06625    75 KSLSIFMEYMPGGSV----KDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTS--VGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPP-PTL 265
Cdd:cd06625   151 RLQTICSSTGMKsvTGTPYWMSPEVINGE-----GYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTnPQL 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 lhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06625   226 --PPHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
25-302 4.50e-46

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 167.89  E-value: 4.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   25 GLESLPDPTDTWEIIET---IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFY 101
Cdd:cd06657     8 ALQMVVDPGDPRTYLDNfikIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  102 kadhcVGGQLWLVLELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKL 181
Cdd:cd06657    88 -----VGDELWVVMEFLEGGALTDIVTH-----TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  182 VDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNP 261
Cdd:cd06657   158 SDFGFCAQVSKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  262 PPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06657   233 PPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
34-302 8.84e-46

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 165.50  E-value: 8.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA---EYNILQFLpNHPNVVKFYGMF-YKADHCVgg 109
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNlrqEIEILRKL-NHPNIIEMLDSFeTKKEFVV-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qlwlvlelcnggsVTELVKG----LLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd14002    78 -------------VTEYAQGelfqILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRLRRNTSVGTPFWMAPEVIAcEQQYDSsydaRCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPtl 265
Cdd:cd14002   145 FARAMSCNTLVLTSIKGTPLYMAPELVQ-EQPYDH----TADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVK-- 217
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  266 lHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14002   218 -WPSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
37-302 2.75e-44

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 161.25  E-value: 2.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFL---PNHPNVVKFYGMFYkadHCVGGQLWL 113
Cdd:cd05118     2 EVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLndvEGHPNIVKLLDVFE---HRGGNHLCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCnGGSVTELVKgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG-VKLVDFGVSAQLTS 192
Cdd:cd05118    79 VFELM-GMNLYELIK---DYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARSFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLrrNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRnppptLLHPekwc 272
Cdd:cd05118   155 PPY--TPYVATRWYRAPEVLLGAKPYGSS----IDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR-----LLGT---- 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd05118   220 PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
37-300 1.26e-43

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 159.48  E-value: 1.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLP--NHPNVVKFYGMFykadhCVGGQLWLV 114
Cdd:cd08530     3 KVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLAsvNHPNIIRYKEAF-----LDGNRLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd08530    78 MEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRrnTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTL-FKIPRN--PPPtllhPEKW 271
Cdd:cd08530   158 AK--TQIGTPLYAAPEVWK-----GRPYDYKSDIWSLGCLLYEMATFRPP-FEARTMQELrYKVCRGkfPPI----PPVY 225
                         250       260
                  ....*....|....*....|....*....
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd08530   226 SQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
34-303 1.65e-43

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 160.40  E-value: 1.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDE----EIEAEYNILQfLPNHPNVVKFYGMFYkadhcVGG 109
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIR--LELDEskfnQIIMELDILH-KAVSPYIVDFYGAFF-----IEG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELVKGLLRCGqRLDEAMISYILYGALLGLQHL---HNnrIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd06622    73 AVYMCMEYMDAGSLDKLYAGGVATE-GIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVNGNGQVKLCDFGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRrnTSVGTPFWMAPEVIACEQQYDS-SYDARCDVWSLGITAIELGDGD---PPLFDMHPVKTLFKIPRNPP 262
Cdd:cd06622   150 SGNLVASLAK--TNIGCQSYMAPERIKSGGPNQNpTYTVQSDVWSLGLSILEMALGRypyPPETYANIFAQLSAIVDGDP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  263 PTLlhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06622   228 PTL--PSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
42-303 2.10e-43

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 160.22  E-value: 2.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIE--AEYNILQFLPNHPNVVKFYGMFYKADHCvggqlWLVLELCN 119
Cdd:cd06616    14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRllMDLDVVMRSSDCPYIVKFYGALFREGDC-----WICMELMD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GgSVTELVKGL-LRCGQRLDEAMISYILYGALLGLQHLHNN-RIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTrLRR 197
Cdd:cd06616    89 I-SLDKFYKYVyEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDS-IAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 NTSVGTPFWMAPEVIACEQQYDsSYDARCDVWSLGITAIELGDGDPP------LFDMhpvktLFKIPRNPPPTLLHPEK- 270
Cdd:cd06616   167 TRDAGCRPYMAPERIDPSASRD-GYDVRSDVWSLGITLYEVATGKFPypkwnsVFDQ-----LTQVVKGDPPILSNSEEr 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  271 -WCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06616   241 eFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIK 274
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
37-299 2.13e-43

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 158.81  E-value: 2.13e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    37 EIIETIGKGTYGKVYKVTNKRDGSLA----AVKILDPvSDMDEEIEA---EYNILQFLpNHPNVVKFYGMfykadhCVGG 109
Cdd:pfam07714    2 TLGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKE-GADEEEREDfleEASIMKKL-DHPNIVKLLGV------CTQG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   110 Q-LWLVLELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:pfam07714   74 EpLYIVTEYMPGGD---LLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   189 QLTSTRLRRNTSVGT--PFWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL-GDGDPPLFDMHPVKTLFKI---PRNPP 262
Cdd:pfam07714  151 DIYDDDYYRKRGGGKlpIKWMAPESLK-----DGKFTSKSDVWSFGVLLWEIfTLGEQPYPGMSNEEVLEFLedgYRLPQ 225
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 578803747   263 ptllhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:pfam07714  226 -----PENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
40-302 1.11e-42

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 157.54  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILD-PVSDMD----------EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvg 108
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVElPKTSSDradsrqktvvDALKSEIDTLKDL-DHPNIVQYLGFEETEDY--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS- 187
Cdd:cd06629    83 --FSIFLEYVPGGSIGSC----LRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISk 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 -AQLTSTRLRRNTSVGTPFWMAPEVIACEQQydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI------PRN 260
Cdd:cd06629   157 kSDDIYGNNGATSMQGSVFWMAPEVIHSQGQ---GYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnkrsaPPV 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  261 PPPTLLHPEKwceefNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06629   234 PEDVNLSPEA-----LDFLNACFAIDPRDRPTAAELLSHPFL 270
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
37-303 2.65e-42

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 157.15  E-value: 2.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMDEE---IEAEYNILQFLPNHPNVVKFYGMF-YKADhcvggqLW 112
Cdd:cd06618    18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQM-RRSGNKEEnkrILMDLDVVLKSHDCPYIVKCYGYFiTDSD------VF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd06618    91 ICMELMS----TCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISGRLV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRlRRNTSVGTPFWMAPEVIacEQQYDSSYDARCDVWSLGITAIELGDGDPPL------FDMhpvktLFKIPRNPPPTL 265
Cdd:cd06618   167 DSK-AKTRSAGCAAYMAPERI--DPPDNPKYDIRADVWSLGISLVELATGQFPYrnckteFEV-----LTKILNEEPPSL 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  266 LHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06618   239 PPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
37-305 4.04e-42

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 156.45  E-value: 4.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYkADHcvgGQLWLV 114
Cdd:cd06620     8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIhiDAKSSVRKQILRELQILHEC-HSPYIVSFYGAFL-NEN---NNIIIC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHN-NRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd06620    83 MEYMDCGSL----DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 rlRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDMHPVKT------------LFKIPRNP 261
Cdd:cd06620   159 --IADTFVGTSTYMSPERIQGGK-----YSVKSDVWSLGLSIIELALGEFP-FAGSNDDDdgyngpmgildlLQRIVNEP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  262 PPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGV 305
Cdd:cd06620   231 PPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQA 274
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
42-306 1.68e-40

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 151.21  E-value: 1.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMD-----EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVI-KKRDMIrknqvDSVLAERNILSQA-QNPFVVKLYYSFQGKKN-----LYLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS--------- 187
Cdd:cd05579    74 YLPGGDL----YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrrqi 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 ------AQLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI--PR 259
Cdd:cd05579   150 klsiqkKSNGAPEKEDRRIVGTPDYLAPEILLGQ-----GHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNIlnGK 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  260 NPPPTLLHPEKwceEFNHFISQCLIKDFERRP---SVTHLLDHPFIKGVH 306
Cdd:cd05579   225 IEWPEDPEVSD---EAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
42-302 3.00e-40

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 150.25  E-value: 3.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMD------EEIEAEYNIlqflpNHPNVVKFYGMFykadhCVGGQLWLVL 115
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEI-PERDSRevqplhEEIALHSRL-----SHKNIVQYLGSV-----SEDGFFKIFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVK---GLLRCgqrlDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT-EGGVKLVDFGVSAQLT 191
Cdd:cd06624    85 EQVPGGSLSALLRskwGPLKD----NENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIACEQQydsSYDARCDVWSLGITAIELGDGDPPLFDM-HPVKTLFKIP--RNPPPTllhP 268
Cdd:cd06624   161 GINPCTETFTGTLQYMAPEVIDKGQR---GYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKVGmfKIHPEI---P 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06624   235 ESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
36-298 4.41e-39

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 146.65  E-value: 4.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMD-----EEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQ 110
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQ-IFEMMdakarQDCLKEIDLLQQL-NHPNIIKYLASFIE-----NNE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd08224    75 LNIVLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLF-DMHPVKTLFKIPRN---PPptlL 266
Cdd:cd08224   155 SSKTTAAHSLVGTPYYMSPERI-----REQGYDFKSDIWSLGCLLYEMAALQSPFYgEKMNLYSLCKKIEKceyPP---L 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  267 HPEKWCEEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd08224   227 PADLYSQELRDLVAACIQPDPEKRPDISYVLD 258
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
37-320 8.86e-38

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 145.74  E-value: 8.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL-----DPVSdmdEEIEAEYNILQFLpNHPNVVKFYGMFykaDHcvGGQL 111
Cdd:PLN00034   77 ERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVR---RQICREIEILRDV-NHPNVVKCHDMF---DH--NGEI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTelvkgllrcGQRL-DEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:PLN00034  148 QVLLEFMDGGSLE---------GTHIaDEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSVGTPFWMAPEVIACEQQyDSSYDARC-DVWSLGITAIELGDGDPPLfdmhPV-----------KTLFKIP 258
Cdd:PLN00034  219 AQTMDPCNSSVGTIAYMSPERINTDLN-HGAYDGYAgDIWSLGVSILEFYLGRFPF----GVgrqgdwaslmcAICMSQP 293
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  259 RNPPPTLlhpekwCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFLQKQLAKVL 320
Cdd:PLN00034  294 PEAPATA------SREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQLL 349
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
40-302 1.10e-37

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 143.10  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNILqFLPNHPNVVKFYGMFYkadhcVGGQLWLVLEL 117
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVipLDITVELQKQIMSELEIL-YKCDSPYIIGFYGAFF-----VENRISICTEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSvtelvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRr 197
Cdd:cd06619    81 MDGGS--------LDVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAK- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 nTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGD---PPLFDMH----PVKTLFKIPRNPPPTLLHPEk 270
Cdd:cd06619   152 -TYVGTNAYMAPERISGEQ-----YGIHSDVWSLGISFMELALGRfpyPQIQKNQgslmPLQLLQCIVDEDPPVLPVGQ- 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd06619   225 FSEKFVHFITQCMRKQPKERPAPENLMDHPFI 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
37-302 3.67e-37

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 141.85  E-value: 3.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKildpVSDMDEEIEA-------EYNILQFLpNHPNVVKFYGMFYKadhcvGG 109
Cdd:cd07829     2 EKLEKLGEGTYGVVYKAKDKKTGEIVALK----KIRLDNEEEGipstalrEISLLKEL-KHPNIVKLLDVIHT-----EN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd07829    72 KLYLVFEYCD----QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTrLRRNTS-VGTPFWMAPEVIACEQQYDSSydarCDVWSLG-ITAiELGDGDpPLF------DMhpvktLFKI---- 257
Cdd:cd07829   148 FGIP-LRTYTHeVVTLWYRAPEILLGSKHYSTA----VDIWSVGcIFA-ELITGK-PLFpgdseiDQ-----LFKIfqil 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  258 ---------------------PRNPPPTLLHPEKWC-EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd07829   216 gtpteeswpgvtklpdykptfPKWPKNDLEKVLPRLdPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
36-302 1.17e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 139.71  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYN--ILQFLPNHPNVVKFYGMFYKadhcvGGQLWL 113
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKevILLAKMKHPNIVTFFASFQE-----NGRLFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV-KLVDFGVSAQLTS 192
Cdd:cd08225    77 VMEYCDGGDLMKRIN--RQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEViaCEQQydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNppptLLHP--EK 270
Cdd:cd08225   155 SMELAYTCVGTPYYLSPEI--CQNR---PYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQG----YFAPisPN 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08225   226 FSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
45-318 2.76e-36

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 140.12  E-value: 2.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   45 GTYGKVYKvtNKRDGSLAAVKILDPVSDMDEE---IEAEYNILQFLpNHPNVVKFYGMFykadhCVGGQLWLVLELCNGG 121
Cdd:cd08216    13 GGVVHLAK--HKPTNTLVAVKKINLESDSKEDlkfLQQEILTSRQL-QHPNILPYVTSF-----VVDNDLYVVTPLMAYG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELVKGLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSV 201
Cdd:cd08216    85 SCRDLLKTHFPEG--LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVVH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  202 GTP-------FWMAPEVIaceQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLL-------- 266
Cdd:cd08216   163 DFPksseknlPWLSPEVL---QQNLLGYNEKSDIYSVGITACELANGVVPFSDMPATQMLLEKVRGTTPQLLdcstyple 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  267 ----------------------HP--EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFLQKQLAK 318
Cdd:cd08216   240 edsmsqsedsstehpnnrdtrdIPyqRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQCRRSNTSLLDLLKP 315
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
36-300 3.10e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 138.72  E-value: 3.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL----DPVSDMDEEIEAEYNILQFLP--NHPNVVKFYGMFYKADHcvgg 109
Cdd:cd06630     2 WLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVsfcrNSSSEQEEVVEAIREEIRMMArlNHPNIVRMLGATQHKSH---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELVKgllRCGQRLDEAMISYIlYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG-VKLVDFGVSA 188
Cdd:cd06630    78 -FNIFVEWMAGGSVASLLS---KYGAFSENVIINYT-LQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTStrlrRNTS--------VGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDMHPVKT----LFK 256
Cdd:cd06630   153 RLAS----KGTGagefqgqlLGTIAFMAPEVLRGEQ-----YGRSCDVWSVGCVIIEMATAKPP-WNAEKISNhlalIFK 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  257 I--PRNPPPTllhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd06630   223 IasATTPPPI---PEHLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
36-302 2.44e-35

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 136.01  E-value: 2.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS----DMDEEIEA--EYNILQFLpNHPNVVKFYGMFYKADH-CVg 108
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISvgelQPDETVDAnrEAKLLSKL-DHPAIVKFHDSFVEKESfCI- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqlwlVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLtTEGGVKLVDFGVSA 188
Cdd:cd08222    80 -----VTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLlhP 268
Cdd:cd08222   154 ILMGTSDLATTFTGTPYYMSPEVLKHE-----GYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSL--P 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08222   227 DKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
37-301 4.73e-35

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 135.42  E-value: 4.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLW 112
Cdd:cd05581     4 KFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKkvkyVTIEKEVLSRL-AHPGIVKLYYTFQDES-----KLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd05581    78 FVLEYAPNG---DLLEYIRKYG-SLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 T-----------------RLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLF 255
Cdd:cd05581   154 DsspestkgdadsqiaynQARAASFVGTAEYVSPELLN-----EKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQ 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  256 KIprnppptlLHPE-KWCEEFNH----FISQCLIKDFERRPSV------THLLDHPF 301
Cdd:cd05581   229 KI--------VKLEyEFPENFPPdakdLIQKLLVLDPSKRLGVnenggyDELKAHPF 277
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
37-298 4.82e-35

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 134.97  E-value: 4.82e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747     37 EIIETIGKGTYGKVYKVTNKRDGS----LAAVKILDPVSDMD--EEIEAEYNILQFLpNHPNVVKFYGMfykadhCVGGQ 110
Cdd:smart00219    2 TLGKKLGEGAFGEVYKGKLKGKGGkkkvEVAVKTLKEDASEQqiEEFLREARIMRKL-DHPNVVKLLGV------CTEEE 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    111 -LWLVLELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:smart00219   75 pLYIVMEYMEGGD---LLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    190 LTSTRLRRNTSVGTP-FWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL-GDGDPPLFDMHPVKTLFKIP---RNPPPT 264
Cdd:smart00219  152 LYDDDYYRKRGGKLPiRWMAPESLK-----EGKFTSKSDVWSFGVLLWEIfTLGEQPYPGMSNEEVLEYLKngyRLPQPP 226
                           250       260       270
                    ....*....|....*....|....*....|....
gi 578803747    265 LLHPekwceEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:smart00219  227 NCPP-----ELYDLMLQCWAEDPEDRPTFSELVE 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
37-301 4.90e-35

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 135.77  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA-------EYNILQFLpNHPNVVKFYG-MFYKADHCVG 108
Cdd:cd07840     2 EKIAQIGEGTYGQVYKARNKKTGELVALKKIR----MENEKEGfpitairEIKLLQKL-DHPNVVRLKEiVTSKGSAKYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNggsvTELvKGLLRC-GQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd07840    77 GSIYMVFEYMD----HDL-TGLLDNpEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTS-VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPL------------FDM--HP-- 250
Cdd:cd07840   152 RPYTKENNADYTNrVITLWYRPPELLLGATRYGPE----VDMWSVGCILAELFTGKPIFqgkteleqlekiFELcgSPte 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  251 -----VKTL-----FKIPRNPPPTLLhpekwcEEFNHFISQ---CLIK-----DFERRPSVTHLLDHPF 301
Cdd:cd07840   228 enwpgVSDLpwfenLKPKKPYKRRLR------EVFKNVIDPsalDLLDklltlDPKKRISADQALQHEY 290
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
39-300 5.67e-35

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 134.43  E-value: 5.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEA--EYNILQFLPNHPNVVKFYGMFYKadhcvGGQLWLVL 115
Cdd:cd13997     5 LEQIGSGSFSEVFKVRSKVDGCLYAVKkSKKPFRGPKERARAlrEVEAHAALGQHPNIVRYYSSWEE-----GGHLYIQM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTStrl 195
Cdd:cd13997    80 ELCENGSLQDALEELSP-ISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLET--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPplfdMHPVKTLFKIPRNPPPTLLHPEKWCEEF 275
Cdd:cd13997   156 SGDVEEGDSRYLAPELLNENYTHLPK----ADIFSLGVTVYEAATGEP----LPRNGQQWQQLRQGKLPLPPGLVLSQEL 227
                         250       260
                  ....*....|....*....|....*
gi 578803747  276 NHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd13997   228 TRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
42-301 1.10e-34

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 133.50  E-value: 1.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP---VSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLELC 118
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRkklNKKLQENLESEIAILKSI-KHPNIVRLYDVQKTEDF-----IYLVLEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVSAQLTSTRL 195
Cdd:cd14009    75 AGGDLSQY----IRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 rRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN------PPPTLLHPE 269
Cdd:cd14009   151 -AETLCGSPLYMAPEILQFQK-----YDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSdavipfPIAAQLSPD 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  270 kwCEEfnhFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14009   225 --CKD---LLRRLLRRDPAERISFEEFFAHPF 251
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
32-302 1.16e-34

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 134.02  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDtWEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVS-DMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADHc 106
Cdd:cd06652     1 PTN-WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESpETSKEVNALECEIQLLKNllHERIVQYYGCLRDPQE- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 vgGQLWLVLELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd06652    79 --RTLSIFMEYMPGGSI----KDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLR---RNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI---PRN 260
Cdd:cd06652   153 SKRLQTICLSgtgMKSVTGTPYWMSPEVISGE-----GYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIatqPTN 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  261 P--PPtllHPEKWCEEFNHFIsqclIKDFERRPSVTHLLDHPFI 302
Cdd:cd06652   228 PqlPA---HVSDHCRDFLKRI----FVEAKLRPSADELLRHTFV 264
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
36-302 1.45e-34

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 133.61  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVS-DMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADHcvgGQ 110
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSqETSKEVNALECEIQLLKNlrHDRIVQYYGCLRDPEE---KK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd06653    81 LSIFVEYMPGGSV----KDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 tSTRLRRNTSV----GTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLL 266
Cdd:cd06653   157 -QTICMSGTGIksvtGTPYWMSPEVISGE-----GYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPQL 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  267 hPEKWCEEFNHFISQCLIKDfERRPSVTHLLDHPFI 302
Cdd:cd06653   231 -PDGVSDACRDFLRQIFVEE-KRRPTAEFLLRHPFV 264
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
37-305 1.69e-34

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 134.24  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLW 112
Cdd:cd05580     4 EFLKTLGTGSFGRVRLVKHKDSGKYYALKILkkAKIIKLKQVehVLNEKRILSEV-RHPFIVNLLGSFQDDR-----NLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKgLLRCGQRL--DEAMIsyilYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05580    78 MVMEYVPGG---ELFS-LLRRSGRFpnDVAKF----YAAevVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTStrlRRNTSVGTPFWMAPEVIACeqqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpppTLLHP 268
Cdd:cd05580   150 RVKD---RTYTLCGTPEYLAPEIILS-----KGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEG---KIRFP 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  269 EKWCEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGV 305
Cdd:cd05580   219 SFFDPDAKDLIKRLLVVDLTKRlgnlkNGVEDIKNHPWFAGI 260
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
34-305 1.70e-34

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 136.26  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEE--IEAEYNILQFlPNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILrkSDMLKREQIahVRAERDILAD-ADSPWIVRLHYAFQDEDH---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGsvtELVkGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05573    76 -LYLVMEYMPGG---DLM-NLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTST-----------------------------RLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGD 240
Cdd:cd05573   151 MNKSgdresylndsvntlfqdnvlarrrphkqrRVRAYSAVGTPDYIAPEVLRGT-----GYGPECDWWSLGVILYEMLY 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  241 GDPPLFDMHPVKTLFKIpRNPPPTLLHP--EKWCEEFNHFISQcLIKDFERR-PSVTHLLDHPFIKGV 305
Cdd:cd05573   226 GFPPFYSDSLVETYSKI-MNWKESLVFPddPDVSPEAIDLIRR-LLCDPEDRlGSAEEIKAHPFFKGI 291
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
36-302 1.98e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 133.01  E-value: 1.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMD----EEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvgGQL 111
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEIN-ISKMSpkerEESRKEVAVLSKM-KHPNIVQYQESFEEN-----GNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd08218    75 YIVMDYCDGGDLYKRINA--QRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEViaCEQQydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTL-FKIPR-NPPPTllhPE 269
Cdd:cd08218   153 STVELARTCIGTPYYLSPEI--CENK---PYNNKSDIWALGCVLYEMCTLKHA-FEAGNMKNLvLKIIRgSYPPV---PS 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  270 KWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08218   224 RYSYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
37-298 5.42e-34

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 131.90  E-value: 5.42e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747     37 EIIETIGKGTYGKVYKVTNKRDGS----LAAVKILDPVSDMD--EEIEAEYNILQFLpNHPNVVKFYGMfykadhCVGGQ 110
Cdd:smart00221    2 TLGKKLGEGAFGEVYKGTLKGKGDgkevEVAVKTLKEDASEQqiEEFLREARIMRKL-DHPNIVKLLGV------CTEEE 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    111 -LWLVLELCNGGSvteLVKGLLRC-GQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:smart00221   75 pLMIVMEYMPGGD---LLDYLRKNrPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    189 QLTSTRLRRNTSVGTP-FWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL-GDGDPPLFDMHPVKTLFKIP---RNPPP 263
Cdd:smart00221  152 DLYDDDYYKVKGGKLPiRWMAPESLK-----EGKFTSKSDVWSFGVLLWEIfTLGEEPYPGMSNAEVLEYLKkgyRLPKP 226
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 578803747    264 TLLHPekwceEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:smart00221  227 PNCPP-----ELYKLMLQCWAEDPEDRPTFSELVE 256
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
37-300 5.63e-34

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 131.66  E-value: 5.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPV---SDMDEEIEAEYNILQfLPNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd14050     4 TILSKLGEGSFGEVFKVRSREDGKLYAVKrSRSRFrgeKDRKRKLEEVERHEK-LGEHPNCVRFIKAWEEKGI-----LY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNggsvTELVKGLLRCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLtS 192
Cdd:cd14050    78 IQTELCD----TSLQQYCEET-HSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVEL-D 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIaceqqyDSSYDARCDVWSLGITAIELG-DGDPPLF--DMHPVktlfkipRN---PPPTLl 266
Cdd:cd14050   152 KEDIHDAQEGDPRYMAPELL------QGSFTKAADIFSLGITILELAcNLELPSGgdGWHQL-------RQgylPEEFT- 217
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  267 hpEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14050   218 --AGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
30-301 8.57e-34

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 131.74  E-value: 8.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   30 PDPTDTWEIIETIGKGTYGKVYKVTNKRDG-SLAAVKI-LDPVS-DMDEEIEAEYNILQFLPN--HPNVVKFYGMFykAD 104
Cdd:cd06651     3 PSAPINWRRGKLLGQGAFGRVYLCYDVDTGrELAAKQVqFDPESpETSKEVSALECEIQLLKNlqHERIVQYYGCL--RD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCvGGQLWLVLELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd06651    81 RA-EKTLTIFMEYMPGGSV----KDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 GVSAQL-----TSTRLRRNTsvGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI-- 257
Cdd:cd06651   156 GASKRLqticmSGTGIRSVT--GTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIat 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  258 -PRNPPptllHPEKWCEEFNHFIsQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd06651   229 qPTNPQ----LPSHISEHARDFL-GCIFVEARHRPSAEELLRHPF 268
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
36-301 8.91e-34

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 132.01  E-value: 8.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSD------MDEEIEAEYNILQFlpNHPNVVKFYGMFYKADHCVG 108
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKkVRVPLSEegiplsTIREIALLKQLESF--EHPNVVRLLDVCHGPRTDRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNggsvTELVKGLLRCGQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVs 187
Cdd:cd07838    79 LKLTLVFEHVD----QDLATYLDKCPKPgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGL- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDpPLF----DMHPVKTLFKI------ 257
Cdd:cd07838   154 ARIYSFEMALTSVVVTLWYRAPEVL-----LQSSYATPVDMWSVGCIFAELFNRR-PLFrgssEADQLGKIFDViglpse 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  258 ---PRN-------------PPPTLLHPEKwCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07838   228 eewPRNsalprssfpsytpRPFKSFVPEI-DEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
42-302 1.96e-33

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 130.94  E-value: 1.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILD-------------------------PVSDMDeEIEAEYNILQFLpNHPNVVKF 96
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSkkkllkqagffrrppprrkpgalgkPLDPLD-RVYREIAILKKL-DHPNVVKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   97 YGMFykaDHCVGGQLWLVLELCNGGSVTELVKgllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE 176
Cdd:cd14118    80 VEVL---DDPNEDNLYMVFELVDKGAVMEVPT-----DNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  177 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQydsSYDARC-DVWSLGITAIELGDGDPPLFDMHPVKtLF 255
Cdd:cd14118   152 GHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRK---KFSGKAlDIWAMGVTLYCFVFGRCPFEDDHILG-LH 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  256 KIPRNPPptLLHPEK--WCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14118   228 EKIKTDP--VVFPDDpvVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
40-292 2.23e-33

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 130.35  E-value: 2.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYK--VTNKRDGSLA-AVKILDPVSDMDE--EIEAEYNILQFLpNHPNVVKFYGMfykadhCV-GGQLWL 113
Cdd:cd00192     1 KKLGEGAFGEVYKgkLKGGDGKTVDvAVKTLKEDASESErkDFLKEARVMKKL-GHPNVVRLLGV------CTeEEPLYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALL--------GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd00192    74 VMEYMEGGD---LLDFLRKSRPVFPSPEPSTLSLKDLLsfaiqiakGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRLRRNTSvGTPF---WMAPEVIAcEQQYDS-SydarcDVWSLGITAIELG-DGDPPLFDMHPVKTLFKIP-- 258
Cdd:cd00192   151 LSRDIYDDDYYRKKT-GGKLpirWMAPESLK-DGIFTSkS-----DVWSFGVLLWEIFtLGATPYPGLSNEEVLEYLRkg 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  259 -RNPPPTLLHPekwceEFNHFISQCLIKDFERRPS 292
Cdd:cd00192   224 yRLPKPENCPD-----ELYELMLSCWQLDPEDRPT 253
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
36-302 2.32e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 129.85  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDM--DEEIEA--EYNILQFLpNHPNVVKFYGMFY--KAdhcvgg 109
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQI-PVEQMtkEERQAAlnEVKVLSML-HHPNIIEYYESFLedKA------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG-VKLVDFGVSA 188
Cdd:cd08220    74 -LMIVMEYAPGGTLFEYIQQ--RKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLtSTRLRRNTSVGTPFWMAPEViaCEQqydSSYDARCDVWSLGITaielgdgdppLFDMHPVKTLFKIPrNPPPTLLH- 267
Cdd:cd08220   151 IL-SSKSKAYTVVGTPCYISPEL--CEG---KPYNQKSDIWALGCV----------LYELASLKRAFEAA-NLPALVLKi 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  268 --------PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08220   214 mrgtfapiSDRYSEELRHLILSMLHLDPNKRPTLSEIMAQPII 256
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
39-302 2.80e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 129.86  E-value: 2.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKadhcvGGQLWLV 114
Cdd:cd08221     5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVN-LSRLSEKERRdalnEIDILSLL-NHDNIITYYNHFLD-----GESLFIE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTElvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd08221    78 MEYCNGGNLHD--KIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLhpEKWCEE 274
Cdd:cd08221   156 SMAESIVGTPYYMSPELVQGVK-----YNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDID--EQYSEE 228
                         250       260
                  ....*....|....*....|....*...
gi 578803747  275 FNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08221   229 IIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
33-302 3.12e-33

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 130.21  E-value: 3.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD-------------PVSDMDEEIEaeynILQFLpNHPNVVKFYGM 99
Cdd:cd14084     5 RKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINkrkftigsrreinKPRNIETEIE----ILKKL-SHPCIIKIEDF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  100 FYKADhcvggQLWLVLELCNGGSVTELVKGLLRcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---E 176
Cdd:cd14084    80 FDAED-----DYYIVLELMEGGELFDRVVSNKR----LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSqeeE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  177 GGVKLVDFGVSAQLTSTRLRRnTSVGTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFK 256
Cdd:cd14084   151 CLIKITDFGLSKILGETSLMK-TLCGTPTYLAPEVLRSFGT--EGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKE 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  257 IPRNPPPTlLHPEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14084   228 QILSGKYT-FIPKAWknvSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
42-253 5.53e-33

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 128.88  E-value: 5.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMD--EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVkkRHIVQTRqqEHIFSEKEILEEC-NSPFIVKLYRTFKDKKY-----LYMLMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRlRR 197
Cdd:cd05572    75 CLGG---ELWTILRDRGL-FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGR-KT 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  198 NTSVGTPFWMAPEVIaCEQQYDSSydarCDVWSLGITAIELGDGDPPlF---DMHPVKT 253
Cdd:cd05572   150 WTFCGTPEYVAPEII-LNKGYDFS----VDYWSLGILLYELLTGRPP-FggdDEDPMKI 202
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
36-303 2.06e-32

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 128.13  E-value: 2.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS-DMDEEIEaeynILQFLPNHPNVVKFYGMFYkadhcVGGQLWLV 114
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKrDPSEEIE----ILLRYGQHPNIITLRDVYD-----DGNSVYLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVSAQL 190
Cdd:cd14091    73 TELLRGG---ELLDRILRQKF-FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TStrlrRNTSVGTPFW----MAPEVIacEQQydsSYDARCDVWSLGITaielgdgdppLFDMHPVKTLFKIPRNPPP--- 263
Cdd:cd14091   149 RA----ENGLLMTPCYtanfVAPEVL--KKQ---GYDAACDIWSLGVL----------LYTMLAGYTPFASGPNDTPevi 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578803747  264 ---------TLLHPeKWC---EEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14091   210 larigsgkiDLSGG-NWDhvsDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR 260
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
36-297 2.20e-32

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 127.01  E-value: 2.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFyKADhcvgGQLWLV 114
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKeIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESF-EAD----GHLYIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd08219    77 MEYCDGGDLMQKIK--LQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTL-FKIPRNPPPTLlhPEKWCE 273
Cdd:cd08219   155 AYACTYVGTPYYVPPEIWE-----NMPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLiLKVCQGSYKPL--PSHYSY 226
                         250       260
                  ....*....|....*....|....
gi 578803747  274 EFNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd08219   227 ELRSLIKQMFKRNPRSRPSATTIL 250
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
37-306 3.67e-32

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 128.58  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDM--DEEI---EAEYNILQFlPNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd05601     4 EVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKK-SETlaQEEVsffEEERDIMAK-ANSPWITKLQYAFQDSEN-----L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05601    77 YLVMEYHPGGDLLSL---LSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTS-VGTPFWMAPEVI-ACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRNPPPTLLHPE 269
Cdd:cd05601   154 SDKTVTSKMpVGTPDYIAPEVLtSMNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI-MNFKKFLKFPE 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  270 KWC--EEFNHFISQcLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd05601   233 DPKvsESAVDLIKG-LLTDAKERLGYEGLCCHPFFSGID 270
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
36-302 4.64e-32

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 126.21  E-value: 4.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQfLPNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvlmkVEREIAIMK-LIEHPNVLKLYDVYENKKY-----L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA-QL 190
Cdd:cd14081    77 YLVLEYVSGG---ELFDYLVKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASlQP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRrnTSVGTPFWMAPEVIACEQqydssYDAR-CDVWSLGITAIELGDGDPPlFD-------MHPVKT-LFKIPRNP 261
Cdd:cd14081   153 EGSLLE--TSCGSPHYACPEVIKGEK-----YDGRkADIWSCGVILYALLVGALP-FDddnlrqlLEKVKRgVFHIPHFI 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  262 PPtllhpekwceEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14081   225 SP----------DAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
37-301 4.91e-32

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 126.88  E-value: 4.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL-DPVSDMDE-----EIEAeyniLQFLPNHPNVVKFYGMFYKADHcvggq 110
Cdd:cd07830     2 KVIKQLGDGTFGSVYLARNKETGELVAIKKMkKKFYSWEEcmnlrEVKS----LRKLNEHPNIVKLKEVFRENDE----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGgSVTELVKglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd07830    73 LYFVFEYMEG-NLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TStRLRRNTSVGTPFWMAPEVIAceqqYDSSYDARCDVWSLGITAIELGDGDpPLF------DM---------HPVKTL- 254
Cdd:cd07830   150 RS-RPPYTDYVSTRWYRAPEILL----RSTSYSSPVDIWALGCIMAELYTLR-PLFpgsseiDQlykicsvlgTPTKQDw 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  255 -----------FKIPRNPPPTL--LHPEKwCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07830   224 pegyklasklgFRFPQFAPTSLhqLIPNA-SPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
38-301 5.91e-32

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 126.25  E-value: 5.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEeIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd14010     4 LYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDK-SKRPE-VLNEVRLTHEL-KHPNVLKFYEWYETSNH-----LWLVVEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT------ 191
Cdd:cd14010    76 CTGGDLETL----LRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGeilkel 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 ----------STRLRRNTSVGTPFWMAPEVIaceQQYDSSYDArcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN- 260
Cdd:cd14010   152 fgqfsdegnvNKVSKKQAKRGTPYYMAPELF---QGGVHSFAS--DLWALGCVLYEMFTGKPPFVAESFTELVEKILNEd 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  261 -PPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14010   227 pPPPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
42-305 6.98e-32

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 127.72  E-value: 6.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDmDEEIEA---EYNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLkkEVIIE-DDDVECtmtEKRVLALANRHPFLTGLHACFQTEDR-----LYFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGsvtELVKGLLRCGqRLDEAMISYilYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd05570    77 YVNGG---DLMFHIQRAR-RFTEERARF--YAAeiCLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIaCEQQYDSSydarCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPtlLHPEKWCEE 274
Cdd:cd05570   151 NTTSTFCGTPDYIAPEIL-REQDYGFS----VDWWALGVLLYEMLAGQSP-FEGDDEDELFEAILNDEV--LYPRWLSRE 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  275 FNHFISQCLIKDFERR----PSVTH-LLDHPFIKGV 305
Cdd:cd05570   223 AVSILKGLLTKDPARRlgcgPKGEAdIKAHPFFRNI 258
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
36-301 1.04e-31

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 126.28  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDmDEEIEA----EYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESED-DEDVKKtalrEVKVLRQL-RHENIVNLKEAFRR-----KGRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCnGGSVTELVKgLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd07833    76 YLVFEYV-ERTLLELLE-ASPGG--LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTS-VGTPFWMAPEVIACeqqyDSSYDARCDVWSLGITAIELGDGDP--P------------------------ 244
Cdd:cd07833   152 ARPASPLTDyVATRWYRAPELLVG----DTNYGKPVDVWAIGCIMAELLDGEPlfPgdsdidqlyliqkclgplppshqe 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  245 LFDMHPVKTLFKIPRNPPPTLL---HPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07833   228 LFSSNPRFAGVAFPEPSQPESLerrYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
37-302 1.19e-31

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 125.06  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--------DPVSDMDEEIEaeynILQFLpNHPNVVKFYGMFYKADHcvg 108
Cdd:cd05578     3 QILRVIGKGSFGKVCIVQKKDTKKMFAMKYMnkqkciekDSVRNVLNELE----ILQEL-EHPFLVNLWYSFQDEED--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05578    75 --MYMVVDLLLGG---DLRYHLQQ-KVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIAT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSvGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRN-PPPTLLH 267
Cdd:cd05578   149 KLTDGTLATSTS-GTKPYMAPEVFMRA-----GYSFAVDWWSLGVTAYEMLRGKRP-YEIHSRTSIEEIRAKfETASVLY 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPS-VTHLLDHPFI 302
Cdd:cd05578   222 PAGWSEEAIDLINKLLERDPQKRLGdLSDLKNHPYF 257
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
34-303 1.25e-31

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 126.40  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLihLEIKPAIRNQIIRELKVLHEC-NSPYIVGFYGAFYS-----DGEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKgllRCGqRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd06615    75 SICMEHMDGGSLDQVLK---KAG-RIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTrlRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGD---PP-----LFDMHPV----------- 251
Cdd:cd06615   151 IDS--MANSFVGTRSYMSPERLQ-----GTHYTVQSDIWSLGLSLVEMAIGRypiPPpdakeLEAMFGRpvsegeakesh 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  252 -----------------KTLFKIPRNPPPTLlhPEK-WCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06615   224 rpvsghppdsprpmaifELLDYIVNEPPPKL--PSGaFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
35-299 1.89e-31

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 124.91  E-value: 1.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKildPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVGGQ---- 110
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIK---RVKLNNEKAEREVKALAKL-DHPNIVRYNGCWDGFDYDPETSssns 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 -------LWLVLELCNGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd14047    83 srsktkcLFIQMEFCEKGTLESWIEK--RNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQLTSTrLRRNTSVGTPFWMAPeviacEQQYDSSYDARCDVWSLGITAIELgdgdpplfdMHPVKTLFKipRNPPP 263
Cdd:cd14047   161 FGLVTSLKND-GKRTKSKGTLSYMSP-----EQISSQDYGKEVDIYALGLILFEL---------LHVCDSAFE--KSKFW 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  264 TLLH----PEKWCEEF---NHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14047   224 TDLRngilPDIFDKRYkieKTIIKKMLSKKPEDRPNASEILRT 266
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
36-244 2.08e-31

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 124.37  E-value: 2.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD---PVSDMDEEIEAEYNIlQFLPNHPNVVKFYGmfykadHCVGGQ-L 111
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDmkrAPGDCPENIKKEVCI-QKMLSHKNVVRFYG------HRREGEfQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKglLRCGQRLDEAmiSYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsaqlt 191
Cdd:cd14069    76 YLFLEYASGGELFDKIE--PDVGMPEDVA--QFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGL----- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  192 STRLRR-------NTSVGTPFWMAPEVIaceqqYDSSYDA-RCDVWSLGITAIELGDGDPP 244
Cdd:cd14069   147 ATVFRYkgkerllNKMCGTLPYVAPELL-----AKKKYRAePVDVWSCGIVLFAMLAGELP 202
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
36-306 5.72e-31

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 123.60  E-value: 5.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD----EEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDakarQDCVKEIDLLKQL-NHPNVIKYLDSFIEDN-----EL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd08228    78 NIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLF--DMHPVKTLFKIPR-NPPPtlLHP 268
Cdd:cd08228   158 SKTTAAHSLVGTPYYMSPERI-----HENGYNFKSDIWSLGCLLYEMAALQSPFYgdKMNLFSLCQKIEQcDYPP--LPT 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLldHPFIKGVH 306
Cdd:cd08228   231 EHYSEKLRELVSMCIYPDPDQRPDIGYV--HQIAKQMH 266
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
39-305 7.72e-31

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 122.97  E-value: 7.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMDEE-----IEAEYNILQFLPNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRSTGDYFAIKVL-KKSDMIAKnqvtnVKAERAIMMIQGESPYVAKLYYSFQSKDY-----LYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd05611    75 VMEYLNGGDCASLIKTL----GGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTsVGTPFWMAPEVIACEQQydssyDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKiprnpppTLLHPE-KWC 272
Cdd:cd05611   151 RHNKKF-VGTPDYLAPETILGVGD-----DKMSDWWSLGCVIFEFLFGYPP-FHAETPDAVFD-------NILSRRiNWP 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  273 EEFNHFISQclikdfERRPSVTHLLD-----------------HPFIKGV 305
Cdd:cd05611   217 EEVKEFCSP------EAVDLINRLLCmdpakrlgangyqeiksHPFFKSI 260
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
34-303 8.98e-31

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 124.40  E-value: 8.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLihLEIKPAIRNQIIRELQVLHEC-NSPYIVGFYGAFYS-----DGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKgllRCGqRLDEAMISYILYGALLGLQHL-HNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd06650    79 SICMEHMDGGSLDQVLK---KAG-RIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTrlRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPL------------------------- 245
Cdd:cd06650   155 IDS--MANSFVGTRSYMSPERLQ-----GTHYSVQSDIWSMGLSLVEMAVGRYPIpppdakelelmfgcqvegdaaetpp 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  246 -------------FDMHPVKTLFKIPR---NPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06650   228 rprtpgrplssygMDSRPPMAIFELLDyivNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIK 301
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
35-293 9.76e-31

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 123.00  E-value: 9.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDG----SLAAVKILDPVSDMDE--------EIEAEYNILQFLPNHPNVVKFYGMFYK 102
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKSNGqtllALKEINMTNPAFGRTEqerdksvgDIISEVNIIKEQLRHPNIVRYYKTFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 ADhcvggQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILLTTEGGVKL 181
Cdd:cd08528    81 ND-----RLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  182 VDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR-- 259
Cdd:cd08528   156 TDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNE-----PYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEae 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  260 -NPPPTLLhpekWCEEFNHFISQCLIKDFERRPSV 293
Cdd:cd08528   231 yEPLPEGM----YSDDITFVIRSCLTPDPEARPDI 261
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
40-301 1.35e-30

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 122.46  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA---------EYNILQFLPNHPNVVKFYGMFYKADHcvggq 110
Cdd:cd14093     9 EILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAeelreatrrEIEILRQVSGHPNIIELHDVFESPTF----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSV----TELVkgllrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd14093    84 IFLVFELCRKGELfdylTEVV--------TLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTsVGTPFWMAPEVIACeQQYDSS--YDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRNPPPT 264
Cdd:cd14093   156 ATRLDEGEKLREL-CGTPGYLAPEVLKC-SMYDNApgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI-MEGKYE 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  265 LLHPEkW---CEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14093   233 FGSPE-WddiSDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
42-302 1.69e-30

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 122.03  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVT--NKRDGSLAAVKIL---DPVSDMDEEIE---AEYNILQFLpNHPNVVKFYgmfykaDHCV--GGQL 111
Cdd:cd13994     1 IGKGATSVVRIVTkkNPRSGVLYAVKEYrrrDDESKRKDYVKrltSEYIISSKL-HHPNIVKVL------DLCQdlHGKW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLRCGqrLDEAmisYILYGALL-GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd13994    74 CLVMEYCPGGDLFTLIEKADSLS--LEEK---DCFFKQILrGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 T----STRLRRNTSVGTPFWMAPEVIaceqqYDSSYDAR-CDVWSLGITAIELGDGDPPlfdmhpvktlFKIPRN----- 260
Cdd:cd13994   149 GmpaeKESPMSAGLCGSEPYMAPEVF-----TSGSYDGRaVDVWSCGIVLFALFTGRFP----------WRSAKKsdsay 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  261 --------------PPPTLLHPEKWceefNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd13994   214 kayeksgdftngpyEPIENLLPSEC----RRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
36-309 1.79e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 122.83  E-value: 1.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARAdcikEIDLLKQL-NHPNVIKYYASFIEDN-----EL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd08229   100 NIVLELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLF--DMHPVKTLFKIPR-NPPPtlLHP 268
Cdd:cd08229   180 SKTTAAHSLVGTPYYMSPERI-----HENGYNFKSDIWSLGCLLYEMAALQSPFYgdKMNLYSLCKKIEQcDYPP--LPS 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDhpFIKGVHGKV 309
Cdd:cd08229   253 DHYSEELRQLVNMCINPDPEKRPDITYVYD--VAKRMHART 291
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
42-300 4.96e-30

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 120.44  E-value: 4.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILD-----PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvgGQLWLVLE 116
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKkrklrRIPNGEANVKREIQILRRL-NHRNVIKLVDVLYNEEK---QKLYMVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT----S 192
Cdd:cd14119    77 YCVGGLQEML---DSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDlfaeD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRrnTSVGTPFWMAPEvIACEQQYDSSYDArcDVWSLGITAIELGDGDPPlFDMHPVKTLF-KIPRNP---PPTLlhP 268
Cdd:cd14119   154 DTCT--TSQGSPAFQPPE-IANGQDSFSGFKV--DIWSAGVTLYNMTTGKYP-FEGDNIYKLFeNIGKGEytiPDDV--D 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  269 EKWCEefnhFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14119   226 PDLQD----LLRGMLEKDPEKRFTIEQIRQHP 253
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
36-302 6.01e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 120.23  E-value: 6.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADhcvgGQLWL 113
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKlkHPNIVSYKESFEGED----GFLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd08223    78 VMGFCEGGDLYTRLKE--QKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTL-FKIPRNPPPTLlhPEKWC 272
Cdd:cd08223   156 SDMATTLIGTPYYMSPELFS-----NKPYNHKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYKILEGKLPPM--PKQYS 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd08223   228 PELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
36-301 6.93e-30

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 120.27  E-value: 6.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP--VSDMDEEIEA---EYNILQFLpNHPNVVKFYGMFYKADHcvggq 110
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrkVAGNDKNLQLfqrEINILKSL-EHPGIVRLIDWYEDDQH----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVsA 188
Cdd:cd14098    76 IYLVMEYVEGG---DLMDFIMAWGA-IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGL-A 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVI-ACEQQYDSSYDARCDVWSLGITAIELGDGDPPlFD---MHPVKTLFKIPRNPPPT 264
Cdd:cd14098   151 KVIHTGTFLVTFCGTMAYLAPEILmSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALP-FDgssQLPVEKRIRKGRYTQPP 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  265 LLHPEKwCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14098   230 LVDFNI-SEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
36-302 7.43e-30

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 120.07  E-value: 7.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSD-MDEEIEaEYNILQFL-----PNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDyLDQSLD-EIRLLELLnkkdkADKYHIVRLKDVFYFKNH---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCnGGSVTELVKGLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT--TEGGVKLVDFGVS 187
Cdd:cd14133    76 -LCIVFELL-SQNLYEFLKQNKFQY--LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKIIDFGSS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTStrlRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDpPLFD-------MHPVKTLFKIPrn 260
Cdd:cd14133   152 CFLTQ---RLYSYIQSRYYRAPEVILGLP-----YDEKIDMWSLGCILAELYTGE-PLFPgasevdqLARIIGTIGIP-- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  261 PPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14133   221 PAHMLDQGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
37-301 8.48e-30

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 120.01  E-value: 8.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKrDGSLAAVKILDpVSDMDEEIEAEY----NILQFLPNHPNVVKFYgmfykaDHCVG---G 109
Cdd:cd14131     4 EILKQLGKGGSSKVYKVLNP-KKKIYALKRVD-LEGADEQTLQSYkneiELLKKLKGSDRIIQLY------DYEVTdedD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLElCNGGSVTELVKglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTtEGGVKLVDFGVSAQ 189
Cdd:cd14131    76 YLYMVME-CGEIDLATILK--KKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV-KGRLKLIDFGIAKA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTS--TRLRRNTSVGTPFWMAPEVIACEQQY-----DSSYDARCDVWSLGITAIELGDGDPPLFD-MHPVKTLFKIPrNP 261
Cdd:cd14131   152 IQNdtTSIVRDSQVGTLNYMSPEAIKDTSASgegkpKSKIGRPSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAII-DP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  262 PPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14131   231 NHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
37-305 9.43e-30

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 121.57  E-value: 9.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEE-----IEAEYNILQfLPNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd05599     4 EPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRK-SEMLEKeqvahVRAERDILA-EADNPWVVKLYYSFQDEEN-----L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSV-TELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd05599    77 YLIMEFLPGGDMmTLLMKK-----DTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTsVGTPFWMAPEVIACeqqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRN-------PPP 263
Cdd:cd05599   152 KKSHLAYST-VGTPDYIAPEVFLQ-----KGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKI-MNwretlvfPPE 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  264 TLLHPEkwCEEfnhfisqcLIKDF----ERR---PSVTHLLDHPFIKGV 305
Cdd:cd05599   225 VPISPE--AKD--------LIERLlcdaEHRlgaNGVEEIKSHPFFKGV 263
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
34-302 9.81e-30

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 119.68  E-value: 9.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPV----SDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvgG 109
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAqlekAGVEHQLRREVEIQSHL-RHPNILRLYGYFHDA-----T 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGsvtELVKGLLRCGQRLDEAMISYILYGALlGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd14116    79 RVYLILEYAPLG---TVYRELQKLSKFDEQRTATYITELAN-ALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTrlRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRnppPTLLHPE 269
Cdd:cd14116   155 APSS--RRTTLCGTLDYLPPEMIE-----GRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISR---VEFTFPD 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  270 KWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14116   225 FVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
42-300 1.60e-29

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 118.52  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLELCNG 120
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFI-PKRDKKkEAVLREISILNQL-QHPRIIQLHEAYESPTE-----LVLILELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQLTSTRLRRN 198
Cdd:cd14006    74 G---ELLDRLAERG-SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGEELKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  199 TsVGTPFWMAPEVIaceQQYDSSYDArcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR-NPPPTLLHPEKWCEEFNH 277
Cdd:cd14006   150 I-FGTPEFVAPEIV---NGEPVSLAT--DMWSIGVLTYVLLSGLSPFLGEDDQETLANISAcRVDFSEEYFSSVSQEAKD 223
                         250       260
                  ....*....|....*....|...
gi 578803747  278 FISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14006   224 FIRKLLVKEPRKRPTAQEALQHP 246
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
40-302 3.23e-29

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 118.10  E-value: 3.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAA---VKiLDPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvgGQLWLVL 115
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAwneIK-LRKLPKAErQRFKQEIEILKSL-KHPNIIKFYDSWESKSK---KEVIFIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNR--IIHRDVKGNNILLT-TEGGVKLVDFGVSAQLts 192
Cdd:cd13983    82 ELMTSGTLKQYLKRF----KRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLL-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 tRLRRNTSV-GTPFWMAPEViaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFD-MHPVKTLFKIPRNPPPTLLHPEK 270
Cdd:cd13983   156 -RQSFAKSViGTPEFMAPEM------YEEHYDEKVDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTSGIKPESLSKVK 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  271 wCEEFNHFISQClIKDFERRPSVTHLLDHPFI 302
Cdd:cd13983   229 -DPELKDFIEKC-LKPPDERPSARELLEHPFF 258
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
37-299 4.55e-29

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 118.24  E-value: 4.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVK--ILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd14046     9 EELQVLGKGAFGQVVKVRNKLDGRYYAIKkiKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERA-----NLYIQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGLLRcgQRLDEA--MISYILYGallgLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS----- 187
Cdd:cd14046    83 MEYCEKSTLRDLIDSGLF--QDTDRLwrLFRQILEG----LAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnkl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 ---------AQLTSTRLRRN----TSVGTPFWMAPEViacEQQYDSSYDARCDVWSLGITAIELgdGDPPLFDMHPVKTL 254
Cdd:cd14046   157 nvelatqdiNKSTSAALGSSgdltGNVGTALYVAPEV---QSGTKSTYNEKVDMYSLGIIFFEM--CYPFSTGMERVQIL 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  255 FKIpRNPPPTllHPEKWCEEFnHF----ISQCLI-KDFERRPSVTHLLDH 299
Cdd:cd14046   232 TAL-RSVSIE--FPPDFDDNK-HSkqakLIRWLLnHDPAKRPSAQELLKS 277
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
38-302 8.11e-29

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 116.90  E-value: 8.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLA--AVKILDPVSDMDEEIEaeynilQFLP---------NHPNVVKFYGMFYkadhc 106
Cdd:cd14080     4 LGKTIGEGSYSKVKLAEYTKSGLKEkvACKIIDKKKAPKDFLE------KFLPreleilrklRHPNIIQVYSIFE----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILygalLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd14080    73 RGSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLA----LAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRN--TSVGTPFWMAPEVIaCEQQYDSsydARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNP--- 261
Cdd:cd14080   149 ARLCPDDDGDVLskTFCGSAAYAAPEIL-QGIPYDP---KKYDIWSLGVILYIMLCGSMP-FDDSNIKKMLKDQQNRkvr 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  262 -PPTLLHPEKWCEEfnhFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14080   224 fPSSVKKLSPECKD---LIDQLLEPDPTKRATIEEILNHPWL 262
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
388-507 8.56e-29

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 113.98  E-value: 8.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  388 ILIALNPFQNLSIYSPQFS-RLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGESGSGKTESAHLIVQHLT--- 463
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLAsva 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  464 FLGKANNQT------------LREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEM 507
Cdd:cd01363    81 FNGINKGETegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
42-305 1.41e-28

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 117.87  E-value: 1.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIEA---EYNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALKKdVVLEDDDVECtmiERRVLALASQHPFLTHLFCTFQTESH-----LFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGqRLDEAMISYilYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd05592    78 LNGG---DLMFHIQQSG-RFDEDRARF--YGAeiICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGEN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPtllHPEKW-CEE 274
Cdd:cd05592   152 KASTFCGTPDYIAPEILKGQK-----YNQSVDWWSFGVLLYEMLIGQSP-FHGEDEDELFWSICNDTP---HYPRWlTKE 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  275 FNHFISQCLIKDFERRPSVT-----HLLDHPFIKGV 305
Cdd:cd05592   223 AASCLSLLLERNPEKRLGVPecpagDIRDHPFFKTI 258
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
34-303 2.06e-28

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 117.84  E-value: 2.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLihLEIKPAIRNQIIRELQVLHEC-NSPYIVGFYGAFYS-----DGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGllrcGQRLDEAMISYILYGALLGLQHL-HNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd06649    79 SICMEHMDGGSLDQVLKE----AKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTrlRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPL------------------------- 245
Cdd:cd06649   155 IDS--MANSFVGTRSYMSPERLQ-----GTHYSVQSDIWSMGLSLVELAIGRYPIpppdakeleaifgrpvvdgeegeph 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  246 -----------------FDMHPVKTLFK----IPRNPPPTLLHpEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd06649   228 sisprprppgrpvsghgMDSRPAMAIFElldyIVNEPPPKLPN-GVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIK 305
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
37-305 2.18e-28

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 117.66  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKG--TYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLP--NHPNVVKFYGMFykadhCVGGQLW 112
Cdd:cd08226     1 ELQVELGKGfcNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHffRHPNIMTHWTVF-----TEGSWLW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKGLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVdfGVSAQLTS 192
Cdd:cd08226    76 VISPFMAYGSARGLLKTYFPEG--MNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLS--GLSHLYSM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPF---------WMAPEVIaceQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPP 263
Cdd:cd08226   152 VTNGQRSKVVYDFpqfstsvlpWLSPELL---RQDLHGYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQKLKGPPY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  264 TLLH--------------------------------------------PEKWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd08226   229 SPLDifpfpelesrmknsqsgmdsgigesvatssmtrtmtserlqtpsSKTFSPAFHNLVELCLQQDPEKRPSASSLLSH 308

                  ....*.
gi 578803747  300 PFIKGV 305
Cdd:cd08226   309 SFFKQV 314
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
42-265 2.80e-28

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 117.12  E-value: 2.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVY---KVTNKRDGSLAAVKILDPVSDMDEE-----IEAEYNILQFLpNHPNVVKFYGMFYkadhcVGGQLWL 113
Cdd:cd05584     4 LGKGGYGKVFqvrKTTGSDKGKIFAMKVLKKASIVRNQkdtahTKAERNILEAV-KHPFIVDLHYAFQ-----TGGKLYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGsvtELVKGLLRCGQRLdEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd05584    78 ILEYLSGG---ELFMHLEREGIFM-EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR---NPPPTL 265
Cdd:cd05584   154 GTVTHTFCGTIEYMAPEILT-----RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKgklNLPPYL 223
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
36-302 8.66e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 113.80  E-value: 8.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS----DMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAmqkaGMVQRVRNEVEIHCQL-KHPSILELYNYFEDSNY-----V 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLRcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14186    77 YLVLEMCHNGEMSRYLKNRKK---PFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVK-TLFKIPRNpppTLLHPEK 270
Cdd:cd14186   154 MPHEKHFTMCGTPNYISPEIAT-----RSAHGLESDVWSLGCMFYTLLVGRPP-FDTDTVKnTLNKVVLA---DYEMPAF 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14186   225 LSREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
37-314 1.18e-27

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 115.69  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP--VSDMD--EEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLW 112
Cdd:PTZ00263   21 EMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKreILKMKqvQHVAQEKSILMEL-SHPFIVNMMCSFQDEN-----RVY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:PTZ00263   95 FLLEFVVGG---ELFTHLRKAG-RFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 trlRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpppTLLHPeKWC 272
Cdd:PTZ00263  171 ---RTFTLCGTPEYLAPEVIQSK-----GHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG---RLKFP-NWF 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  273 EE-FNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:PTZ00263  239 DGrARDLVKGLLQTDHTKRlgtlkGGVADVKNHPYFHGANWDKLYARY 286
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
42-299 2.00e-27

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 112.58  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDmDEEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvgGQLWLVLELCNGG 121
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDE-QRSFLKEVKLMRRL-SHPNILRFIGVCVKD-----NKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELVKGL---LRCGQRLDEAM-ISYilygallGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV---DFGVSAQLTSTR 194
Cdd:cd14065    74 TLEELLKSMdeqLPWSQRVSLAKdIAS-------GMAYLHSKNIIHRDLNSKNCLVREANRGRNAvvaDFGLAREMPDEK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LR------RNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELgdgdpplfdmhpvktLFKIPRNP---PPTL 265
Cdd:cd14065   147 TKkpdrkkRLTVVGSPYWMAPEMLRGE-----SYDEKVDVFSFGIVLCEI---------------IGRVPADPdylPRTM 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  266 -----------LHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14065   207 dfgldvrafrtLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHH 251
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
32-301 2.88e-27

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 113.37  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVK--ILDPvsdmdEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVGG 109
Cdd:cd14137     2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDK-----RYKNRELQIMRRL-KHPNIVKLKYFFYSSGEKKDE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 -QLWLVLElCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV-KLVDFGvS 187
Cdd:cd14137    76 vYLNLVME-YMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDFG-S 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQltstRLRRNTS----VGTPFWMAPEVIACEQQYDSSydarCDVWSLG-ITAiELGDGDpPLF---------------- 246
Cdd:cd14137   154 AK----RLVPGEPnvsyICSRYYRAPELIFGATDYTTA----IDIWSAGcVLA-ELLLGQ-PLFpgessvdqlveiikvl 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  247 ---------DMHPVKTLFKIPRNPPPTL--LHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14137   224 gtptreqikAMNPNYTEFKFPQIKPHPWekVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
42-299 3.06e-27

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 112.41  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdPVSDM---DEEIEAEYNilqflpnHPNVVKFYGMFykadhcvggqLW-----L 113
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLI-PVEQFkpsDVEIQACFR-------HENIAELYGAL----------LWeetvhL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTElvkGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVkLVDFGVSAQLTST 193
Cdd:cd13995    74 FMEAGEGGSVLE---KLESCGP-MREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTED 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKT----LFKIPRNPPPTLLHPE 269
Cdd:cd13995   149 VYVPKDLRGTEIYMSPEVILCR-----GHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQAPPLEDIAQ 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  270 KWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd13995   224 DCSPAMRELLEAALERNPNHRSSAAELLKH 253
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
40-302 3.37e-27

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 112.44  E-value: 3.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDP---VSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLE 116
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrrGQDCRNEILHEIAVLELCKDCPRVVNLHEVYETRS-----ELILILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGsvtELvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGVSAQL-TS 192
Cdd:cd14106    89 LAAGG---EL-QTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRVIgEG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRntSVGTPFWMAPEVIaceqqydsSYDARC---DVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpppTLLHPE 269
Cdd:cd14106   165 EEIRE--ILGTPDYVAPEIL--------SYEPISlatDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQC---NLDFPE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  270 kwcEEFN-------HFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14106   232 ---ELFKdvsplaiDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
33-300 4.68e-27

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 111.69  E-value: 4.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggq 110
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDkkALKGKEDSLENEIAVLRKI-KHPNIVQLLDIYESKSH----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL-LTTEGGVKLV--DFGVS 187
Cdd:cd14083    76 LYLVMELVTGG---ELFDRIVEKGS-YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyYSPDEDSKIMisDFGLS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLrrNTSVGTPFWMAPEVIAceQQydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRnppptllh 267
Cdd:cd14083   152 KMEDSGVM--STACGTPGYVAPEVLA--QK---PYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILK-------- 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  268 pekwCE-EFN------------HFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14083   217 ----AEyEFDspywddisdsakDFIRHLMEKDPNKRYTCEQALEHP 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
37-307 4.95e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 113.77  E-value: 4.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDmdeEIEA-----EYNILQFLpNHPNVVKFYGMFYKADHCVGGQ 110
Cdd:cd07834     3 ELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNVFDD---LIDAkrilrEIKILRHL-KHENIIGLLDILRPPSPEEFND 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNggsvTELVKgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd07834    79 VYIVTELME----TDLHK-VIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTS--VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLFD-MHPVKTLFKI---------- 257
Cdd:cd07834   154 DPDEDKGFLTeyVVTRWYRAPELLLSSKKYTKA----IDIWSVGCIFAELLTRK-PLFPgRDYIDQLNLIvevlgtpsee 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  258 ------------------PRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHG 307
Cdd:cd07834   229 dlkfissekarnylkslpKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHD 296
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
42-301 4.97e-27

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 111.95  E-value: 4.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdPVSDM-----DEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIV-PKSLLlkphqKEKMSMEIAIHRSL-AHQHVVGFHGFFEDNDF-----VYVVLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd14187    88 LCRRRSLLELHKRR----KALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGER 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVK-TLFKIPRN--PPPTLLHPEKwce 273
Cdd:cd14187   164 KKTLCGTPNYIAPEVLS-----KKGHSFEVDIWSIGCIMYTLLVGKPP-FETSCLKeTYLRIKKNeySIPKHINPVA--- 234
                         250       260
                  ....*....|....*....|....*...
gi 578803747  274 efNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14187   235 --ASLIQKMLQTDPTARPTINELLNDEF 260
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
36-301 8.51e-27

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 111.61  E-value: 8.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA-------EYNILQFLpNHPNVVKFYGMFYkADHCvg 108
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIR----LETEDEGvpstairEISLLKEL-NHPNIVRLLDVVH-SENK-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNggsvTELVKGLLRCGQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVs 187
Cdd:cd07835    73 --LYLVFEFLD----LDLKKYMDSSPLTgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGL- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNT-SVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLFdmhP----VKTLFKI----- 257
Cdd:cd07835   146 ARAFGVPVRTYThEVVTLWYRAPEILLGSKHYSTP----VDIWSVGCIFAEMVTRR-PLF---PgdseIDQLFRIfrtlg 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  258 --------------------PRNPPPTLLHPEKWCEEFNH-FISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07835   218 tpdedvwpgvtslpdykptfPKWARQDLSKVVPSLDEDGLdLLSQMLVYDPAKRISAKAALQHPY 282
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
42-302 8.63e-27

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 110.78  E-value: 8.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlwLVLELCNG 120
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDrEDVRNEIEIMNQL-RHPRLLQLYDAFETPREMV-----LVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELVkgllrcgqrLDEamiSYILYGA---------LLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQ 189
Cdd:cd14103    75 GELFERV---------VDD---DFELTERdcilfmrqiCEGVQYMHKQGILHLDLKPENILCVSRTGnqIKIIDFGLARK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 L-TSTRLRRNtsVGTPFWMAPEVIaceqqydsSYDA---RCDVWSLG-ITAIEL-------GDGDpplfdmhpVKTLFKI 257
Cdd:cd14103   143 YdPDKKLKVL--FGTPEFVAPEVV--------NYEPisyATDMWSVGvICYVLLsglspfmGDND--------AETLANV 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  258 PRNppptllhpeKW---CEEFN-------HFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14103   205 TRA---------KWdfdDEAFDdisdeakDFISKLLVKDPRKRMSAAQCLQHPWL 250
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
477-1003 8.90e-27

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 118.69  E-value: 8.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  477 ILQVNSLVEAFGNSCTAINDNSSRFGKY--LEMMFtptGV------VMGARISEYLLEKSRVIKQAAREK------NFHI 542
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAF---GLhpwefqICGCHISPFLLEKSRVTSERGRESgdqnelNFHI 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  543 FYYIYAGLHhqkKLSDFRLPEEK---------PPRYIADETGRVMHDITSKESYRRQFEAIQHC---FRIIGFTDKEVHS 610
Cdd:cd14894   326 LYAMVAGVN---AFPFMRLLAKElhldgidcsALTYLGRSDHKLAGFVSKEDTWKKDVERWQQVidgLDELNVSPDEQKT 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  611 VYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCI-SPEELQEALTSHCVVTRGETIIRANTVDRAA--D 687
Cdd:cd14894   403 IFKVLSAVLWLGNIELDYREVSGKLVMSSTGALNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEKGQvnH 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  688 VRDAMSKALYGRLFSWIVNRINTLL------------QPDENICSAGGGMNVGILDIFGFENFQRNSFEQLCINianeqi 755
Cdd:cd14894   483 VRDTLARLLYQLAFNYVVFVMNEATkmsalstdgnkhQMDSNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCIN------ 556
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  756 qyYFNQHVFALEQmeyqnegiDAVPVEYEdNRPLL-------DMFL--QKPLGLLALLDEESRFPQATDqtlVDKFEDNL 826
Cdd:cd14894   557 --YLSEKLYAREE--------QVIAVAYS-SRPHLtardsekDVLFiyEHPLGVFASLEELTILHQSEN---MNAQQEEK 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  827 RCKYFWR-------------PKGVE------------LCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLL 881
Cdd:cd14894   623 RNKLFVRniydrnssrlpepPRVLSnakrhtpvllnvLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHF 702
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  882 QQLFSIPLTKTGNLAQTRARITVASSSLpphfSAGKAKVdtlevirhpeettnmkrqtvaSYFRYSLMDLLSKMVVGQPH 961
Cdd:cd14894   703 CRMLNESSQLGWSPNTNRSMLGSAESRL----SGTKSFV---------------------GQFRSHVNVLTSQDDKNMPF 757
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 578803747  962 FVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYS 1003
Cdd:cd14894   758 YFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSS 799
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
36-302 1.11e-26

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 111.76  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYK-VTNKRDGSLAAVKIL---DPVSDMDE-----EIEAEYNILQFLpNHPNVVKFYGMFYKADHC 106
Cdd:cd14096     3 YRLINKIGEGAFSNVYKaVPLRNTGKPVAIKVVrkaDLSSDNLKgssraNILKEVQIMKRL-SHPNIVKLLDFQESDEYY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 vggqlWLVLELCNGGSV-TELVKglLRCgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---------- 175
Cdd:cd14096    82 -----YIVLELADGGEIfHQIVR--LTY---FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivkl 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  176 -----------EGG------------VKLVDFGVSAQLTSTRLRrnTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLG 232
Cdd:cd14096   152 rkadddetkvdEGEfipgvggggigiVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDE-----RYSKKVDMWALG 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  233 ITAIELGDGDPPLFDmHPVKTLFKIPRNPPPTLLHPekWCEEFNH----FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14096   225 CVLYTLLCGFPPFYD-ESIETLTEKISRGDYTFLSP--WWDEISKsakdLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
37-297 1.58e-26

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 110.85  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEE-IEAEYNILQFLpNHPNVVKFYGMFykadhCVGGQLWLV 114
Cdd:cd13996     9 EEIELLGSGGFGSVYKVRNKVDGVTYAIKkIRLTEKSSASEkVLREVKALAKL-NHPNIVRYYTAW-----VEEPPLYIQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTE-LVKGLLRCGQRLDEAMIsyILYGALLGLQHLHNNRIIHRDVKGNNILLTTE-GGVKLVDFG------- 185
Cdd:cd13996    83 MELCEGGTLRDwIDRRNSSSKNDRKLALE--LFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGlatsign 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 --VSAQLTSTRLRRNTS-----VGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELgdgdpplfdMHPVKTLF--- 255
Cdd:cd13996   161 qkRELNNLNNNNNGNTSnnsvgIGTPLYASPEQLDGEN-----YNEKADIYSLGIILFEM---------LHPFKTAMers 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  256 ---------KIPRNppPTLLHPEKWCeefnhFISQCLIKDFERRPSVTHLL 297
Cdd:cd13996   227 tiltdlrngILPES--FKAKHPKEAD-----LIQSLLSKNPEERPSAEQLL 270
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
42-305 1.74e-26

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 110.56  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVY---KVTNKRDGSLAAVKILDPVSDMD-----EEIEAEYNILQFLPNHPNVVKFYGMFyKADhcvgGQLWL 113
Cdd:cd05583     2 LGTGAYGKVFlvrKVGGHDAGKLYAMKVLKKATIVQkaktaEHTMTERQVLEAVRQSPFLVTLHYAF-QTD----AKLHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGsvtELVKGLLRcGQRLDEAMISyiLYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05583    77 ILDYVNGG---ELFTHLYQ-REHFTESEVR--IYIGeiVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTS-VGTPFWMAPEVIaceQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR-----NPPptl 265
Cdd:cd05583   151 PGENDRAYSfCGTIEYMAPEVV---RGGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKrilksHPP--- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  266 lHPEKWCEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGV 305
Cdd:cd05583   225 -IPKTFSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFKGL 268
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
37-238 1.94e-26

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 110.13  E-value: 1.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKIL---DPVSDMDEEIEA-----EYNILQFLPNHPNVVKFYGMFYKADHcvg 108
Cdd:cd13993     3 QLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksGPNSKDGNDFQKlpqlrEIDLHRRVSRHPNIITLHDVFETEVA--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELVKgLLRCGQRLDEaMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG-VKLVDFGVS 187
Cdd:cd13993    80 --IYIVLEYCPNGDLFEAIT-ENRIYVGKTE-LIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGtVKLCDFGLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578803747  188 aqlTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDAR-CDVWSLGITAIEL 238
Cdd:cd13993   156 ---TTEKISMDFGVGSEFYMAPECFDEVGRSLKGYPCAaGDIWSLGIILLNL 204
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
34-301 2.37e-26

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 110.54  E-value: 2.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDpvSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvg 108
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVE--SEDDPVIKKialrEIRMLKQL-KHPNLVNLIEVFRRKR---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd07847    74 -KLHLVFEYCDHTVLNELEKNP----RGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDP---------PLFdmHPVKTLFK-IP 258
Cdd:cd07847   149 ILTGPGDDYTDYVATRWYRAPELLVGDTQYGPP----VDVWAIGCVFAELLTGQPlwpgksdvdQLY--LIRKTLGDlIP 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  259 RN---------------PPPTLLHP--EKWCEEFNH---FISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07847   223 RHqqifstnqffkglsiPEPETREPleSKFPNISSPalsFLKGCLQMDPTERLSCEELLEHPY 285
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
36-302 2.56e-26

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 109.84  E-value: 2.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYN---------------ILQFLPNHPNVVKFYGMF 100
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRlekeisrdirtireaALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  101 YKADHcvggqLWLVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK 180
Cdd:cd14077    83 RTPNH-----YYMLFEYVDGG---QLLDYIISHG-KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSaQLTSTRLRRNTSVGTPFWMAPEVIACeQQYDSsydARCDVWSLGITAIELGDGDPPlFDMHPVKTLF-KIPR 259
Cdd:cd14077   154 IIDFGLS-NLYDPRRLLRTFCGSLYFAAPELLQA-QPYTG---PEVDVWSFGVVLYVLVCGKVP-FDDENMPALHaKIKK 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  260 NpppTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14077   228 G---KVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
34-287 2.84e-26

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 110.60  E-value: 2.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--PVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAipEVIRLKQEqhVHNEKRVLKEV-SHPFIIRLFWTEHDQRF---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGsvtELVKgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05612    76 -LYMLMEYVPGG---ELFS-YLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LtstRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIprnppptLLHPE 269
Cdd:cd05612   151 L---RDRTWTLCGTPEYLAPEVIQ-----SKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKI-------LAGKL 215
                         250
                  ....*....|....*...
gi 578803747  270 KWCEEFNhFISQCLIKDF 287
Cdd:cd05612   216 EFPRHLD-LYAKDLIKKL 232
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
121-303 2.97e-26

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 106.72  E-value: 2.97e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    121 GSVTELVKGLlrcGQRLDEAMISYILYGALLGLQHLHNNRIIHrdvkgnNILLTTEGGVKLvdFGVSAQLTstrlrRNTS 200
Cdd:smart00750    1 VSLADILEVR---GRPLNEEEIWAVCLQCLGALRELHRQAKSG------NILLTWDGLLKL--DGSVAFKT-----PEQS 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747    201 VGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH-----PEKWCE-- 273
Cdd:smart00750   65 RPDPYFMAPEVIQGQ-----SYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADDPrdrsnLEGVSAar 139
                           170       180       190
                    ....*....|....*....|....*....|
gi 578803747    274 EFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:smart00750  140 SFEDFMRLCASRLPQRREAANHYLAHCRAL 169
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
36-313 3.24e-26

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 110.22  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYkADHcvggQL 111
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVR-LDDDDEGVPSsalrEICLLKEL-KHKNIVRLYDVLH-SDK----KL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd07839    75 TLVFEYCD----QDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPV----KTLFKIPRNPpptllH 267
Cdd:cd07839   151 IPVRCYSAEVVTLWYRPPDVLFGAKLYSTS----IDMWSAGCIFAELANAGRPLFPGNDVddqlKRIFRLLGTP-----T 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  268 PEKWceefnhfisqclikdferrPSVTHLLDHPFIKGVHGKVLFLQ 313
Cdd:cd07839   222 EESW-------------------PGVSKLPDYKPYPMYPATTSLVN 248
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
42-238 3.32e-26

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 109.90  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSlaaVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKadhcvGGQLWLVLEL 117
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGE---VMVMKELIRFDEEAQRnflkEVKVMRSL-DHPNVLKFIGVLYK-----DKKLNLITEY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKGL---LRCGQRLDEAMisyilyGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS------- 187
Cdd:cd14154    72 IPGGTLKDVLKDMarpLPWAQRVRFAK------DIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveer 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  188 ----AQLTSTRLR---------RNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL 238
Cdd:cd14154   146 lpsgNMSPSETLRhlkspdrkkRYTVVGNPYWMAPEMLN-----GRSYDEKVDIFSFGIVLCEI 204
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
38-301 3.51e-26

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 109.28  E-value: 3.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLAAVKILD----PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWL 113
Cdd:cd14079     6 LGKTLGVGSFGKVKLAEHELTGHKVAVKILNrqkiKSLDMEEKIRREIQILKLF-RHPHIIRLYEVIETPT-----DIFM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd14079    80 VMEYVSGG---ELFDYIVQKG-RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRnTSVGTPFWMAPEVIaCEQQYDSSydaRCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPTLlhPEKWCE 273
Cdd:cd14079   156 EFLK-TSCGSPNYAAPEVI-SGKLYAGP---EVDVWSCGVILYALLCGSLP-FDDEHIPNLFKKIKSGIYTI--PSHLSP 227
                         250       260
                  ....*....|....*....|....*...
gi 578803747  274 EFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14079   228 GARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
42-301 6.34e-26

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 108.48  E-value: 6.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMD-----EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVI-PHSRVAkphqrEKIVNEIELHRDL-HHKHVVKFSHHFEDAEN-----IYIFLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd14189    82 LCSRKSLAHIWKAR----HTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPTLlhPEKWCEEFN 276
Cdd:cd14189   158 KKTICGTPNYLAPEVL-----LRQGHGPESDVWSLGCVMYTLLCGNPP-FETLDLKETYRCIKQVKYTL--PASLSLPAR 229
                         250       260
                  ....*....|....*....|....*
gi 578803747  277 HFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14189   230 HLLAGILKRNPGDRLTLDQILEHEF 254
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
36-299 7.32e-26

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 108.12  E-value: 7.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNkRDGSLAAVKIL--DPVSDMDE--EIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggql 111
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARD-SSGRLVAIKSIrkDRIKDEQDllHIRREIEIMSSL-NHPHIISVYEVFENSSKIV---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 wLVLELCNGGSVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14161    79 -IVMEYASRGDLYDYISE----RQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRnTSVGTPFWMAPEVIACEQQYDSSYDArcdvWSLGITAIELGDGDPPlFDMHPVKTLFK-----IPRNPPptll 266
Cdd:cd14161   154 QDKFLQ-TYCGSPLYASPEIVNGRPYIGPEVDS----WSLGVLLYILVHGTMP-FDGHDYKILVKqissgAYREPT---- 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  267 HPEKWCeefnHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14161   224 KPSDAC----GLIRWLLMVNPERRATLEDVASH 252
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
34-303 7.98e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 109.05  E-value: 7.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD----PVSDMdEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINtkklSARDH-QKLEREARICRLL-KHPNIVRLHDSISEEGF---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELVkgLLRcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGV 186
Cdd:cd14086    75 -HYLVFDLVTGGELFEDI--VAR--EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKskgAAVKLADFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN----PP 262
Cdd:cd14086   150 AIEVQGDQQAWFGFAGTPGYLSPEVLRKD-----PYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGaydyPS 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  263 PtllhpeKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14086   225 P------EWdtvTPEAKDLINQMLTVNPAKRITAAEALKHPWIC 262
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
38-302 8.55e-26

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 107.86  E-value: 8.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLAAVK------ILDP--VSDMD-EEIEAEYNILQFL--PNHPNVVKFYGMFYKAD-- 104
Cdd:cd14004     4 ILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkerILVDtwVRDRKlGTVPLEIHILDTLnkRSHPNIVKLLDFFEDDEfy 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 ------HCVGGQLWLVLELcnggsvtelvkgllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG 178
Cdd:cd14004    84 ylvmekHGSGMDLFDFIER----------------KPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  179 VKLVDFGVSAQLTSTRLrrNTSVGTPFWMAPEVIACEqqydsSYDAR-CDVWSLGITAIELGDGDPPLFDM-HPVKTLFK 256
Cdd:cd14004   148 IKLIDFGSAAYIKSGPF--DTFVGTIDYAAPEVLRGN-----PYGGKeQDIWALGVLLYTLVFKENPFYNIeEILEADLR 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  257 IPRnppptLLHpekwcEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14004   221 IPY-----AVS-----EDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
36-256 1.11e-25

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 107.47  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKADHCVggql 111
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQdmvrIRREIEIMSSL-NHPHIIRIYEVFENKDKIV---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 wLVLELCNGGsvtELVKGLLRCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14073    78 -IVMEYASGG---ELYDYISER-RRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  192 STRLRRnTSVGTPFWMAPEVIAcEQQYdssYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFK 256
Cdd:cd14073   153 KDKLLQ-TFCGSPLYASPEIVN-GTPY---QGPEVDCWSLGVLLYTLVYGTMP-FDGSDFKRLVK 211
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
42-299 1.16e-25

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 107.20  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKvtNKRDGSLAAVKildpvsDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKAD-HCVggqlwlVLELCNG 120
Cdd:cd14059     1 LGSGAQGAVFL--GKFRGEEVAVK------KVRDEKETDIKHLRKL-NHPNIIKFKGVCTQAPcYCI------LMEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT--STRLrrn 198
Cdd:cd14059    66 GQLYEV----LRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSekSTKM--- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  199 TSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpPPTLLHPEKWCEEFNHF 278
Cdd:cd14059   139 SFAGTVAWMAPEVIRNE-----PCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSN-SLQLPVPSTCPDGFKLL 212
                         250       260
                  ....*....|....*....|.
gi 578803747  279 ISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14059   213 MKQCWNSKPRNRPSFRQILMH 233
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
42-314 1.22e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 108.38  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQfLPNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETmalnEKIILE-KVSSPFIVSLAYAFETKDK-----LCLVLTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGQR-LDEAMIsyILYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLtSTR 194
Cdd:cd05577    75 MNGG---DLKYHIYNVGTRgFSEARA--IFYAAeiICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEF-KGG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR---NPPPTLlhPEKW 271
Cdd:cd05577   149 KKIKGRVGTHGYMAPEVLQKEVAYDFS----VDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRrtlEMAVEY--PDSF 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  272 CEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05577   223 SPEARSLCEGLLQKDPERRlgcrgGSADEVKEHPFFRSLNWQRLEAGM 270
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
42-303 1.23e-25

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 109.63  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIE---AEYNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKALKKdVVLMDDDVEctmVEKRVLSLAWEHPFLTHLFCTFQTKEN-----LFFVMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05619    88 LNGG---DLMFHIQSC-HKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 NTSVGTPFWMAPEVIaCEQQYDSSydarCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPtlLHPEKWCEEFNH 277
Cdd:cd05619   164 STFCGTPDYIAPEIL-LGQKYNTS----VDWWSFGVLLYEMLIGQSP-FHGQDEEELFQSIRMDNP--FYPRWLEKEAKD 235
                         250       260
                  ....*....|....*....|....*..
gi 578803747  278 FISQCLIKDFERRPSVT-HLLDHPFIK 303
Cdd:cd05619   236 ILVKLFVREPERRLGVRgDIRQHPFFR 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
34-318 1.27e-25

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 108.54  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPV-SDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSpLSRDSSLENEIAVLKRI-KHENIVTLEDIYESTTH-----YY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL-LTTEGGVKLV--DFGVSaq 189
Cdd:cd14166    77 LVMQLVSGG---ELFDRILERGV-YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKIMitDFGLS-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 ltstRLRRN----TSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPtl 265
Cdd:cd14166   151 ----KMEQNgimsTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYE-- 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  266 LHPEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFIKG--------VHGKVLFLQKQLAK 318
Cdd:cd14166   220 FESPFWddiSESAKDFIRHLLEKNPSKRYTCEKALSHPWIIGntalhrdiYPSVSEQIQKNFAK 283
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
42-302 1.58e-25

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 108.11  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKIL-------------------------DPVSDMD--EEIEAEYNILQFLpNHPNVV 94
Cdd:cd14200     8 IGKGSYGVVKLAYNESDDKYYAMKVLskkkllkqygfprrppprgskaaqgEQAKPLAplERVYQEIAILKKL-DHVNIV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   95 KFYGMFykaDHCVGGQLWLVLELCNGGSVTELvkgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT 174
Cdd:cd14200    87 KLIEVL---DDPAEDNLYMVFDLLRKGPVMEV-----PSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  175 TEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQydsSYDARC-DVWSLGITAIELGDGDPPLFDMHpVKT 253
Cdd:cd14200   159 DDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQ---SFSGKAlDVWAMGVTLYCFVYGKCPFIDEF-ILA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  254 LFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14200   235 LHNKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
32-303 1.72e-25

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 108.40  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMD-------EEIEAEYNILQFLpNHPNVVKFYGMfYKAD 104
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVD-VAKFTsspglstEDLKREASICHML-KHPHIVELLET-YSSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HcvggQLWLVLELCNGGSVT-ELVKgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVK 180
Cdd:cd14094    78 G----MLYMVFEFMDGADLCfEIVK-RADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLF----DMHPVKTLFK 256
Cdd:cd14094   153 LGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-----YGKPVDVWGCGVILFILLSGCLPFYgtkeRLFEGIIKGK 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  257 IPRNPPptllhpeKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14094   228 YKMNPR-------QWshiSESAKDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
36-301 1.73e-25

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 107.11  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPV----SDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEqvarEGMVEQIKREIAIMKLL-RHPNIVELHEVMATKTK-----I 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAqLT 191
Cdd:cd14663    76 FFVMELVTGG---ELFSKIAK-NGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSA-LS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRR---NTSVGTPFWMAPEVIaCEQQYDSsydARCDVWSLGITAIELGDGDPPlFDMHPVKTLF-KIPRNPPPtllH 267
Cdd:cd14663   151 EQFRQDgllHTTCGTPNYVAPEVL-ARRGYDG---AKADIWSCGVILFVLLAGYLP-FDDENLMALYrKIMKGEFE---Y 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14663   223 PRWFSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
40-301 1.91e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 107.02  E-value: 1.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMD-----EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKII-PHSRVSkphqrEKIDKEIELHRIL-HHKHVVQFYHYFEDKEN-----IYIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd14188    80 LEYCSRRSMAHI----LKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNP----PPTLLHPEK 270
Cdd:cd14188   156 HRRRTICGTPNYLSPEVLN-----KQGHGCESDIWALGCVMYTMLLGRPP-FETTNLKETYRCIREAryslPSSLLAPAK 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  271 wceefnHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14188   230 ------HLIASMLSKNPEDRPSLDEIIRHDF 254
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
36-301 2.34e-25

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 107.51  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEEIEA-EYNILQFLpNHPNVVKFYGMFYKADhcvggQLW 112
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFleSEDDKMVKKIAMrEIKMLKQL-RHENLVNLIEVFRRKK-----RWY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKgllRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd07846    77 LVFEFVDHTVLDDLEK---YPNG-LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIACeqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI--------------- 257
Cdd:cd07846   153 PGEVYTDYVATRWYRAPELLVG----DTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIikclgnliprhqelf 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  258 PRNPP------PTLLHPE-------KWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07846   229 QKNPLfagvrlPEVKEVEplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
71-305 4.29e-25

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 108.11  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   71 SDMDEEIEAEYNILQfLPNHPNVVKfygmfYKADHCVGGQLWLVLELCNGGSVTELVKGLLRCGqrLDEAMISYILYGAL 150
Cdd:cd08227    40 NEMVTFLQGELHVSK-LFNHPNIVP-----YRATFIADNELWVVTSFMAYGSAKDLICTHFMDG--MSELAIAYILQGVL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  151 LGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVdfGVSAQLTSTRLRRNTSVGTPF---------WMAPEVIaceQQYDSS 221
Cdd:cd08227   112 KALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMINHGQRLRVVHDFpkysvkvlpWLSPEVL---QQNLQG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  222 YDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFK------------------------------------------IPR 259
Cdd:cd08227   187 YDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtttipaeeltmkpsrsgansglgesttvstpRPS 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  260 NPPPTlLHP--EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGV 305
Cdd:cd08227   267 NGESS-SHPynRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQI 313
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
34-302 4.36e-25

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 106.97  E-value: 4.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD---------------------------EEIEAEYNILQF 86
Cdd:cd14199     2 NQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqprgpiERVYQEIAILKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   87 LpNHPNVVKFYGMF--YKADHcvggqLWLVLELCNGGSVTELvkgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHR 164
Cdd:cd14199    82 L-DHPNVVKLVEVLddPSEDH-----LYMVFELVKQGPVMEV-----PTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  165 DVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAcEQQYDSSYDArCDVWSLGITAIELGDGDPP 244
Cdd:cd14199   151 DVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLS-ETRKIFSGKA-LDVWAMGVTLYCFVFGQCP 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  245 LFDMHPVKTLFKIPRNPpptLLHPEK--WCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14199   229 FMDERILSLHSKIKTQP---LEFPDQpdISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
36-303 4.62e-25

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 106.89  E-value: 4.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK-I-LDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFykadhCVGG 109
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKkIkLGERKEAKDGINFtalrEIKLLQEL-KHPNIIGLLDVF-----GHKS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd07841    76 NINLVFEFME----TDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI--------PRNP 261
Cdd:cd07841   152 FGSPNRKMTHQVVTRWYRAPELLFGARHYGVG----VDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIfealgtptEENW 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  262 PPTLLHPEKWceEFNHF-------------------ISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd07841   228 PGVTSLPDYV--EFKPFpptplkqifpaasddaldlLQRLLTLNPNKRITARQALEHPYFS 286
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
34-310 5.48e-25

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 106.10  E-value: 5.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEE-----IEAEYNILQFLpNHPNVVKFYGMFYKADhcvg 108
Cdd:cd14117     6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFK-SQIEKEgvehqLRREIEIQSHL-RHPNILRLYNYFHDRK---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd14117    80 -RIYLILEYAPRG---ELYKELQKHG-RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTStrLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPlFD----MHPVKTLFKIPRNPPPT 264
Cdd:cd14117   155 HAPS--LRRRTMCGTLDYLPPEMIE-----GRTHDEKVDLWCIGVLCYELLVGMPP-FEsashTETYRRIVKVDLKFPPF 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  265 LlhpekwCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVL 310
Cdd:cd14117   227 L------SDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSRRVL 266
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
40-302 8.38e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 106.66  E-value: 8.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQfLPNHPNVVKFYGMFYKADHCvggqLWLVLELCN 119
Cdd:cd14170     8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQ-CPHIVRIVDVYENLYAGRKC----LLIVMECLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGVsAQLTSTRLR 196
Cdd:cd14170    83 GGELFSRIQD--RGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGF-AKETTSHNS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKT---LFKIPRNPPPTLLHPEkWCE 273
Cdd:cd14170   160 LTTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgMKTRIRMGQYEFPNPE-WSE 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  274 ---EFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14170   234 vseEVKMLIRNLLKTEPTQRMTITEFMNHPWI 265
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
36-301 1.11e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 105.49  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILdPVSDMDEEIEA----EYNILQFLPNHPNVVKFygmfyKADHCVGGQL 111
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKKV-ALRKLEGGIPNqalrEIKALQACQGHPYVVKL-----RDVFPHGTGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCnGGSVTELVKGLLRcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLT 191
Cdd:cd07832    76 VLVFEYM-LSSLSEVLRDEER---PLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGL-ARLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTS--VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDP--------------------PLFDMH 249
Cdd:cd07832   151 SEEDPRLYShqVATRWYRAPELLYGSRKYDEG----VDLWAVGCIFAELLNGSPlfpgendieqlaivlrtlgtPNEKTW 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  250 P-VKTL---FKI--PRNPPPTL--LHPEKWCEEFNhFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07832   227 PeLTSLpdyNKItfPESKGIRLeeIFPDCSPEAID-LLKGLLVYNPKKRLSAEEALRHPY 285
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
34-257 1.13e-24

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 105.56  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP--VSDMD--EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKqkVVKLKqvEHTLNEKRILQAI-NFPFLVKLEYSFKDNSN---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGsvtELVKGLLRCGqRLDEAMISYilYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd14209    76 -LYMVMEYVPGG---EMFSHLRRIG-RFSEPHARF--YAAqiVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLtstRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI 257
Cdd:cd14209   149 KRV---KGRTWTLCGTPEYLAPEIIL-----SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 210
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
34-305 1.35e-24

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 106.66  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEEIEA-----EYNILQFlPNHPNVVKFYGMFYKADHcvg 108
Cdd:cd05597     1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNK-WEMLKRAETacfreERDVLVN-GDRRWITKLHYAFQDENY--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05597    76 --LYLVMDYYCGGDLLTL---LSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRL-RRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFD----------MHpVKTLFKI 257
Cdd:cd05597   151 KLREDGTvQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAeslvetygkiMN-HKEHFSF 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  258 PrnppptlLHPEKWCEEFNHFISQcLIKDFERR---PSVTHLLDHPFIKGV 305
Cdd:cd05597   230 P-------DDEDDVSEEAKDLIRR-LICSRERRlgqNGIDDFKKHPFFEGI 272
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
36-306 1.60e-24

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 105.47  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVY---KVTNKRDGSLAAVKILDPVSDMD-----EEIEAEYNILQFLPNHPNVVKFYGMFYkadhcV 107
Cdd:cd05613     2 FELLKVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLKKATIVQkaktaEHTRTERQVLEHIRQSPFLVTLHYAFQ-----T 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSV-TELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd05613    77 DTKLHLILDYINGGELfTHLSQR-----ERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSV-GTPFWMAPEVIaceQQYDSSYDARCDVWSLGITAIELGDGDPPLF----DMHPVKTLFKIPRNP 261
Cdd:cd05613   152 SKEFLLDENERAYSFcGTIEYMAPEIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSE 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  262 PPtllHPEKWCEEFNHFISQCLIKDFERR----PS-VTHLLDHPFIKGVH 306
Cdd:cd05613   229 PP---YPQEMSALAKDIIQRLLMKDPKKRlgcgPNgADEIKKHPFFQKIN 275
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
40-301 2.06e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 103.91  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDG-SLAAVKILD-------PVSDMDEEIEaeynILQFLpNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGArEVVAVKCVSksslnkaSTENLLTEIE----LLKKL-KHPHIVELKDFQWDEEH-----I 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTelvkGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV--KLVDFGVsAQ 189
Cdd:cd14121    71 YLIMEYCSGGDLS----RFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGF-AQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNTSVGTPFWMAPEVIACeqqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPP---PTLL 266
Cdd:cd14121   146 HLKPNDEAHSLRGSPLYMAPEMILK-----KKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPieiPTRP 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  267 HPEKWCEEfnhFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14121   221 ELSADCRD---LLLRLLQRDPDRRISFEEFFAHPF 252
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
39-233 2.36e-24

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 105.46  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIeaeyNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVLELC 118
Cdd:cd14092    11 EEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREV----QLLRLCQGHPNIVKLHEVFQDELH-----TYLVMELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGsvtELVKgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVsAQLTSTRL 195
Cdd:cd14092    82 RGG---ELLE-RIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGF-ARLKPENQ 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 578803747  196 RRNTSVGTPFWMAPEVIAcEQQYDSSYDARCDVWSLGI 233
Cdd:cd14092   157 PLKTPCFTLPYAAPEVLK-QALSTQGYDESCDLWSLGV 193
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
33-302 2.94e-24

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 103.92  E-value: 2.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEII-ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNIlQFLPNHPNVVKFYGMFYKADHCvggqL 111
Cdd:cd14172     2 TDDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRA-SGGPHIVHILDVYENMHHGKRC----L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGVSA 188
Cdd:cd14172    77 LIIMECMEGGELFSRIQE--RGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QlTSTRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFD-----MHP-VKTLFKIPRNPP 262
Cdd:cd14172   155 E-TTVQNALQTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGFPPFYSntgqaISPgMKRRIRMGQYGF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  263 PtllHPEkW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14172   229 P---NPE-WaevSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
42-302 4.45e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 103.55  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSL-AAVKILDP--VSDMDEEIEAEYNILQFLpNHPNVVKFYGmFYKADHCVggqlWLVLELC 118
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKHDLeVAVKCINKknLAKSQTLLGKEIKILKEL-KHENIVALYD-FQEIANSV----YLVMEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELVKGLlRCgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---------VKLVDFGVSAQ 189
Cdd:cd14202    84 NGGDLADYLHTM-RT---LSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnnirIKIADFGFARY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRnTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHP--VKTLFKIPRNPPPTLlh 267
Cdd:cd14202   160 LQNNMMAA-TLCGSPMYMAPEVIMSQH-----YDAKADLWSIGTIIYQCLTGKAPFQASSPqdLRLFYEKNKSLSPNI-- 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14202   232 PRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
37-300 5.25e-24

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 103.27  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLA-AVKILDP----VSDMDEEIEaEYNILQFL--PNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd14052     3 ANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPnyagAKDRLRRLE-EVSILRELtlDGHDNIVQLIDSWEYHGH---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELVK--GLLrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd14052    78 -LYIQTELCENGSLDVFLSelGLL---GRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTsvGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIE----------------LGDGD----PPLFD 247
Cdd:cd14052   154 TVWPLIRGIERE--GDREYIAPEILS-----EHMYDKPADIFSLGLILLEaaanvvlpdngdawqkLRSGDlsdaPRLSS 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578803747  248 MHPVKTlFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14052   227 TDLHSA-SSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
36-314 5.85e-24

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 104.62  E-value: 5.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVY---KVTNKRDGSLAAVKILDPVS-----DMDEEIEAEYNILQFLPNHPNVVKFYGMFYkadhcV 107
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMKVLRKAAlvqkaKTVEHTRTERNVLEHVRQSPFLVTLHYAFQ-----T 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd05614    77 DAKLHLILDYVSGG---ELFTHLYQ-RDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTS-VGTPFWMAPEVIaceqQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR-----NP 261
Cdd:cd05614   153 KEFLTEEKERTYSfCGTIEYMAPEII----RGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRrilkcDP 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  262 P-PTLLHPEKwceefNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05614   229 PfPSFIGPVA-----RDLLQKLLCKDPKKRlgagpQGAQEIKEHPFFKGLDWEALALRK 282
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
42-296 5.86e-24

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 103.11  E-value: 5.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdpvSDMDEEIE----AEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKEL---IRFDEETQrtflKEVKVMRCL-EHPNVLKFIGVLYKDK-----RLNFITEY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKGL---LRCGQRLDEAMisyilyGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS------- 187
Cdd:cd14221    72 IKGGTLRGIIKSMdshYPWSQRVSFAK------DIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdek 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 -------AQLTSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIEL---GDGDPplfDMHPVKTLFKI 257
Cdd:cd14221   146 tqpeglrSLKKPDRKKRYTVVGNPYWMAPEMI-----NGRSYDEKVDVFSFGIVLCEIigrVNADP---DYLPRTMDFGL 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  258 ----------PRNPPPTllhpekwceeFNHFISQCLIKDFERRPSVTHL 296
Cdd:cd14221   218 nvrgfldrycPPNCPPS----------FFPIAVLCCDLDPEKRPSFSKL 256
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
40-300 8.33e-24

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 102.37  E-value: 8.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEaeyniLQFL-PNHPNVVKF---YGMFYKADHCvggqLWLVL 115
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVE-----LHWRaSGCPHIVRIidvYENTYQGRKC----LLVVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELvkgLLRCGQRLDEAM----ISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVsA 188
Cdd:cd14089    78 ECMEGG---EL---FSRIQERADSAFtereAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGF-A 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPV---KTLFKIPRNPPPTL 265
Cdd:cd14089   151 KETTTKKSLQTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGYPPFYSNHGLaisPGMKKRIRNGQYEF 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  266 LHPEkW---CEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14089   226 PNPE-WsnvSEEAKDLIRGLLKTDPSERLTIEEVMNHP 262
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
34-304 8.86e-24

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 102.41  E-value: 8.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIakKALEGKETSIENEIAVLHKI-KHPNIVALDDIYES-----GGHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELV--KGLLrcgqrlDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL---LTTEGGVKLVDFGV 186
Cdd:cd14167    77 YLIMQLVSGGELFDRIveKGFY------TERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SaQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR-----NP 261
Cdd:cd14167   151 S-KIEGSGSVMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKaeyefDS 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  262 PptllHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKG 304
Cdd:cd14167   225 P----YWDDISDSAKDFIQHLMEKDPEKRFTCEQALQHPWIAG 263
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
40-310 1.06e-23

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 103.49  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIE---AEYNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVL 115
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKdVVLIDDDVEctmVEKRVLALAWENPFLTHLYCTFQTKEH-----LFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELV--KGllrcgqRLDeaMISYILYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05620    76 EFLNGGDLMFHIqdKG------RFD--LYRATFYAAeiVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPtllHPEKW 271
Cdd:cd05620   148 FGDNRASTFCGTPDYIAPEILQGLK-----YTFSVDWWSFGVLLYEMLIGQSP-FHGDDEDELFESIRVDTP---HYPRW 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  272 CEEFNHFIsqcLIKDFERRPS-----VTHLLDHPFIKGVHGKVL 310
Cdd:cd05620   219 ITKESKDI---LEKLFERDPTrrlgvVGNIRGHPFFKTINWTAL 259
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
36-254 1.11e-23

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 101.83  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA---EYNILQFLpNHPNVVKFYGMFYKADhcvggQLW 112
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKlfrEVRIMKIL-NHPNIVKLFEVIETEK-----TLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGallgLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd14072    76 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSA----VQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTP 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  193 -TRLrrNTSVGTPFWMAPEVIAcEQQYDSSydaRCDVWSLGITAIELGDGDPPlFDMHPVKTL 254
Cdd:cd14072   152 gNKL--DTFCGSPPYAAPELFQ-GKKYDGP---EVDVWSLGVILYTLVSGSLP-FDGQNLKEL 207
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
39-305 1.22e-23

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 103.47  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEE-----IEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:cd05574     6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDK-EEMIKRnkvkrVLTEREILATL-DHPFLPTLYASFQTSTH-----LCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKglLRCGQRLDEAMISYilYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05574    79 VMDYCPGGELFRLLQ--KQPGKRLPEEVARF--YAAevLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 ST-RLRR----------------------------NTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGD 242
Cdd:cd05574   155 VTpPPVRkslrkgsrrssvksieketfvaepsarsNSFVGTEEYIAPEVIK-----GDGHGSAVDWWTLGILLYEMLYGT 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  243 PPLFDMHPVKTLFKIPRNPpptLLHPEKW--CEEFNHFISQCLIKDFERR----PSVTHLLDHPFIKGV 305
Cdd:cd05574   230 TPFKGSNRDETFSNILKKE---LTFPESPpvSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFRGV 295
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
42-305 1.27e-23

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 103.45  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIEA---EYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLKKdVILQDDDVECtmtEKRILSLARNHPFLTQLYCCFQTPD-----RLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05590    78 VNGG---DLMFHIQKS-RRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 NTSVGTPFWMAPEVIAcEQQYDSSydarCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNppPTLLHPEKWCEEFNH 277
Cdd:cd05590   154 STFCGTPDYIAPEILQ-EMLYGPS----VDWWAMGVLLYEMLCGHAP-FEAENEDDLFEAILN--DEVVYPTWLSQDAVD 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  278 FISQCLIKDFERRPSVTHL------LDHPFIKGV 305
Cdd:cd05590   226 ILKAFMTKNPTMRLGSLTLggeeaiLRHPFFKEL 259
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
38-299 1.29e-23

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 102.37  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPvSDMDEEI---EAEYnilQFLPNHPNVVKFYgmfykaDHCVGGQ--- 110
Cdd:cd13986     4 IQRLLGEGGFSFVYLVEDLSTGRLYALKkILCH-SKEDVKEamrEIEN---YRLFNHPNILRLL------DSQIVKEagg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 ---LWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRII---HRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd13986    74 kkeVYLLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 G----VSAQLTSTRLRRNTSV-----GTPFWMAPEVIACEQQydSSYDARCDVWSLGITAIELGDGDPPlFDMHPVK--- 252
Cdd:cd13986   154 GsmnpARIEIEGRREALALQDwaaehCTMPYRAPELFDVKSH--CTIDEKTDIWSLGCTLYALMYGESP-FERIFQKgds 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747  253 -------TLFKIPRNPPptllhpekWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd13986   231 lalavlsGNYSFPDNSR--------YSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
42-306 1.32e-23

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 102.03  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMD--EEIEAEYNILQFLPNHPNVVKFYG--MFYKadhcvGGQL--WLVL 115
Cdd:cd13985     8 LGEGGFSYVYLAHDVNTGRRYALKRMY-FNDEEqlRVAIKEIEIMKRLCGHPNIVQYYDsaILSS-----EGRKevLLLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCnGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLH--NNRIIHRDVKGNNILLTTEGGVKLVDFGvSA----- 188
Cdd:cd13985    82 EYC-PGSLVDILEK--SPPSPLSEEEVLRIFYQICQAVGHLHsqSPPIIHRDIKIENILFSNTGRFKLCDFG-SAttehy 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTR--------LRRNTsvgTPFWMAPEVI-------ACEQQydssydarcDVWSLGITAIELGDGDPPLFDMHPVKT 253
Cdd:cd13985   158 PLERAEevniieeeIQKNT---TPMYRAPEMIdlyskkpIGEKA---------DIWALGCLLYKLCFFKLPFDESSKLAI 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  254 L---FKIPRNPpptllhpeKWCEEFNHFISQCLIKDFERRPSVTHLLDhpFIKGVH 306
Cdd:cd13985   226 VagkYSIPEQP--------RYSPELHDLIRHMLTPDPAERPDIFQVIN--IITKDT 271
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-303 1.75e-23

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 104.31  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   16 LFHYNPMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFlPNHP 91
Cdd:cd05621    34 LNRYEKIVNKIRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAffweERDIMAF-ANSP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   92 NVVKFYGMFYKADHcvggqLWLVLELCNGGSVTELVKGLlrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNI 171
Cdd:cd05621   113 WVVQLFCAFQDDKY-----LYMVMEYMPGGDLVNLMSNY-----DVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  172 LLTTEGGVKLVDFGVSAQLTSTRLRR-NTSVGTPFWMAPEVIAcEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHP 250
Cdd:cd05621   183 LLDKYGHLKLADFGTCMKMDETGMVHcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSL 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  251 VKTLFKIpRNPPPTLLHPE--KWCEEFNHFISQCLIKDFER--RPSVTHLLDHPFIK 303
Cdd:cd05621   262 VGTYSKI-MDHKNSLNFPDdvEISKHAKNLICAFLTDREVRlgRNGVEEIKQHPFFR 317
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
42-302 1.76e-23

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 101.47  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPV---SDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVLELC 118
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKKINREkagSSAVKLLEREVDILKHV-NHAHIIHLEEVFETPK-----RMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELvkgLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG-------GVKLVDFGVSAQ-- 189
Cdd:cd14097    83 EDGELKEL---LLRKGF-FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQky 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 -LTSTRLRrnTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPTLLHp 268
Cdd:cd14097   159 gLGEDMLQ--ETCGTPIYMAPEVISAH-----GYSQQCDIWSIGVIMYMLLCGEPP-FVAKSEEKLFEEIRKGDLTFTQ- 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578803747  269 EKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14097   230 SVWqsvSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
42-305 2.29e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 102.48  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVY---KVTNKRDGSLAAVKILDP----VSDMdEEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvgGQLWLV 114
Cdd:cd05582     3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLKKatlkVRDR-VRTKMERDILADV-NHPFIVKLHYAFQTE-----GKLYLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSV-TELVKGLLrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 193
Cdd:cd05582    76 LDFLRGGDLfTRLSKEVM-----FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNP--PPTLLHPEkw 271
Cdd:cd05582   151 EKKAYSFCGTVEYMAPEVVN-----RRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKlgMPQFLSPE-- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  272 ceefnhfiSQCLIKD-FERRPS---------VTHLLDHPFIKGV 305
Cdd:cd05582   224 --------AQSLLRAlFKRNPAnrlgagpdgVEEIKRHPFFATI 259
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
39-246 3.14e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 102.35  E-value: 3.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDP--VSDMDEE--IEAEYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKkvILNRKEQkhIMAERNVLLKNVKHPFLVGLHYSFQTTD-----KLYFV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGsvtELVKGLLRcGQRLDEAMISYilYGALLG--LQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd05604    76 LDFVNGG---ELFFHLQR-ERSFPEPRARF--YAAEIAsaLGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGIS 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIAcEQQYDSSydarCDVWSLGITAIELGDGDPPLF 246
Cdd:cd05604   150 NSDTTTTFCGTPEYLAPEVIR-KQPYDNT----VDWWCLGSVLYEMLYGLPPFY 198
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
41-246 3.84e-23

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 102.01  E-value: 3.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   41 TIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD----EEIEAEYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLE 116
Cdd:cd05575     2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKrnevKHIMAERNVLLKNVKHPFLVGLHYSFQTKD-----KLYFVLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGsvtELVKGLLRcGQRLDEAMISYilYGALLG--LQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd05575    77 YVNGG---ELFFHLQR-ERHFPEPRARF--YAAEIAsaLGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPS 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578803747  195 LRRNTSVGTPFWMAPEVIAcEQQYDSSydarCDVWSLGITAIELGDGDPPLF 246
Cdd:cd05575   151 DTTSTFCGTPEYLAPEVLR-KQPYDRT----VDWWCLGAVLYEMLYGLPPFY 197
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-303 4.19e-23

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 103.55  E-value: 4.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   16 LFHYNPMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFlPNHP 91
Cdd:cd05622    55 LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffweERDIMAF-ANSP 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   92 NVVKFYGMFYKADHcvggqLWLVLELCNGGSVTELVKGLlrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNI 171
Cdd:cd05622   134 WVVQLFYAFQDDRY-----LYMVMEYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNM 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  172 LLTTEGGVKLVDFGVSAQLTSTRLRR-NTSVGTPFWMAPEVIAcEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHP 250
Cdd:cd05622   204 LLDKSGHLKLADFGTCMKMNKEGMVRcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSL 282
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  251 VKTLFKIpRNPPPTLLHPE--KWCEEFNHFISQCLIKDFER--RPSVTHLLDHPFIK 303
Cdd:cd05622   283 VGTYSKI-MNHKNSLTFPDdnDISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFK 338
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
33-302 4.65e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 101.24  E-value: 4.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS-DMDEEIEaeynILQFLPNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd14178     2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKrDPSEEIE----ILLRYGQHPNIITLKDVYDD-----GKFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRcgQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGV 186
Cdd:cd14178    73 YLVMELMRGG---ELLDRILR--QKcFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGnpesIRICDFGF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTSVGTPFWMAPEVIacEQQydsSYDARCDVWSLGITAIELGDGDPPLF---DMHPVKTLFKIPRNppP 263
Cdd:cd14178   148 AKQLRAENGLLMTPCYTANFVAPEVL--KRQ---GYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSG--K 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  264 TLLHPEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14178   221 YALSGGNWdsiSDAAKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
36-246 4.99e-23

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 100.81  E-value: 4.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL-DPVSDMDE-----EIEAeyniLQFLPNHPNVVKFYGMFYKADHcvgG 109
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMkKHFKSLEQvnnlrEIQA----LRRLSPHPNILRLIEVLFDRKT---G 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGgSVTELVKGLLRCgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEgGVKLVDFGvSAQ 189
Cdd:cd07831    74 RLALVFELMDM-NLYELIKGRKRP---LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG-SCR 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  190 LTSTRLRRNTSVGTPFWMAPEVIACeqqyDSSYDARCDVWSLG-----ITAIElgdgdpPLF 246
Cdd:cd07831   148 GIYSKPPYTEYISTRWYRAPECLLT----DGYYGPKMDIWAVGcvffeILSLF------PLF 199
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
36-301 5.41e-23

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 99.96  E-value: 5.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVL 115
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARL-SHRRLTCLLDQFETRK-----TLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCnggSVTELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT--TEGGVKLVDFGVSAQLTST 193
Cdd:cd14107    78 ELC---SSEELLDRLFLKGV-VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVspTREDIKICDFGFAQEITPS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRnTSVGTPFWMAPEVIaceQQydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN----PPPTLLHPE 269
Cdd:cd14107   154 EHQF-SKYGSPEFVAPEIV---HQ--EPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGvvswDTPEITHLS 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  270 kwcEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14107   228 ---EDAKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
38-305 7.00e-23

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 101.88  E-value: 7.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS----DMDEEIEAEYNILQfLPNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:cd05610     8 IVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADminkNMVHQVQAERDALA-LSKSPFIVHLYYSLQSANN-----VYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS------ 187
Cdd:cd05610    82 VMEYLIGGDV----KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 ------------------------AQL----------TSTRLRRNTSV-------------GTPFWMAPEVIaceqqYDS 220
Cdd:cd05610   158 elnmmdilttpsmakpkndysrtpGQVlslisslgfnTPTPYRTPKSVrrgaarvegerilGTPDYLAPELL-----LGK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  221 SYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd05610   233 PHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312

                  ....*
gi 578803747  301 FIKGV 305
Cdd:cd05610   313 LFHGV 317
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
31-302 7.54e-23

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 100.00  E-value: 7.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIET--IGKGTYGKVYKVTNKRDGSLAAVKILDPV---SDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADH 105
Cdd:cd14198     3 DNFNNFYILTSkeLGRGKFAVVRQCISKSTGQEYAAKFLKKRrrgQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 CVggqlwLVLELCNGGSVTELVkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---EGGVKLV 182
Cdd:cd14198    83 II-----LILEYAAGGEIFNLC--VPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDIKIV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQL-TSTRLRRntSVGTPFWMAPEVIaceqQYDSSYDArCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRnp 261
Cdd:cd14198   156 DFGMSRKIgHACELRE--IMGTPEYLAPEIL----NYDPITTA-TDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQ-- 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  262 pptlLHPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14198   227 ----VNVDYSEETFSSvsqlatdFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
42-244 9.72e-23

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 100.64  E-value: 9.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIE---AEYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLKKdVILQDDDVDctmTEKRILALAAKHPFLTALHSCFQTKD-----RLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05591    78 VNGG---DLMFQIQR-ARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  198 NTSVGTPFWMAPEVIAcEQQYDSSydarCDVWSLGITAIELGDGDPP 244
Cdd:cd05591   154 TTFCGTPDYIAPEILQ-ELEYGPS----VDWWALGVLMYEMMAGQPP 195
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
36-300 9.85e-23

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 99.32  E-value: 9.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmIENEVAILRRV-KHPNIVQLIEEYDTDTE-----LYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKGLLRCGQRLDEAMIsYILYGALlglQHLHNNRIIHRDVKGNNILLTTEG----GVKLVDFGVSAQ 189
Cdd:cd14095    76 VMELVKGGDLFDAITSSTKFTERDASRMV-TDLAQAL---KYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLrrnTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLG-ITAIELGdGDPP----------LFDmHPVKTLFKIp 258
Cdd:cd14095   152 VKEPLF---TVCGTPTYVAPEILA-----ETGYGLKVDIWAAGvITYILLC-GFPPfrspdrdqeeLFD-LILAGEFEF- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  259 rnPPPTllhpekW---CEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14095   221 --LSPY------WdniSDSAKDLISRMLVVDPEKRYSAGQVLDHP 257
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
36-302 1.06e-22

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 98.99  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDE------EIEAEYNILqflpnHPNVVKFYGMFYKADHcvgg 109
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDlprvktEIEALKNLS-----HQHICRLYHVIETDNK---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGsvtELVKGLLRcGQRL--DEA------MISYILYgallglqhLHNNRIIHRDVKGNNILLTTEGGVKL 181
Cdd:cd14078    76 -IFMVLEYCPGG---ELFDYIVA-KDRLseDEArvffrqIVSAVAY--------VHSQGYAHRDLKPENLLLDEDQNLKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  182 VDFGVSAQLTS-TRLRRNTSVGTPFWMAPEVIACEQQYDSsydaRCDVWSLGITAIELGDGDPPlFDMHPVKTLF-KIPR 259
Cdd:cd14078   143 IDFGLCAKPKGgMDHHLETCCGSPAYAAPELIQGKPYIGS----EADVWSMGVLLYALLCGFLP-FDDDNVMALYrKIQS 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  260 N--PPPTLLHPEKwceefNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14078   218 GkyEEPEWLSPSS-----KLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
40-292 1.10e-22

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 99.38  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKrdGSLAAVKILDPVSD---MDEEIEAEYNILQFlpNHPNVVKFYGMFYKADHCVGGQLwlVLE 116
Cdd:cd13979     9 EPLGSGGFGSVYKATYK--GETVAVKIVRRRRKnraSRQSFWAELNAARL--RHENIVRVLAAETGTDFASLGLI--IME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTelvkgllrcgQRLDEAMISYILYGALL-------GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd13979    83 YCGNGTLQ----------QLIYEGSEPLPLAHRILisldiarALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTR---LRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVkTLFKI------PRN 260
Cdd:cd13979   153 LGEGNevgTPRSHIGGTYTYRAPELLKGE-----RVTPKADIYSFGITLWQMLTRELPYAGLRQH-VLYAVvakdlrPDL 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  261 PPPTLLHPEKWCEEfnhFISQCLIKDFERRPS 292
Cdd:cd13979   227 SGLEDSEFGQRLRS---LISRCWSAQPAERPN 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
41-302 1.15e-22

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 99.08  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   41 TIGKGTYGKVYKVTNKRDGSLAAVKILD----PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvgGQLWLVLE 116
Cdd:cd14165     8 NLGEGSYAKVKSAYSERLKCNVAIKIIDkkkaPDDFVEKFLPRELEILARL-NHKSIIKTYEIFETSD----GKVYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKgllrCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd14165    83 LGVQGDLLEFIK----LRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 R----NTSVGTPFWMAPEVIAceqqyDSSYDARC-DVWSLGITAIELGDGDPPlFDMHPVKTLFKIP-----RNPPPTLL 266
Cdd:cd14165   159 RivlsKTFCGSAAYAAPEVLQ-----GIPYDPRIyDIWSLGVILYIMVCGSMP-YDDSNVKKMLKIQkehrvRFPRSKNL 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  267 HPEkwCEEfnhFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14165   233 TSE--CKD---LIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
42-292 1.29e-22

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 98.66  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVKILDPVSDMdEEIEAEYNILQFLpNHPNVVKFYGMfykadhCVGGQLW-LVLELCNG 120
Cdd:cd14058     1 VGRGSFGVVCKARWR--NQIVAVKIIESESEK-KAFEVEVRQLSRV-DHPNIIKLYGA------CSNQKPVcLVMEYAEG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELVKGLLRCGQRLDEAMISYILYGALlGLQHLHN---NRIIHRDVKGNNILLTTEGGV-KLVDFGVSAQLtSTRLR 196
Cdd:cd14058    71 GSLYNVLHGKEPKPIYTAAHAMSWALQCAK-GVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDI-STHMT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTsvGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL--------GDGDPPLFDMHPVKTLFKiprnpPPTLLHP 268
Cdd:cd14058   149 NNK--GSAAWMAPEVFE-----GSKYSEKCDVFSWGIILWEVitrrkpfdHIGGPAFRIMWAVHNGER-----PPLIKNC 216
                         250       260
                  ....*....|....*....|....
gi 578803747  269 EKWCEEfnhFISQCLIKDFERRPS 292
Cdd:cd14058   217 PKPIES---LMTRCWSKDPEKRPS 237
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
37-302 1.34e-22

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 100.31  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFL-----PNHPNVVKFYGMFYKADH-CVggq 110
Cdd:cd14210    16 EVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLndndpDDKHNIVRYKDSFIFRGHlCI--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 lwlVLEL--CNggsVTELVKglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGV 186
Cdd:cd14210    93 ---VFELlsIN---LYELLK--SNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSksSIKVIDFGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLrrnTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDP--P-------------LFDMHPV 251
Cdd:cd14210   165 SCFEGEKVY---TYIQSRFYRAPEVI-----LGLPYDTAIDMWSLGCILAELYTGYPlfPgeneeeqlacimeVLGVPPK 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  252 KTLFKIPR---------NPPPTLLHPEKW---------------CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14210   237 SLIDKASRrkkffdsngKPRPTTNSKGKKrrpgskslaqvlkcdDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
42-246 1.55e-22

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 100.04  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKeqnhIMAERNVLLKNLKHPFLVGLHYSFQTSE-----KLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05603    78 VNGG---ELFFHLQR-ERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  198 NTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLF 246
Cdd:cd05603   154 STFCGTPEYLAPEVLRKE-----PYDRTVDWWCLGAVLYEMLYGLPPFY 197
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
36-301 1.57e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 99.12  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA-------EYNILQFLpNHPNVVKFYGMFYKADhcvg 108
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIR----LDTETEGvpstairEISLLKEL-NHPNIVKLLDVIHTEN---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCNggsvTELVKGLLRC-GQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVs 187
Cdd:cd07860    73 -KLYLVFEFLH----QDLKKFMDASaLTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGL- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNT-SVGTPFWMAPEVIACEQQYDSSydarCDVWSLG------ITAIELGDGDPplfdmhPVKTLFKIPRN 260
Cdd:cd07860   147 ARAFGVPVRTYThEVVTLWYRAPEILLGCKYYSTA----VDIWSLGcifaemVTRRALFPGDS------EIDQLFRIFRT 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  261 ---------PPPTLLhPE------KWC-EEFNHFI-----------SQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07860   217 lgtpdevvwPGVTSM-PDykpsfpKWArQDFSKVVppldedgrdllSQMLHYDPNKRISAKAALAHPF 283
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
34-305 1.57e-22

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 102.01  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEEIEA-----EYNIL-----QFlpnhpnVVKFYGMFYKA 103
Cdd:cd05624    72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNK-WEMLKRAETacfreERNVLvngdcQW------ITTLHYAFQDE 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  104 DHcvggqLWLVLELCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd05624   145 NY-----LYLVMDYYVGGDLLTL---LSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLAD 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQLTST-RLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI----P 258
Cdd:cd05624   217 FGSCLKMNDDgTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnheE 296
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  259 RNPPPTllHPEKWCEEFNHFIsQCLIKDFERRPSVTHLLD---HPFIKGV 305
Cdd:cd05624   297 RFQFPS--HVTDVSEEAKDLI-QRLICSRERRLGQNGIEDfkkHAFFEGL 343
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
34-257 1.80e-22

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 99.22  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA-------EYNILQFLpNHPNVVKFYGMFYKADHc 106
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLK----MEKEKEGfpitslrEINILLKL-QHPNIVTVKEVVVGSNL- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 vgGQLWLVLELcnggsVTELVKGLL-RCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd07843    79 --DKIYMVMEY-----VEHDLKSLMeTMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFG 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  186 VSAQLTSTrLRRNTS-VGTPFWMAPEVIACEQQydssYDARCDVWSLGITAIELGDGDpPLFDMH-PVKTLFKI 257
Cdd:cd07843   152 LAREYGSP-LKPYTQlVVTLWYRAPELLLGAKE----YSTAIDMWSVGCIFAELLTKK-PLFPGKsEIDQLNKI 219
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
36-302 1.84e-22

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 98.23  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDK-SQLDEEnlkkIYREVQIMKML-NHPHIIKLYQVMETKD-----ML 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14071    75 YLVTEYASNGEIFDY----LAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLrRNTSVGTPFWMAPEVIAcEQQYDSSydaRCDVWSLGITAIELGDGDPPlFDMHPVKTL--------FKIPrnppp 263
Cdd:cd14071   151 PGEL-LKTWCGSPPYAAPEVFE-GKEYEGP---QLDIWSLGVVLYVLVCGALP-FDGSTLQTLrdrvlsgrFRIP----- 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  264 tlLHPEKWCEefnHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14071   220 --FFMSTDCE---HLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
42-299 2.01e-22

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 98.57  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVKIL--DPVSDMD---EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd14146     2 IGVGGFGKVYRATWK--GQEVAVKAArqDPDEDIKataESVRQEAKLFSML-RHPNIIKLEGVCLEEPN-----LCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGL-----LRCGQRLDEAMISYILYGALLGLQHLHNNR---IIHRDVKGNNILLTTE--------GGVK 180
Cdd:cd14146    74 FARGGTLNRALAAAnaapgPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddicnKTLK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSAQLTSTRlrRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN 260
Cdd:cd14146   154 ITDFGLAREWHRTT--KMSAAGTYAWMAPEVIK-----SSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVN 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  261 pPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14146   227 -KLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
42-298 2.12e-22

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 98.48  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILdpvSDMDEEIE----AEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKEL---IRCDEETQktflTEVKVMRSL-DHPNVLKFIGVLYKDK-----RLNLLTEF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKGLLRC--GQRLDEAMisyilyGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR- 194
Cdd:cd14222    72 IEGGTLKDFLRADDPFpwQQKVSFAK------GIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKk 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 -------------LRRN------TSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL-----GDGD--PPLFDM 248
Cdd:cd14222   146 kpppdkpttkkrtLRKNdrkkryTVVGNPYWMAPEMLN-----GKSYDEKVDIFSFGIVLCEIigqvyADPDclPRTLDF 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578803747  249 H-PVKTLFK--IPRNPPPTllhpekwceeFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd14222   221 GlNVRLFWEkfVPKDCPPA----------FFPLAAICCRLEPDSRPAFSKLED 263
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
36-246 2.26e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 98.63  E-value: 2.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS----DMDEEIEAEYNILQFLPNhPNVVKFYGMFYKADHcvggqL 111
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNlilrNQIQQVFVERDILTFAEN-PFVVSMYCSFETKRH-----L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS---- 187
Cdd:cd05609    76 CMVMEYVEGGDCATLLKNI----GPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkigl 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 ----AQLTSTRLRRNTS-------VGTPFWMAPEVIAceQQydsSYDARCDVWSLGITAIELGDGDPPLF 246
Cdd:cd05609   152 msltTNLYEGHIEKDTRefldkqvCGTPEYIAPEVIL--RQ---GYGKPVDWWAMGIILYEFLVGCVPFF 216
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
33-325 2.31e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 100.09  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS-DMDEEIEaeynILQFLPNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd14176    18 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKrDPTEEIE----ILLRYGQHPNIITLKDVYDD-----GKYV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVS 187
Cdd:cd14176    89 YVVTELMKGG---ELLDKILR-QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpesIRICDFGFA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLF---DMHPVKTLFKIPRNPPPt 264
Cdd:cd14176   165 KQLRAENGLLMTPCYTANFVAPEVLE-----RQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFS- 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  265 lLHPEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFIkgVHGKVLfLQKQLAKvlQDQKH 325
Cdd:cd14176   239 -LSGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI--VHWDQL-PQYQLNR--QDAPH 296
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
34-233 2.79e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 98.95  E-value: 2.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS-DMDEEIEaeynILQFLPNHPNVVKFYGMFYKadhcvGGQLW 112
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKrDPSEEIE----ILLRYGQHPNIITLKDVYDD-----GKHVY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVSA 188
Cdd:cd14175    72 LVTELMRGG---ELLDKILR-QKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGnpesLRICDFGFAK 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIacEQQydsSYDARCDVWSLGI 233
Cdd:cd14175   148 QLRAENGLLMTPCYTANFVAPEVL--KRQ---GYDEGCDIWSLGI 187
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
42-314 2.91e-22

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 99.18  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPV-----SDMDEEIeAEYNILQFLpNHPNVVKFYGMFYKAdhcvgGQLWLVLE 116
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAhivsrSEVTHTL-AERTVLAQV-DCPFIVPLKFSFQSP-----EKLYLVLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd05585    75 FINGG---ELFHHLQREG-RFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPpptLLHPEKWCEEFN 276
Cdd:cd05585   151 TNTFCGTPEYLAPELLLGH-----GYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEP---LRFPDGFDRDAK 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  277 HFISQCLIKDFERRPSV---THLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05585   223 DLLIGLLNRDPTKRLGYngaQEIKNHPFFDQIDWKRLLMKK 263
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
34-303 3.08e-22

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 98.06  E-value: 3.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD----------PVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKA 103
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgggsfspeEVQELREATLKEIDILRKVSGHPNIIQLKDTYETN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  104 DHcvggqLWLVLELCNGGSV----TELVKgllrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV 179
Cdd:cd14182    83 TF-----FFLVFDLMKKGELfdylTEKVT--------LSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  180 KLVDFGVSAQLTSTRlRRNTSVGTPFWMAPEVIACE-QQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIp 258
Cdd:cd14182   150 KLTDFGFSCQLDPGE-KLREVCGTPGYLAPEIIECSmDDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI- 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  259 RNPPPTLLHPEkW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14182   228 MSGNYQFGSPE-WddrSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
31-232 3.55e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 98.98  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILdpvsdMDEEIEA-------EYNILQFLpNHPNVVKFYGMFYK 102
Cdd:cd07865     9 DEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKkVL-----MENEKEGfpitalrEIKILQLL-KHENVVNLIEICRT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 ---ADHCVGGQLWLVLELCNGGsvtelVKGLLRCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG 178
Cdd:cd07865    83 katPYNRYKGSIYLVFEFCEHD-----LAGLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  179 VKLVDFGV----SAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLG 232
Cdd:cd07865   158 LKLADFGLarafSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPP----IDMWGAG 211
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
42-301 3.73e-22

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 97.44  E-value: 3.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYK--VTNKRDGSLAAVKILDP-VSDMDEEIEAEYNILQFLpNHPNVVKFYGmFYKADHCVggqlWLVLELC 118
Cdd:cd14120     1 IGHGAFAVVFKgrHRKKPDLPVAIKCITKKnLSKSQNLLGKEIKILKEL-SHENVVALLD-CQETSSSV----YLVMEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTE--LVKGllrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---------VKLVDFGVS 187
Cdd:cd14120    75 NGGDLADylQAKG------TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRnTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHP--VKTLFKIPRNPPPTL 265
Cdd:cd14120   149 RFLQDGMMAA-TLCGSPMYMAPEVIMSLQ-----YDAKADLWSIGTIVYQCLTGKAPFQAQTPqeLKAFYEKNANLRPNI 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  266 lhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14120   223 --PSGTSPALKDLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
42-245 4.94e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 98.57  E-value: 4.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHCvggqlWLVLELCNGG 121
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIVS--KRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHT-----FLVMELLKGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVSaqltstRLR-- 196
Cdd:cd14179    88 ELLERIKK----KQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDnseIKIIDFGFA------RLKpp 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578803747  197 RNTSVGTP----FWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPL 245
Cdd:cd14179   158 DNQPLKTPcftlHYAAPELLN-----YNGYDESCDLWSLGVILYTMLSGQVPF 205
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
40-301 5.50e-22

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 97.10  E-value: 5.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPV---SDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVLE 116
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLrfpTKQESQLRNEVAILQQL-SHPGVVNLECMFETPE-----RVFVVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGgSVTELVkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVsAQLTST 193
Cdd:cd14082    83 KLHG-DMLEMI--LSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGF-ARIIGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVK-----TLFKIPRNPpptllhp 268
Cdd:cd14082   159 KSFRRSVVGTPAYLAPEVLR-----NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINdqiqnAAFMYPPNP------- 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  269 ekWCE---EFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14082   227 --WKEispDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
42-298 6.52e-22

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 96.69  E-value: 6.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVKI--LDPVSDMDEEIEaeyNILQ-----FLPNHPNVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd14061     2 IGVGGFGKVYRGIWR--GEEVAVKAarQDPDEDISVTLE---NVRQearlfWMLRHPNIIALRGVCLQPPN-----LCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTE-LVKGLLRCGQRLDEAMIsyilygALLGLQHLHNNR---IIHRDVKGNNILL--------TTEGGVKLV 182
Cdd:cd14061    72 MEYARGGALNRvLAGRKIPPHVLVDWAIQ------IARGMNYLHNEApvpIIHRDLKSSNILIleaienedLENKTLKIT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQLTSTRlrRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpP 262
Cdd:cd14061   146 DFGLAREWHKTT--RMSAAGTYAWMAPEVIK-----SSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVN-K 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  263 PTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd14061   218 LTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILK 253
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
42-233 7.13e-22

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 96.62  E-value: 7.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYG-MFYKADHCVGGQlwlvlELCNG 120
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDvAFETEDYYVFAQ-----EYAPY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELVKGllRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGVSAQLTSTRLRRN 198
Cdd:cd13987    76 GDLFSIIPP--QVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRVGSTVKRVS 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 578803747  199 TSvgTPFwMAPEViaCEQQYDSSY--DARCDVWSLGI 233
Cdd:cd13987   152 GT--IPY-TAPEV--CEAKKNEGFvvDPSIDVWAFGV 183
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
36-302 7.74e-22

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 96.45  E-value: 7.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVL 115
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRV-RHTNIIQLIEVFETKE-----RVYMVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT---TEGGVKLVDFGVSAQLTS 192
Cdd:cd14087    77 ELATGG---ELFDRIIAKG-SFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYhpgPDSKIMITDFGLASTRKK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 T-RLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNppPTLLHPEKW 271
Cdd:cd14087   153 GpNCLMKTTCGTPEYIAPEILL-----RKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRA--KYSYSGEPW 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  272 CEEFN---HFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14087   226 PSVSNlakDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
39-301 8.95e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 97.11  E-value: 8.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDmDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd07861     5 IEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESE-EEGVPStairEISLLKEL-QHPNIVCLEDVLMQEN-----RLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNggsvTELVKGL--LRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLTS 192
Cdd:cd07861    78 FEFLS----MDLKKYLdsLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGL-ARAFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNT-SVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR--NPPPTLLHPE 269
Cdd:cd07861   153 IPVRVYThEVVTLWYRAPEVLLGSPRYSTP----VDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRilGTPTEDIWPG 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  270 ------------KWCEEF--NHF----------ISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd07861   229 vtslpdykntfpKWKKGSlrTAVknldedgldlLEKMLIYDPAKRISAKKALVHPY 284
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
40-302 9.37e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 96.52  E-value: 9.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlwLVLELC 118
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEkEEVKNEIEVMNQL-NHANLIQLYDAFESRNDIV-----LVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGsvtELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVsAQLTSTRLR 196
Cdd:cd14193    84 DGG---ELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGL-ARRYKPREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIaceqQYD-SSYDArcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIprnppptL-----LHPEK 270
Cdd:cd14193   160 LRVNFGTPEFLAPEVV----NYEfVSFPT--DMWSLGVIAYMLLSGLSPFLGEDDNETLNNI-------LacqwdFEDEE 226
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  271 W---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14193   227 FadiSEEAKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
42-293 1.08e-21

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 96.57  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTnKRDGSLAAVKILDPVSDM--DEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlwLVLELCN 119
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMNCAasKKEFLTELEMLGRL-RHPNLVRLLGYCLESDEKL-----LVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSVTELvkglLRCG---------QRLDeamisyILYGALLGLQHLHN---NRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd14066    74 NGSLEDR----LHCHkgspplpwpQRLK------IAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTS--VGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKiprnppptL 265
Cdd:cd14066   144 RLIPPSESVSKTSavKGTIGYLAPEYI-----RTGRVSTKSDVYSFGVVLLELLTGKPA-VDENRENASRK--------D 209
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  266 LHP---EKWCEEFNHFISQCLIKDFERRPSV 293
Cdd:cd14066   210 LVEwveSKGKEELEDILDKRLVDDDGVEEEE 240
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
42-276 1.17e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 96.91  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVGGQLWLVLELCN 119
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKScrLELSVKNKDRWCHEIQIMKKL-NHPNVVKACDVPEEMNFLVNDVPLLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSVTELV-KGLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV---KLVDFGVSAQLTSTRL 195
Cdd:cd14039    80 GGDLRKLLnKPENCCG--LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGYAKDLDQGSL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 rrNTS-VGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDG-DPPLFDMHPVKTLFKIPRNPPPTLLHpekwCE 273
Cdd:cd14039   158 --CTSfVGTLQYLAPELFE-----NKSYTVTVDYWSFGTMVFECIAGfRPFLHNLQPFTWHEKIKKKDPKHIFA----VE 226

                  ...
gi 578803747  274 EFN 276
Cdd:cd14039   227 EMN 229
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
40-297 1.22e-21

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 96.25  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKrdGSLAAVKIL--DPVSDMD---EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd14147     9 EVIGIGGFGKVYRGSWR--GELVAVKAArqDPDEDISvtaESVRQEARLFAML-AHPNIIALKAVCLEEPN-----LCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVkgllrCGQRLDEAMISYILYGALLGLQHLHNNRI---IHRDVKGNNILLTTEG--------GVKLVD 183
Cdd:cd14147    81 MEYAAGGPLSRAL-----AGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIenddmehkTLKITD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQLTSTrlRRNTSVGTPFWMAPEVIACeqqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpPP 263
Cdd:cd14147   156 FGLAREWHKT--TQMSAAGTYAWMAPEVIKA-----STFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVN-KL 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  264 TLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd14147   228 TLPIPSTCPEPFAQLMADCWAQDPHRRPDFASIL 261
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
42-300 1.26e-21

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 95.77  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-------EEIEAEYNILQFL--PNHPNVVKFYGMFYKADHCVggqlw 112
Cdd:cd14005     8 LGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEwamingpVPVPLEIALLLKAskPGVPGVIRLLDWYERPDGFL----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLElcNGGSVTELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG-VKLVDFGVSAQLT 191
Cdd:cd14005    83 LIME--RPEPCQDLFDFITERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGeVKLIDFGCGALLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRrnTSVGTPFWMAPEVIaceqqYDSSYDAR-CDVWSLGITAIELGDGDPPLFdmhpvKTLFKIPRNPpptlLHPEK 270
Cdd:cd14005   160 DSVYT--DFDGTRVYSPPEWI-----RHGRYHGRpATVWSLGILLYDMLCGDIPFE-----NDEQILRGNV----LFRPR 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14005   224 LSKECCDLISRCLQFDPSKRPSLEQILSHP 253
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
34-302 1.31e-21

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 96.11  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE-IEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlw 112
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKEtVRKEIQIMNQL-HHPKLINLHDAFEDDNEMV----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGsvtELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 190
Cdd:cd14114    76 LILEFLSGG---ELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSneVKLIDFGLATHL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSvGTPFWMAPEVIacEQQYDSSYdarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEK 270
Cdd:cd14114   153 DPKESVKVTT-GTAEFAAPEIV--EREPVGFY---TDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFS 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  271 W-CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14114   227 GiSEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
42-314 1.31e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 97.43  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDE--EIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLEL 117
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILkkEVIIAKDEvaHTLTENRVLQNT-RHPFLTSLKYSFQTNDR-----LCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGqRLDEAMISYilYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd05571    77 VNGG---ELFFHLSRER-VFSEDRTRF--YGAeiVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDM-HPVktLFKI----PRNPPPTLLHPEK 270
Cdd:cd05571   151 TTKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNRdHEV--LFELilmeEVRFPSTLSPEAK 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  271 wceefnHFISQCLIKDFERR----PS-VTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05571   224 ------SLLAGLLKKDPKKRlgggPRdAKEIMEHPFFASINWDDLYQKK 266
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
34-305 1.36e-21

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 97.77  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEE-----IEAEYNILQFLPNhPNVVKFYGMFYKADHcvg 108
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRK-KDVLKRnqvahVKAERDILAEADN-EWVVKLYYSFQDKEN--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELvkgLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSa 188
Cdd:cd05598    76 --LYFVMDYIPGGDLMSL---LIKKGI-FEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 qlTSTRLRRNTS-------VGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRNP 261
Cdd:cd05598   149 --TGFRWTHDSKyylahslVGTPNYIAPEVLL-----RTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKV-INW 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  262 PPTLLHPE--KWCEEFNHFISQcLIKDFERR---PSVTHLLDHPFIKGV 305
Cdd:cd05598   221 RTTLKIPHeaNLSPEAKDLILR-LCCDAEDRlgrNGADEIKAHPFFAGI 268
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
42-298 1.43e-21

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 95.66  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDEE-IEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLELCNG 120
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYK--NDVDQHkIVREISLLQKL-SHPNIVRYLGICVKDEK-----LHPILEYVSG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELVKGllrcgqrlDEAMISYILYGALL-----GLQHLHNNRIIHRDVKGNNILLTTEGGVK---LVDFGVSAQLTS 192
Cdd:cd14156    73 GCLEELLAR--------EELPLSWREKVELAcdisrGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRL----RRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVK-------TLFK--IPR 259
Cdd:cd14156   145 MPAndpeRKLSLVGSAFWMAPEMLRGEP-----YDRKVDVFSFGIVLCEILARIPADPEVLPRTgdfgldvQAFKemVPG 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  260 NPPPTLlhpekwceefnHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd14156   220 CPEPFL-----------DLAASCCRMDAFKRPSFAELLD 247
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
33-304 1.49e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 96.82  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMdEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLW 112
Cdd:cd14085     2 EDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDK-KIVRTEIGVLLRL-SHPNIIKLKEIFETPTE-----IS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELV--KGLLrcGQRLDEAMISYILYGallgLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVS 187
Cdd:cd14085    75 LVLELVTGGELFDRIveKGYY--SERDAADAVKQILEA----VAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 aQLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLH 267
Cdd:cd14085   149 -KIVDQQVTMKTVCGTPGYCAPEILRGC-----AYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCDYDFVS 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  268 PekWCEEFN----HFISQCLIKDFERRPSVTHLLDHPFIKG 304
Cdd:cd14085   223 P--WWDDVSlnakDLVKKLIVLDPKKRLTTQQALQHPWVTG 261
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
34-257 1.58e-21

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 97.83  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFlPNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd05596    26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAffweERDIMAH-ANSEWIVQLHYAFQDDKY---- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELVKGLlrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05596   101 -LYMVMDYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  190 LTSTRL-RRNTSVGTPFWMAPEVIAcEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI 257
Cdd:cd05596   175 MDKDGLvRSDTAVGTPDYISPEVLK-SQGGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKI 242
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
34-302 1.64e-21

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 95.79  E-value: 1.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL----DPVSD---MDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHC 106
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqSRASRrgvSREEIEREVSILRQV-LHPNIITLHDVYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VggqlwLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLV 182
Cdd:cd14196    84 V-----LILELVSGGELFDF----LAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQLTSTRLRRNTsVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIprnpp 262
Cdd:cd14196   155 DFGLAHEIEDGVEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI----- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  263 pTLLHPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14196   224 -TAVSYDFDEEFFSHtselakdFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
36-301 1.82e-21

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 95.44  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYnILQFLPNHPNVVKFYGMFYKADHcvggqLWLVL 115
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREI-INHRSLRHPNIVRFKEVILTPTH-----LAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL--TTEGGVKLVDFGVSAQlTST 193
Cdd:cd14665    76 EYAAGG---ELFERICNAG-RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKS-SVL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAcEQQYDSSYdarCDVWSLGITAIELGDGDPPLFDMHPV----KTLFKI--PRNPPPTLLH 267
Cdd:cd14665   151 HSQPKSTVGTPAYIAPEVLL-KKEYDGKI---ADVWSCGVTLYVMLVGAYPFEDPEEPrnfrKTIQRIlsVQYSIPDYVH 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  268 PEKWCEefnHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14665   227 ISPECR---HLISRIFVADPATRITIPEIRNHEW 257
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
40-302 1.94e-21

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 95.37  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA-EYNILQFLpNHPNVVKFYGMFYkadhcVGGQLWLVLELC 118
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLlEIQVMNQL-NHRNLIQLYEAIE-----TPNEIVLFMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGsvtELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVsAQLTSTRLR 196
Cdd:cd14190    84 EGG---ELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhqVKIIDFGL-ARRYNPREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTSVGTPFWMAPEVIACEQQYDSSydarcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNppptllhpeKWC---E 273
Cdd:cd14190   160 LKVNFGTPEFLSPEVVNYDQVSFPT-----DMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMG---------NWYfdeE 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  274 EFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14190   226 TFEHvsdeakdFVSNLIIKERSARMSATQCLKHPWL 261
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
40-299 2.31e-21

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 95.49  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTnkRDGSLAAVKIL--DPVSDMDEEIEA---EYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd14145    12 EIIGIGGFGKVYRAI--WIGDEVAVKAArhDPDEDISQTIENvrqEAKLFAML-KHPNIIALRGVCLKEPN-----LCLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRI---IHRDVKGNNILL--TTEGG------VKLVD 183
Cdd:cd14145    84 MEFARGGPLNRVLSG-----KRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILIleKVENGdlsnkiLKITD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQLTstRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpPP 263
Cdd:cd14145   159 FGLAREWH--RTTKMSAAGTYAWMAPEVIR-----SSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMN-KL 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  264 TLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14145   231 SLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQ 266
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
39-244 2.41e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 96.60  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKIL---DPVS-DMDEEIEAEYNILQFL--PNHPNVVKFYGMFYKADH-Cvggql 111
Cdd:cd05589     4 IAVLGRGHFGKVLLAEYKPTGELFAIKALkkgDIIArDEVESLMCEKRIFETVnsARHPFLVNLFACFQTPEHvC----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 wLVLELCNGGSVTELVKGLLRCGQRLdeamisyILYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05589    79 -FVMEYAAGGDLMMHIHEDVFSEPRA-------VFYAAcvVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  190 LTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPP 244
Cdd:cd05589   151 GMGFGDRTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLIYEMLVGESP 200
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
34-303 2.95e-21

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 95.07  E-value: 2.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP---------VSDmdEEIEAEYNILQFLpNHPNVVKFYGMFYKAD 104
Cdd:cd14195     5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKrrlsssrrgVSR--EEIEREVNILREI-QHPNIITLHDIFENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCVggqlwLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VK 180
Cdd:cd14195    82 DVV-----LILELVSGGELFDF----LAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSAQLTSTRLRRNTsVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR- 259
Cdd:cd14195   153 LIDFGIAHKIEAGNEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAv 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  260 NPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14195   227 NYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
39-300 3.77e-21

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 95.16  E-value: 3.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEA--EYNILQFLPNHPNVVKFYGMFYKADHCVggqlwLVL 115
Cdd:cd14051     5 VEKIGSGEFGSVYKCINRLDGCVYAIKkSKKPVAGSVDEQNAlnEVYAHAVLGKHPHVVRYYSAWAEDDHMI-----IQN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT-TEGGVKLVDFGVSAQLTSTR 194
Cdd:cd14051    80 EYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISrTPNPVSSEEEEEDFEGEEDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRN------------TSVGTPF-------WMAPEVIaceqQYDSSYDARCDVWSLGITAIELGDGDPplfdmhpvktlf 255
Cdd:cd14051   160 PESNevtykigdlghvTSISNPQveegdcrFLANEIL----QENYSHLPKADIFALALTVYEAAGGGP------------ 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  256 kIPRNPP----------PTLLHpekwC-EEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14051   224 -LPKNGDewheirqgnlPPLPQ----CsPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
40-302 5.92e-21

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 94.26  E-value: 5.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlwLVLELC 118
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKErEEVKNEINIMNQL-NHVNLIQLYDAFESKTNLT-----LIMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGsvtELVKGLLRCGQRLDEamISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVsAQLTSTR 194
Cdd:cd14192    84 DGG---ELFDRITDESYQLTE--LDAILFTRQIceGVHYLHQHYILHLDLKPENILCVNSTGnqIKIIDFGL-ARRYKPR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPFWMAPEVIaceqQYD-SSYDArcDVWSLGITAIELGDGDPPLFDMHPVKTL-FKIPRNPPPTLLHPEKWC 272
Cdd:cd14192   158 EKLKVNFGTPEFLAPEVV----NYDfVSFPT--DMWSVGVITYMLLSGLSPFLGETDAETMnNIVNCKWDFDAEAFENLS 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  273 EEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14192   232 EEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
37-306 5.94e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 95.70  E-value: 5.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDmdeEIEA-----EYNILQFLPNHPNVVKFYGMfYKADHcvGGQ 110
Cdd:cd07852    10 EILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAFRN---ATDAqrtfrEIMFLQELNDHPNIIKLLNV-IRAEN--DKD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNggsvTEL--V--KGLLRcgqrldEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd07852    84 IYLVFEYME----TDLhaVirANILE------DIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTS-----VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLF--------------- 246
Cdd:cd07852   154 ARSLSQLEEDDENPvltdyVATRWYRAPEILLGSTRYTKG----VDMWSVGCILGEMLLGK-PLFpgtstlnqlekiiev 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  247 -------DMHPVKT------LFKIPRNPPPTLLH-PEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07852   229 igrpsaeDIESIQSpfaatmLESLPPSRPKSLDElFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFH 302
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
40-301 6.29e-21

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 94.65  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILD---------PVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHcvggq 110
Cdd:cd14181    16 EVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTF----- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSV----TELVKgllrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd14181    91 IFLVFDLMRRGELfdylTEKVT--------LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLRRNTsVGTPFWMAPEVIACE-QQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRNPPPTL 265
Cdd:cd14181   163 SCHLEPGEKLREL-CGTPGYLAPEILKCSmDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI-MEGRYQF 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  266 LHPEkW---CEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14181   241 SSPE-WddrSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
42-289 6.42e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 94.82  E-value: 6.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVK----ILDPVSDMDEEIEAEYNILQFLpNHPNVVKFY----GMFYKADHCVGgqlWL 113
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqELSPSDKNRERWCLEVQIMKKL-NHPNVVSARdvppELEKLSPNDLP---LL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGsvtELVKGLLR----CGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGV 186
Cdd:cd13989    77 AMEYCSGG---DLRKVLNQpencCG--LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLrrNTS-VGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPP-LFDMHPVKTLFKIPRNPPPT 264
Cdd:cd13989   152 AKELDQGSL--CTSfVGTLQYLAPELFESKK-----YTCTVDYWSFGTLAFECITGYRPfLPNWQPVQWHGKVKQKKPEH 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  265 LLHPEKWCEEF---------NHfISQCLIKDFER 289
Cdd:cd13989   225 ICAYEDLTGEVkfsselpspNH-LSSILKEYLES 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
34-306 6.51e-21

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 95.51  E-value: 6.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDM---DEEIEAEYNILQFLpNHPNVVKFYGMFY-KADHCVGG 109
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVvttAKRTLRELKILRHF-KHDNIIAIRDILRpKVPYADFK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGsvtelVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd07855    84 DVYVVLDLMESD-----LHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNT----SVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELgDGDPPLFD----MHPVKTLFKIPRNP 261
Cdd:cd07855   159 LCTSPEEHKYfmteYVATRWYRAPELMLSLPEYTQA----IDMWSVGCIFAEM-LGRRQLFPgknyVHQLQLILTVLGTP 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  262 PPTLL--------------------------HPEKWCEEFNhFISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07855   234 SQAVInaigadrvrryiqnlpnkqpvpwetlYPKADQQALD-LLSQMLRFDPSERITVAEALQHPFLAKYH 303
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
42-310 7.03e-21

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 94.56  E-value: 7.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD----EEIEAEYNILQFLPNHPNVVKFYGMFYKADHCvggqlwLVLEL 117
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKrkgyEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLC------LVMTI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05608    83 MNGGDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 NTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLF---DMHPVKTLFKIPRNPPPTllHPEKWCEE 274
Cdd:cd05608   163 KGYAGTPGFMAPELLLGEE-----YDYSVDYFTLGVTLYEMIAARGPFRargEKVENKELKQRILNDSVT--YSEKFSPA 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  275 FNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVL 310
Cdd:cd05608   236 SKSICEALLAKDPEKRlgfrdGNCDGLRTHPFFRDINWRKL 276
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
40-296 7.32e-21

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 94.03  E-value: 7.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYK--VTNKRDGSLA-AVKI--LDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMfykadhCVGGQLWLV 114
Cdd:cd05056    12 RCIGEGQFGDVYQgvYMSPENEKIAvAVKTckNCTSPSVREKFLQEAYIMRQF-DHPHIVKLIGV------ITENPVWIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGsvtELVKGLLRCGQRLDEAmiSYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd05056    85 MELAPLG---ELRSYLQVNKYSLDLA--SLILYAYQLstALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPF-WMAPEVIACEQqydssYDARCDVWSLGITAIE-LGDGDPPLFDMHPVKTLFKI--------PRNPP 262
Cdd:cd05056   160 ESYYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEiLMLGVKPFQGVKNNDVIGRIengerlpmPPNCP 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  263 PTLLhpekwceefnHFISQCLIKDFERRPSVTHL 296
Cdd:cd05056   235 PTLY----------SLMTKCWAYDPSKRPRFTEL 258
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
40-302 9.30e-21

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 94.02  E-value: 9.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPV-----SDMDEEIEaeynILQFLPNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd14090     8 ELLGEGAYASVQTCINLYTGKEYAVKIIEKHpghsrSRVFREVE----TLHQCQGHPNILQLIEYFEDDE-----RFYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSvteLVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV---KLVDFGVSA--Q 189
Cdd:cd14090    79 FEKMRGGP---LLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGSgiK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNTS------VGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLF----------------- 246
Cdd:cd14090   155 LSSTSMTPVTTpelltpVGSAEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIMLCGYPPFYgrcgedcgwdrgeacqd 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  247 --DM--HPVKT-LFKIPRnppptllhpEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14090   235 cqELlfHSIQEgEYEFPE---------KEWshiSAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
42-250 1.02e-20

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 93.31  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKiLDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMfykadhCV-GGQLWLVLELCNG 120
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALK-MNTLSSNRANMLREVQLMNRL-SHPNILRFMGV------CVhQGQLHALTEYING 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELV--KGLLRCGQRLDEAmisyilYGALLGLQHLHNNRIIHRDVKGNNILL-TTEGGVKLV--DFGVSAQL--TST 193
Cdd:cd14155    73 GNLEQLLdsNEPLSWTVRVKLA------LDIARGLSYLHSKGIFHRDLTSKNCLIkRDENGYTAVvgDFGLAEKIpdYSD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIEL---GDGDPplfDMHP 250
Cdd:cd14155   147 GKEKLAVVGSPYWMAPEVL-----RGEPYNEKADVFSYGIILCEIiarIQADP---DYLP 198
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
34-302 1.24e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 93.55  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-------EEIEAEYNILQFLpNHPNVVKFYGMFYKADHC 106
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsrEDIEREVSILKEI-QHPNVITLHEVYENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VggqlwLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLV 182
Cdd:cd14194    84 I-----LILELVAGGELFDF----LAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKII 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQLTSTRLRRNTsVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIprnpp 262
Cdd:cd14194   155 DFGLAHKIDFGNEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPFLGDTKQETLANV----- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  263 pTLLHPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14194   224 -SAVNYEFEDEYFSNtsalakdFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
40-302 1.37e-20

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 92.86  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEEieAEYNILQ-----FLPNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd14074     9 ETLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDDV--SKAHLFQevrcmKLVQHPNVVRLYEVIDTQT-----KLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL-TTEGGVKLVDFGVSAQ-LTS 192
Cdd:cd14074    81 LELGDGGDMYDYI---MKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKfQPG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLrrNTSVGTPFWMAPEVIACEqqydsSYDA-RCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIP--RNPPPTLLHPE 269
Cdd:cd14074   158 EKL--ETSCGSLAYSAPEILLGD-----EYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMdcKYTVPAHVSPE 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  270 kwCEEfnhFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14074   231 --CKD---LIRRMLIRDPKKRASLEEIENHPWL 258
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
36-302 1.55e-20

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 92.75  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvgGQL 111
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRflprELQIVERL-DHKNIIHVYEMLESAD----GKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLttEG-GVKLVDFGVSAQL 190
Cdd:cd14163    77 YLVMELAEDGDVFDCVLH----GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL--QGfTLKLTDFGFAKQL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 -TSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDAR-CDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPP-PTLLH 267
Cdd:cd14163   151 pKGGRELSQTFCGSTAYAAPEVLQ-----GVPHDSRkGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGVSlPGHLG 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  268 PEKWCEEfnhFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14163   226 VSRTCQD---LLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
33-302 1.62e-20

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 93.08  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEII--ETIGKGTYGKVYKVTNKRDGSLAAVKILDPV---SDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHCV 107
Cdd:cd14197     6 QERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRrkgQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEMI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 ggqlwLVLELCNGGSVTElvkgllRCGQRLDEAM----ISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVK 180
Cdd:cd14197    86 -----LVLEYAAGGEIFN------QCVADREEAFkekdVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSAQLTSTRLRRNTsVGTPFWMAPEVIAceqqYDSSYDArCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRn 260
Cdd:cd14197   155 IVDFGLSRILKNSEELREI-MGTPEYVAPEILS----YEPISTA-TDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQ- 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  261 ppptlLHPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14197   228 -----MNVSYSEEEFEHlsesaidFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
34-302 1.64e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 92.94  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP---------VSDmdEEIEAEYNILQFLpNHPNVVKFYGMFYKAD 104
Cdd:cd14105     5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKrrskasrrgVSR--EDIEREVSILRQV-LHPNIITLHDVFENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCVggqlwLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG----GVK 180
Cdd:cd14105    82 DVV-----LILELVAGGELFDF----LAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSAQLTSTRLRRNTsVGTPFWMAPEVIACEqqydsSYDARCDVWSLG-ITAIELGDGDPPLFDMHPvKTLFKIpr 259
Cdd:cd14105   153 LIDFGLAHKIEDGNEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPFLGDTKQ-ETLANI-- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  260 npppTLLHPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14105   224 ----TAVNYDFDDEYFSNtselakdFIRQLLVKDPRKRMTIQESLRHPWI 269
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
40-298 1.84e-20

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 92.51  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKI--LDPVSDMDEEIEAEYNIL-QFlpNHPNVVKFYGMfykadhCVGGQ-LWLVL 115
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTcrETLPPDLKRKFLQEARILkQY--DHPNIVKLIGV------CVQKQpIMIVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ------ 189
Cdd:cd05041    73 ELVPGGS---LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedgey 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRntsvgTPF-WMAPEVIaceqQYdSSYDARCDVWSLGITAIEL-GDGDPPLFDMHPVKTLFKIPRN---PPPT 264
Cdd:cd05041   150 TVSDGLKQ-----IPIkWTAPEAL----NY-GRYTSESDVWSFGILLWEIfSLGATPYPGMSNQQTREQIESGyrmPAPE 219
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578803747  265 LLhPEkWCEEfnhFISQCLIKDFERRPSVTHLLD 298
Cdd:cd05041   220 LC-PE-AVYR---LMLQCWAYDPENRPSFSEIYN 248
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
42-246 1.95e-20

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 94.17  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIE---AEYNILQ--FLPNHPNVVKFYGMFYKADhcvggQLWLVL 115
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKkVIVAKKEVAhtiGERNILVrtALDESPFIVGLKFSFQTPT-----DLYLVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd05586    76 DYMSGG---ELFWHLQKEG-RFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNK 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  196 RRNTSVGTPFWMAPEVIACEqqydSSYDARCDVWSLGITAIELGDGDPPLF 246
Cdd:cd05586   152 TTNTFCGTTEYLAPEVLLDE----KGYTKMVDFWSLGVLVFEMCCGWSPFY 198
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
42-301 1.97e-20

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 92.33  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvgGQLWLVLELCNGG 121
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL-QHPQYITLHDTYESP-----TSYILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGVSAQLTSTRlRRN 198
Cdd:cd14115    75 RLLDY----LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHR-HVH 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  199 TSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRnppPTLLHPEKWCEEFNH- 277
Cdd:cd14115   150 HLLGNPEFAAPEVIQ-----GTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR---VDFSFPDEYFGDVSQa 221
                         250       260
                  ....*....|....*....|....*..
gi 578803747  278 ---FISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14115   222 ardFINVILQEDPRRRPTAATCLQHPW 248
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
42-300 2.28e-20

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 92.68  E-value: 2.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVKILDPVSDMDEEIEAEYNILQFLP---------------------NHPNVVKFYGMF 100
Cdd:cd14000     2 LGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFANVPADTMLRHLRatdamknfrllrqeltvlshlHHPSIVYLLGIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  101 YKAdhcvggqLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT----- 175
Cdd:cd14000    80 IHP-------LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypns 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  176 EGGVKLVDFGVSAQltSTRLRRNTSVGTPFWMAPEVIaceqQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLF 255
Cdd:cd14000   153 AIIIKIADYGISRQ--CCRMGAKGSEGTPGFRAPEIA----RGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEF 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  256 KIPRNPPPTLLHPEkwCEEFNH---FISQCLIKDFERRP---SVTHLLDHP 300
Cdd:cd14000   227 DIHGGLRPPLKQYE--CAPWPEvevLMKKCWKENPQQRPtavTVVSILNSP 275
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
34-305 2.57e-20

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 94.35  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLPNHPNVVKFYGMFYKADhcvgg 109
Cdd:cd05627     2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEqvahIRAERDILVEADGAWVVKMFYSFQDKRN----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05627    77 -LYLIMEFLPGGDMMTL----LMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTS---TRLRRN--------------------------------TSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGIT 234
Cdd:cd05627   152 LKKahrTEFYRNlthnppsdfsfqnmnskrkaetwkknrrqlaySTVGTPDYIAPEVFM-----QTGYNKLCDWWSLGVI 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  235 AIELGDGDPPLFDMHPVKTLFKIpRNPPPTLLHPEK--WCEEFNHFISQCLIkDFERR---PSVTHLLDHPFIKGV 305
Cdd:cd05627   227 MYEMLIGYPPFCSETPQETYRKV-MNWKETLVFPPEvpISEKAKDLILRFCT-DAENRigsNGVEEIKSHPFFEGV 300
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
75-301 3.03e-20

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 91.65  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   75 EEIEAEYNILQFLpNHPNVVKFYGM-FYKADHCVGGQLWLVLELCNGGSVTELvkgLLRCGQ-RLDEAMiSYILygALL- 151
Cdd:cd14012    43 QLLEKELESLKKL-RHPNLVSYLAFsIERRGRSDGWKVYLLTEYAPGGSLSEL---LDSVGSvPLDTAR-RWTL--QLLe 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  152 GLQHLHNNRIIHRDVKGNNILL---TTEGGVKLVDFGVSAQLTSTRLRRN-TSVGTPFWMAPEVIaceqQYDSSYDARCD 227
Cdd:cd14012   116 ALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSlDEFKQTYWLPPELA----QGSKSPTRKTD 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  228 VWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPtllhpekwceEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14012   192 VWDLGLLFLQMLFGLDV-LEKYTSPNPVLVSLDLSA----------SLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
42-233 3.06e-20

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 92.02  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKV----YKVTNKRdgslAAVKILDPvSDMDE--------EIEAEYNIlqflpNHPNVVKFYGMFYKAdhcvgG 109
Cdd:cd14075    10 LGSGNFSQVklgiHQLTKEK----VAIKILDK-TKLDQktqrllsrEISSMEKL-----HHPNIIRLYEVVETL-----S 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGsvtELVKGLLRCGqRLDEaMISYILYGALL-GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd14075    75 KLHLVMEYASGG---ELYTKISTEG-KLSE-SEAKPLFAQIVsAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFST 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  189 QLTSTRlRRNTSVGTPFWMAPEVIaCEQQYdssYDARCDVWSLGI 233
Cdd:cd14075   150 HAKRGE-TLNTFCGSPPYAAPELF-KDEHY---IGIYVDIWALGV 189
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
35-293 3.13e-20

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 92.19  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPV-----SDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADhcvgg 109
Cdd:cd14070     3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKkakkdSYVTKNLRREGRIQQMI-RHPNITQLLDILETEN----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd14070    77 SYYLVMELCPGGNLMHRIYD----KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRR--NTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDMHP--VKTLFKI----PRNP 261
Cdd:cd14070   153 AGILGYSDpfSTQCGSPAYAAPELLARKK-----YGPKVDVWSIGVNMYAMLTGTLP-FTVEPfsLRALHQKmvdkEMNP 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  262 PPTLLHPekwceEFNHFISQCLIKDFERRPSV 293
Cdd:cd14070   227 LPTDLSP-----GAISFLRSLLEPDPLKRPNI 253
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
36-274 3.38e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 92.79  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDG----SLAAVKILDPVSDMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADHCVGG 109
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGgrfvALKRVRVQTGEEGMPLSTIREVAVLRHLETfeHPNVVRLFDVCTVSRTDRET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELVKGllrCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQ 189
Cdd:cd07862    83 KLTLVFEHVDQDLTTYLDKV---PEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGL-AR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDgDPPLF----DMHPVKTLFKIPRNPpptl 265
Cdd:cd07862   159 IYSFQMALTSVVVTLWYRAPEVL-----LQSSYATPVDLWSVGCIFAEMFR-RKPLFrgssDVDQLGKILDVIGLP---- 228

                  ....*....
gi 578803747  266 lHPEKWCEE 274
Cdd:cd07862   229 -GEEDWPRD 236
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
36-309 3.43e-20

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 92.26  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWL 113
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEamVENEIAVLRRI-NHENIVSLEDIYESPTH-----LYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---EGGVKLVDFGVSAQL 190
Cdd:cd14169    79 AMELVTGG---ELFDRIIERGS-YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSKIE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLrrNTSVGTPFWMAPEVIacEQQydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKtLFKIPRNPPPTLLHP-- 268
Cdd:cd14169   155 AQGML--STACGTPGYVAPELL--EQK---PYGKAVDVWAIGVISYILLCGYPPFYDENDSE-LFNQILKAEYEFDSPyw 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  269 EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKG-------VHGKV 309
Cdd:cd14169   227 DDISESAKDFIRHLLERDPEKRFTCEQALQHPWISGdtaldrdIHGSV 274
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
42-314 3.62e-20

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 92.12  E-value: 3.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLPNH---PNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlalnERIMLSLVSTGgdcPFIVCMTYAFQTPD-----KLCFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGsvtELVKGLLRCGQRLDEAMIsyiLYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd05606    77 LDLMNGG---DLHYHLSQHGVFSEAEMR---FYAAevILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TrlRRNTSVGTPFWMAPEVIACEQQYDSSYDarcdvW-SLGITAIELGDGDPPlFDMHPVKTLFKIPRNpppTLLH---- 267
Cdd:cd05606   151 K--KPHASVGTHGYMAPEVLQKGVAYDSSAD-----WfSLGCMLYKLLKGHSP-FRQHKTKDKHEIDRM---TLTMnvel 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05606   220 PDSFSPELKSLLEGLLQRDVSKRlgclgRGATEVKEHPFFKGVDWQQVYLQK 271
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
42-297 3.82e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 91.59  E-value: 3.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVKI--LDPVSDMD---EEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd14148     2 IGVGGFGKVYKGLWR--GEEVAVKAarQDPDEDIAvtaENVRQEARLFWML-QHPNIIALRGVCLNPPH-----LCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVkgllrCGQRLDEAMISYILYGALLGLQHLHNNR---IIHRDVKGNNILLT--------TEGGVKLVDFG 185
Cdd:cd14148    74 YARGGALNRAL-----AGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILepienddlSGKTLKITDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRlrRNTSVGTPFWMAPEVIACeqqydSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpPPTL 265
Cdd:cd14148   149 LAREWHKTT--KMSAAGTYAWMAPEVIRL-----SLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMN-KLTL 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578803747  266 LHPEKWCEEFNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd14148   221 PIPSTCPEPFARLLEECWDPDPHGRPDFGSIL 252
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
34-302 4.26e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 92.56  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA-------EYNILQFLpNHPNVV--------KFYG 98
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR----LDNEKEGfpitairEIKILRQL-NHRSVVnlkeivtdKQDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   99 MFYKADHcvgGQLWLVLELcnggsVTELVKGLLRCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG 177
Cdd:cd07864    82 LDFKKDK---GAFYLVFEY-----MDHDLMGLLESGLvHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  178 GVKLVDFGVSAQLTSTRLRRNTS-VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDgDPPLF----DMHPVK 252
Cdd:cd07864   154 QIKLADFGLARLYNSEESRPYTNkVITLWYRPPELLLGEERYGPA----IDVWSCGCILGELFT-KKPIFqanqELAQLE 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  253 TLFKIPRNPPPTL-----------------LHPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd07864   229 LISRLCGSPCPAVwpdviklpyfntmkpkkQYRRRLREEFSFiptpaldLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
36-306 4.78e-20

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 92.85  E-value: 4.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNK--RDGSLAAVKILDPVsdMDEEIEA-----EYNILQFLPNHPNVVKFYGM---FYKADH 105
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAetSEEETVAIKKITNV--FSKKILAkralrELKLLRHFRGHKNITCLYDMdivFPGNFN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 cvggQLWLVLEL--CNGGSVtelvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd07857    80 ----ELYLYEELmeADLHQI-------IRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVsAQLTSTRLRRNTS-----VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELgDGDPPLFD----MHP---- 250
Cdd:cd07857   149 FGL-ARGFSENPGENAGfmteyVATRWYRAPEIMLSFQSYTKA----IDVWSVGCILAEL-LGRKPVFKgkdyVDQlnqi 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  251 -----------------------VKTLFKIPRNPPPTLLhPEKWCEEFNhFISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07857   223 lqvlgtpdeetlsrigspkaqnyIRSLPNIPKKPFESIF-PNANPLALD-LLEKLLAFDPTKRISVEEALEHPYLAIWH 299
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
36-256 5.37e-20

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 92.75  E-value: 5.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIE---AEYNILQFLPNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKdVVIQDDDVEctmVEKRVLALSGKPPFLTQLHSCFQTMD-----RL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05616    77 YFVMEYVNGG---DLMYHIQQVG-RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENI 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFK 256
Cdd:cd05616   153 WDGVTTKTFCGTPDYIAPEIIAYQ-----PYGKSVDWWAFGVLLYEMLAGQAP-FEGEDEDELFQ 211
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
36-301 5.51e-20

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 90.98  E-value: 5.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVL 115
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSL-RHPNIIRFKEVVLTPTH-----LAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELVKGLLRCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL--TTEGGVKLVDFGV--SAQLT 191
Cdd:cd14662    76 EYAAGG---ELFERICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYskSSVLH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 StrlRRNTSVGTPFWMAPEVIaCEQQYDSSYdarCDVWSLGITAIELGDGDPPLFDMHPVKTLFK-IPR-----NPPPTL 265
Cdd:cd14662   152 S---QPKSTVGTPAYIAPEVL-SRKEYDGKV---ADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKtIQRimsvqYKIPDY 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  266 LHPEKWCEefnHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14662   225 VRVSQDCR---HLLSRIFVANPAKRITIPEIKNHPW 257
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
42-296 5.58e-20

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 91.26  E-value: 5.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYK-VTNKRDGSL--AAVKILDPvSDMD---EEIEAEYNILQFLpNHPNVVKFYGMfykadhCVGGQLWLVL 115
Cdd:cd05060     3 LGHGNFGSVRKgVYLMKSGKEveVAVKTLKQ-EHEKagkKEFLREASVMAQL-DHPCIVRLIGV------CKGEPLMLVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL--TST 193
Cdd:cd05060    75 ELAPLGPLLKYLKK----RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALgaGSD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIE-LGDGDPPLFDMHPVKTLFKIPRNppPTLLHPEKW 271
Cdd:cd05060   151 YYRATTAGRWPLkWYAPECI-----NYGKFSSKSDVWSYGVTLWEaFSYGAKPYGEMKGPEVIAMLESG--ERLPRPEEC 223
                         250       260
                  ....*....|....*....|....*
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHL 296
Cdd:cd05060   224 PQEIYSIMLSCWKYRPEDRPTFSEL 248
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
32-261 6.41e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 92.77  E-value: 6.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDtWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDM----DEEIEAEYNILQFLPNHPNVVKFYGMFYKADhcv 107
Cdd:cd05602     6 PSD-FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILkkkeEKHIMSERNVLLKNVKHPFLVGLHFSFQTTD--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 ggQLWLVLELCNGGSV---TELVKGLLRCGQRLDEAMISYilygallGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd05602    82 --KLYFVLDYINGGELfyhLQRERCFLEPRARFYAAEIAS-------ALGYLHSLNIVYRDLKPENILLDSQGHIVLTDF 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  185 GVSAQLTSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNP 261
Cdd:cd05602   153 GLCKENIEPNGTTSTFCGTPEYLAPEVL-----HKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKP 224
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
34-305 6.62e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 96.73  E-value: 6.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE---IEAEYNILQFLpNHPNVVKFYGMFY-KADHcvgg 109
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREksqLVIEVNVMREL-KHKNIVRYIDRFLnKANQ---- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHN-------NRIIHRDVKGNNILLTTegGV--- 179
Cdd:PTZ00266   88 KLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLST--GIrhi 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  180 ----------------KLVDFGVSAQLTSTRLRrNTSVGTPFWMAPEVIACEQQydsSYDARCDVWSLGITAIELGDGDP 243
Cdd:PTZ00266  166 gkitaqannlngrpiaKIGDFGLSKNIGIESMA-HSCVGTPYYWSPELLLHETK---SYDDKSDMWALGCIIYELCSGKT 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  244 PLFDMHPVKTLF-KIPRNPPPTLLHPEKwceEFNHFISQCLIKDFERRPSVTHLLDHPFIKGV 305
Cdd:PTZ00266  242 PFHKANNFSQLIsELKRGPDLPIKGKSK---ELNILIKNLLNLSAKERPSALQCLGYQIIKNV 301
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
43-297 6.81e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 90.40  E-value: 6.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   43 GKGTYGKVYKVTNKRDGSLAAVKILDpvsdmdeEIEAEYNILQFLpNHPNVVKFYGMFYKA-DHCVggqlwlVLELCNGG 121
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLL-------KIEKEAEILSVL-SHRNIIQFYGAILEApNYGI------VTEYASYG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELVKGllrcgQRLDEAMISYILYGAL---LGLQHLHNN---RIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd14060    68 SLFDYLNS-----NESEEMDMDQIMTWATdiaKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTH 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RrnTSVGTPFWMAPEVIaceQQYDSSydARCDVWSLGITAIELGDGDPPLFDMHPVKTLF-KIPRNPPPTLlhPEKWCEE 274
Cdd:cd14060   143 M--SLVGTFPWMAPEVI---QSLPVS--ETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWlVVEKNERPTI--PSSCPRS 213
                         250       260
                  ....*....|....*....|...
gi 578803747  275 FNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd14060   214 FAELMRRCWEADVKERPSFKQII 236
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
33-233 7.08e-20

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 91.62  E-value: 7.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVS-DMDEEIEaeynILQFLPNHPNVVKFYGMFYKadhcvGGQL 111
Cdd:cd14177     3 TDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKrDPSEEIE----ILMRYGQHPNIITLKDVYDD-----GRYV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVS 187
Cdd:cd14177    74 YLVTELMKGG---ELLDRILR-QKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSAnadsIRICDFGFA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIAceQQydsSYDARCDVWSLGI 233
Cdd:cd14177   150 KQLRGENGLLLTPCYTANFVAPEVLM--RQ---GYDAACDIWSLGV 190
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
40-301 9.29e-20

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 90.79  E-value: 9.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGK-VYKvtNKRDGSLAAVKILDP--VSDMDEEIeaeyNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd13982     7 KVLGYGSEGTiVFR--GTFDGRPVAVKRLLPefFDFADREV----QLLRESDEHPNVIRYFCTEKDRQF-----LYIALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGgSVTELVKGLLRCGQRLDEAMISY-ILYGALLGLQHLHNNRIIHRDVKGNNILLTT-----EGGVKLVDFGVSAQL 190
Cdd:cd13982    76 LCAA-SLQDLVESPRESKLFLRPGLEPVrLLRQIASGLAHLHSLNIVHRDLKPQNILISTpnahgNVRAMISDFGLCKKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 ---TSTRLRRNTSVGTPFWMAPEVIacEQQYDSSYDARCDVWSLG-ITAIELGDGdpplfdMHPVKTLFKIPRN------ 260
Cdd:cd13982   155 dvgRSSFSRRSGVAGTSGWIAPEML--SGSTKRRQTRAVDIFSLGcVFYYVLSGG------SHPFGDKLEREANilkgky 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578803747  261 PPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd13982   227 SLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
42-296 9.50e-20

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 90.65  E-value: 9.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNIlqflpNHPNVVKFYGMFYKadhcvGGQLWLVLELCNGG 121
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGL-----TSPRVVPLYGAVRE-----GPWVNIFMDLKEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG-VKLVDFGVSAQL-----TSTRL 195
Cdd:cd13991    84 SLGQLIKEQ----GCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLdpdglGKSLF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKwCeef 275
Cdd:cd13991   160 TGDYIPGTETHMAPEVVLGK-----PCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPLREIPPS-C--- 230
                         250       260
                  ....*....|....*....|....*
gi 578803747  276 NHFISQC----LIKDFERRPSVTHL 296
Cdd:cd13991   231 APLTAQAiqagLRKEPVHRASAAEL 255
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
37-247 1.02e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 94.86  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvsDM--DEEIeaeynILQF---------LpNHPNVVKFYgmfykaDh 105
Cdd:NF033483   10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRP--DLarDPEF-----VARFrreaqsaasL-SHPNIVSVY------D- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 cVG---GQLWLVLELCNGgsvtELVKGLLRCGQRL--DEAMisYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK 180
Cdd:NF033483   75 -VGedgGIPYIVMEYVDG----RTLKDYIREHGPLspEEAV--EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  181 LVDFGVSAQLTSTRLRRNTSV-GTPFWMAPeviacEQQYDSSYDARCDVWSLGITAIELGDGDPPlFD 247
Cdd:NF033483  148 VTDFGIARALSSTTMTQTNSVlGTVHYLSP-----EQARGGTVDARSDIYSLGIVLYEMLTGRPP-FD 209
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
42-300 1.09e-19

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 90.59  E-value: 1.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVK---ILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCvggqlWLVLELC 118
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKclhSSPNCIEERKALLKEAEKMERA-RHSYVLPLLGVCVERRSL-----GLVMEYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELVKgllRCGQRLDEAMISYILYGALLGLQHLHNNR--IIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL- 195
Cdd:cd13978    75 ENGSLKSLLE---REIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISa 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 -RRNTS---VGTPFWMAPEVIAcEQQYDSsyDARCDVWSLGITAIELGDGDPPLFD-MHPVKTLFKI-----PRNPPPTL 265
Cdd:cd13978   152 nRRRGTenlGGTPIYMAPEAFD-DFNKKP--TSKSDVYSFAIVIWAVLTRKEPFENaINPLLIMQIVskgdrPSLDDIGR 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578803747  266 LHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd13978   229 LKQIENVQELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
34-301 1.11e-19

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 90.48  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE--IEAEYNILQFLpNHPNVVKfygMFYKADhcVGGQL 111
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhlIENEVSILRRV-KHPNIIM---LIEEMD--TPAEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGLLRCGQRLDEAMIsyilYGALLGLQHLHNNRIIHRDVKGNNILLTT----EGGVKLVDFGVS 187
Cdd:cd14184    75 YLVMELVKGGDLFDAITSSTKYTERDASAMV----YNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLrrnTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPP----------LFDMHPVKTLfki 257
Cdd:cd14184   151 TVVEGPLY---TVCGTPTYVAPEIIA-----ETGYGLKVDIWAAGVITYILLCGFPPfrsennlqedLFDQILLGKL--- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578803747  258 pRNPPPtllHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14184   220 -EFPSP---YWDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
40-331 1.23e-19

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 90.79  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKvtNKRDGSLAAVKILdpvSDMDEEI-EAEYNILQF-LPNHPNVVKFYGmfykAD-HCVGG--QLWLV 114
Cdd:cd14056     1 KTIGKGRYGEVWL--GKYRGEKVAVKIF---SSRDEDSwFRETEIYQTvMLRHENILGFIA----ADiKSTGSwtQLWLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSvteLVKGLLRCgqRLDEAMISYILYGALLGLQHLHNN--------RIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd14056    72 TEYHEHGS---LYDYLQRN--TLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 ----SAQLTSTRLRRNTSVGTPFWMAPEVIAcEQQYDSSYDA--RCDVWSLGITAIEL-------GDGD---PPLFDMHP 250
Cdd:cd14056   147 avryDSDTNTIDIPPNPRVGTKRYMAPEVLD-DSINPKSFESfkMADIYSFGLVLWEIarrceigGIAEeyqLPYFGMVP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  251 vktlfkiprnPPPTLlhpekwcEEFNHFIsqCLIKdfeRRPSVT-HLLDHPFIkgvhgkvlflqKQLAKVLQDQKHQNPV 329
Cdd:cd14056   226 ----------SDPSF-------EEMRKVV--CVEK---LRPPIPnRWKSDPVL-----------RSMVKLMQECWSENPH 272

                  ..
gi 578803747  330 AK 331
Cdd:cd14056   273 AR 274
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
40-303 1.29e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 90.86  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILD-----PVSDMDEEIEAEY------NILQFLPnhpnvvkfygmFYKADHCvg 108
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEknaghSRSRVFREVETLYqcqgnkNILELIE-----------FFEDDTR-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDF- 184
Cdd:cd14174    75 --FYLVFEKLRGGSILAHIQKR----KHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPdkvSPVKICDFd 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 -GVSAQLTS-----TRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPL---------FDMH 249
Cdd:cd14174   149 lGSGVKLNSactpiTTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgWDRG 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  250 PV-----KTLFKipRNPPPTLLHPEK-WCE---EFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14174   229 EVcrvcqNKLFE--SIQEGKYEFPDKdWSHissEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
37-306 1.31e-19

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 92.79  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYkVTNKRD-GSLAAVKIL--DPVSDMDE--EIEAEYNILQfLPNHPNVVKFYGMFYKADHcvggqL 111
Cdd:cd05600    14 QILTQVGQGGYGSVF-LARKKDtGEICALKIMkkKVLFKLNEvnHVLTERDILT-TTNSPWLVKLLYAFQDPEN-----V 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELV--KGLLRCGQrldeamISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA- 188
Cdd:cd05600    87 YLAMEYVPGGDFRTLLnnSGILSEEH------ARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 ----------------------QLTSTRLRRNT--------------SVGTPFWMAPEVIACEQqydssYDARCDVWSLG 232
Cdd:cd05600   161 tlspkkiesmkirleevkntafLELTAKERRNIyramrkedqnyansVVGSPDYMAPEVLRGEG-----YDLTVDYWSLG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  233 ITAIELGDGDPPLFDMHPVKTLFKIpRNPPPTLLHP--EKWCEEFN------HFISQCLIKDFERRPSVTHLLDHPFIKG 304
Cdd:cd05600   236 CILFECLVGFPPFSGSTPNETWANL-YHWKKTLQRPvyTDPDLEFNlsdeawDLITKLITDPQDRLQSPEQIKNHPFFKN 314

                  ..
gi 578803747  305 VH 306
Cdd:cd05600   315 ID 316
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
42-247 1.36e-19

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 91.30  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIEA---EYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKILKKdVIIQDDDVECtmvEKRVLALSGKPPFLTQLHSCFQTMD-----RLYFVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGqRLDEAMIsyILYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd05587    79 VNGG---DLMYHIQQVG-KFKEPVA--VFYAAeiAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGK 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578803747  196 RRNTSVGTPFWMAPEVIAcEQQYDSSydarCDVWSLGITAIELGDGDPPlFD 247
Cdd:cd05587   153 TTRTFCGTPDYIAPEIIA-YQPYGKS----VDWWAYGVLLYEMLAGQPP-FD 198
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
36-298 1.38e-19

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 90.64  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK--ILDPVSDMD-EEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqLW 112
Cdd:cd14049     8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKkiLIKKVTKRDcMKVLREVKVLAGL-QHPNIVGYHTAWMEHVQLM---LY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKGLLRCGQRLDEA---------MISYILYGALLGLQHLHNNRIIHRDVKGNNILLT-TEGGVKLV 182
Cdd:cd14049    84 IQMQLCELSLWDWIVERNKRPCEEEFKSapytpvdvdVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  183 DFGVSAQL-------TSTRLRRNTS-----VGTPFWMAPeviacEQQYDSSYDARCDVWSLGITAIELgdGDPPLFDMHP 250
Cdd:cd14049   164 DFGLACPDilqdgndSTTMSRLNGLthtsgVGTCLYAAP-----EQLEGSHYDFKSDMYSIGVILLEL--FQPFGTEMER 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  251 VKTLFKIPRNPPPTLLhpEKWCEEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd14049   237 AEVLTQLRNGQIPKSL--CKRWPVQAKYIKLLTSTEPSERPSASQLLE 282
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
32-316 1.42e-19

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 91.01  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVT----NKRDGSL-AAVKILDPVSDMDEE--IEAEYNILQFLPNHPNVVKFYGMFYKad 104
Cdd:cd05055    33 PRNNLSFGKTLGAGAFGKVVEATayglSKSDAVMkVAVKMLKPTAHSSEReaLMSELKIMSHLGNHENIVNLLGACTI-- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 hcvGGQLWLVLELCNGGSvtelvkgLLRCGQRLDEAMISY-----ILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV 179
Cdd:cd05055   111 ---GGPILVITEYCCYGD-------LLNFLRRKRESFLTLedllsFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIV 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  180 KLVDFGVSAQLTSTrlRRNTSVGTPF----WMAPEVIaceqqYDSSYDARCDVWSLGITAIELGD-GDPPLFDMhPVKTL 254
Cdd:cd05055   181 KICDFGLARDIMND--SNYVVKGNARlpvkWMAPESI-----FNCVYTFESDVWSYGILLWEIFSlGSNPYPGM-PVDSK 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  255 FKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDhpfikgvhgkvlFLQKQL 316
Cdd:cd05055   253 FYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQ------------LIGKQL 302
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
38-302 1.44e-19

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 90.24  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKV-----YKVTNKRDGSLAAVKIL--DPVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMFyKADHCVG 108
Cdd:cd14076     5 LGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIrrDTQQENCQTskIMREINILKGL-THPNIVRLLDVL-KTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqlwLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd14076    83 ----IVLEFVSGG---ELFDYILA-RRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFAN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QL-TSTRLRRNTSVGTPFWMAPEVIACeqqyDSSYDAR-CDVWSLGIT--AIELG----DGDPPLFDMHPVKTLFKIPRN 260
Cdd:cd14076   155 TFdHFNGDLMSTSCGSPCYAAPELVVS----DSMYAGRkADIWSCGVIlyAMLAGylpfDDDPHNPNGDNVPRLYRYICN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  261 PPptLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14076   231 TP--LIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
36-233 1.45e-19

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 91.46  E-value: 1.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDEEIE---AEYNILQFLPN-HPNVVKFY-------GMFYKAD 104
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIR--CNAPENVElalREFWALSSIQRqHPNVIQLEecvlqrdGLAQRMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 H--------------CVGGQ----------LWLVLELCNGGSVTELVkgLLRcgqRLDEAMISYILYGALLGLQHLHNNR 160
Cdd:cd13977    80 HgssksdlylllvetSLKGErcfdprsacyLWFVMEFCDGGDMNEYL--LSR---RPDRQTNTSFMLQLSSALAFLHRNQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  161 IIHRDVKGNNILLTTEGG---VKLVDFGVSAQLTSTRLRR-----------NTSVGTPFWMAPEViaceqqYDSSYDARC 226
Cdd:cd13977   155 IVHRDLKPDNILISHKRGepiLKVADFGLSKVCSGSGLNPeepanvnkhflSSACGSDFYMAPEV------WEGHYTAKA 228

                  ....*..
gi 578803747  227 DVWSLGI 233
Cdd:cd13977   229 DIFALGI 235
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
31-303 1.51e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 90.89  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA-------EYNILQFLpNHPNVVKFygmfykA 103
Cdd:cd07845     4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVR----MDNERDGipisslrEITLLLNL-RHPNIVEL------K 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  104 DHCVGGQL---WLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK 180
Cdd:cd07845    73 EVVVGKHLdsiFLVMEYCE----QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVsAQLTSTRLRRNT-SVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDP---------------- 243
Cdd:cd07845   149 IADFGL-ARTYGLPAKPMTpKVVTLWYRAPELLLGCTTYTTA----IDMWAVGCILAELLAHKPllpgkseieqldliiq 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  244 ----------PLFDMHPVKTLFKIPRNPPPTLLHPEKWCEEFN-HFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd07845   224 llgtpnesiwPGFSDLPLVGKFTLPKQPYNNLKHKFPWLSEAGlRLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
42-377 1.60e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 91.22  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDE--EIEAEYNILQFlPNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILrkEVIIAKDEvaHTVTESRVLQN-TRHPFLTALKYAFQTHD-----RLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRcgQRL---DEAMisyiLYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd05595    77 ANGG---ELFFHLSR--ERVfteDRAR----FYGAEIvsALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDM-HpvKTLF--------KIPRNPPP 263
Cdd:cd05595   148 DGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQdH--ERLFelilmeeiRFPRTLSP 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  264 tllhpekwceEFNHFISQCLIKDFERR----PS-VTHLLDHPFIKGVHGKVLfLQKQLAKVLQDQKHQNpvAKTRH-ERM 337
Cdd:cd05595   221 ----------EAKSLLAGLLKKDPKQRlgggPSdAKEVMEHRFFLSINWQDV-VQKKLLPPFKPQVTSE--VDTRYfDDE 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 578803747  338 HTRRPYHVEDAEKYCleddlvNLEVLDEDTIIHQLQKRYA 377
Cdd:cd05595   288 FTAQSITITPPDRYD------SLDLLESDQRTHFPQFSYS 321
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
36-301 1.78e-19

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 89.62  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP--VSDMDEEIEAEYNILQFLpNHPNVVKFYGMfYKADhcvgGQLWL 113
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKskLKGKEDMIESEILIIKSL-SHPNIVKLFEV-YETE----KEIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGG----SVTELVKgllrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT----TEGGVKLVDFG 185
Cdd:cd14185    76 ILEYVRGGdlfdAIIESVK--------FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRLrrnTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDM-HPVKTLFKIPRNPPPT 264
Cdd:cd14185   148 LAKYVTGPIF---TVCGTPTYVAPEILS-----EKGYGLEVDMWAAGVILYILLCGFPPFRSPeRDQEELFQIIQLGHYE 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  265 LLHP--EKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14185   220 FLPPywDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
42-298 1.82e-19

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 90.26  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFY--KADHCVGGQLWLVL-EL 117
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAASigKEESDQGQAEYLLLtEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKglLRCGQRLDEAMISYILYGALLGLQHLHNNR--IIHRDVKGNNILLTTEGGVKLVDFGV--------- 186
Cdd:cd14036    88 CKGQLVDFVKK--VEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSatteahypd 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 ---SAQ---LTSTRLRRNTsvgTPFWMAPEVIACEQQYDSSydARCDVWSLGITAIELgdgdppLFDMHP---------V 251
Cdd:cd14036   166 yswSAQkrsLVEDEITRNT---TPMYRTPEMIDLYSNYPIG--EKQDIWALGCILYLL------CFRKHPfedgaklriI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  252 KTLFKIPRNPPP-TLLHPekwceefnhFISQCLIKDFERRPSVTHLLD 298
Cdd:cd14036   235 NAKYTIPPNDTQyTVFHD---------LIRSTLKVNPEERLSITEIVE 273
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
42-291 1.90e-19

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 89.37  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKvtNKRDGSLAaVKILDPVSDMDEEIEAEYNILQFL--PNHPNVVKFYGMFYKAdhcvggQLWLVLELCN 119
Cdd:cd14062     1 IGSGSFGTVYK--GRWHGDVA-VKKLNVTDPTPSQLQAFKNEVAVLrkTRHVNILLFMGYMTKP------QLAIVTQWCE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT--STRLRR 197
Cdd:cd14062    72 GSS---LYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTrwSGSQQF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  198 NTSVGTPFWMAPEVIacEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPV-KTLFKIPRNppptLLHPE------K 270
Cdd:cd14062   149 EQPTGSILWMAPEVI--RMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRdQILFMVGRG----YLRPDlskvrsD 222
                         250       260
                  ....*....|....*....|.
gi 578803747  271 WCEEFNHFISQCLIKDFERRP 291
Cdd:cd14062   223 TPKALRRLMEDCIKFQRDERP 243
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
42-256 2.07e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 91.21  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIE---AEYNILQFLPNHPNVVKFYGMFYKADhcvggQLWLVLEL 117
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKdVVIQDDDVEctmVEKRVLALQDKPPFLTQLHSCFQTVD-----RLYFVMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRCGQRLDEAMISYILYGALlGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05615    93 VNGG---DLMYHIQQVGKFKEPQAVFYAAEISV-GLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTT 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  198 NTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFK 256
Cdd:cd05615   169 RTFCGTPDYIAPEIIAYQ-----PYGRSVDWWAYGVLLYEMLAGQPP-FDGEDEDELFQ 221
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
31-305 2.62e-19

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 93.01  E-value: 2.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADHC-- 106
Cdd:PTZ00283   29 EQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNcdFFSIVKCHEDFAKKDPRnp 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 -VGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:PTZ00283  109 eNVLMIALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VS---AQLTSTRLRRnTSVGTPFWMAPEViaceqQYDSSYDARCDVWSLGITAIEL------GDGDpplfDMHPV--KTL 254
Cdd:PTZ00283  189 FSkmyAATVSDDVGR-TFCGTPYYVAPEI-----WRRKPYSKKADMFSLGVLLYELltlkrpFDGE----NMEEVmhKTL 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  255 ---FkiprNPPPTLLHPekwceEFNHFISQCLIKDFERRPSVTHLLDHP----FIKGV 305
Cdd:PTZ00283  259 agrY----DPLPPSISP-----EMQEIVTALLSSDPKRRPSSSKLLNMPicklFISGL 307
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
40-299 2.66e-19

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 89.15  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILD----PVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFykadHCVGGQLWLVL 115
Cdd:cd14164     6 TTIGEGSFSKVKLATSQKYCCKVAIKIVDrrraSPDFVQKFLPRELSILRRV-NHPNIVQMFECI----EVANGRLYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ElcngGSVTELVKGLLRCGqrLDEAMISYILYGALLG-LQHLHNNRIIHRDVKGNNILLTTEG-GVKLVDFGVSAQLTST 193
Cdd:cd14164    81 E----AAATDLLQKIQEVH--HIPKDLARDMFAQMVGaVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTSVGTPFWMAPEVIAceqqyDSSYDA-RCDVWSLGITAIELGDGDPPlFDmhpvKTLFKIPRNPPPTLLHPE--K 270
Cdd:cd14164   155 PELSTTFCGSRAYTPPEVIL-----GTPYDPkKYDVWSLGVVLYVMVTGTMP-FD----ETNVRRLRLQQRGVLYPSgvA 224
                         250       260
                  ....*....|....*....|....*....
gi 578803747  271 WCEEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd14164   225 LEEPCRALIRTLLQFNPSTRPSIQQVAGN 253
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
42-314 2.71e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 90.49  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVS---DMDEEIEAEYNILQFLPNH---PNVVKFYGMFYKADhcvggQLWLVL 115
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLVSTgdcPFIVCMSYAFHTPD-----KLSFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLtsTRL 195
Cdd:cd14223    83 DLMNGG---DLHYHLSQHGV-FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDF--SKK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIaceqQYDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPTLLH-PEKWCEE 274
Cdd:cd14223   157 KPHASVGTHGYMAPEVL----QKGVAYDSSADWFSLGCMLFKLLRGHSP-FRQHKTKDKHEIDRMTLTMAVElPDSFSPE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  275 FNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd14223   232 LRSLLEGLLQRDVNRRlgcmgRGAQEVKEEPFFRGLDWQMVFLQK 276
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
40-292 2.80e-19

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 88.83  E-value: 2.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVK----ILDPvsDMDEEIEAEYNIL-QFlpNHPNVVKFYGMfykadhCVGGQ-LWL 113
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKscreTLPP--DLKAKFLQEARILkQY--SHPNIVRLIGV------CTQKQpIYI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGsvtELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ---- 189
Cdd:cd05084    72 VMELVQGG---DFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREeedg 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 -LTSTRLRRNTSVGtpfWMAPEVIaceqQYdSSYDARCDVWSLGITAIE-LGDGDPPLFDMHPVKTLFKIPRNppPTLLH 267
Cdd:cd05084   149 vYAATGGMKQIPVK---WTAPEAL----NY-GRYSSESDVWSFGILLWEtFSLGAVPYANLSNQQTREAVEQG--VRLPC 218
                         250       260
                  ....*....|....*....|....*
gi 578803747  268 PEKWCEEFNHFISQCLIKDFERRPS 292
Cdd:cd05084   219 PENCPDEVYRLMEQCWEYDPRKRPS 243
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
39-300 3.70e-19

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 89.22  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEA--EYNILQFLPNHPNVVKFYGMFYKADHCVggqlwLVL 115
Cdd:cd14139     5 LEKIGVGEFGSVYKCIKRLDGCVYAIKrSMRPFAGSSNEQLAlhEVYAHAVLGHHPHVVRYYSAWAEDDHMI-----IQN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL----LTTEGGV------------ 179
Cdd:cd14139    80 EYCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFichkMQSSSGVgeevsneedefl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  180 ------KLVDFGVSAQLTSTRLRRntsvGTPFWMAPEVIaceqQYDSSYDARCDVWSLGITaIELGDGDPPL----FDMH 249
Cdd:cd14139   160 sanvvyKIGDLGHVTSINKPQVEE----GDSRFLANEIL----QEDYRHLPKADIFALGLT-VALAAGAEPLptngAAWH 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  250 PVKTlfkipRNPPPTllhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14139   231 HIRK-----GNFPDV---PQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
39-298 6.51e-19

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 88.59  E-value: 6.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKV--TNKRD--GSLAAVKILDP------VSDMDEEIEaeynILQFLpNHPNVVKFYGMFYKADhcvG 108
Cdd:cd05038     9 IKQLGEGHFGSVELCryDPLGDntGEQVAVKSLQPsgeeqhMSDFKREIE----ILRTL-DHEYIVKYKGVCESPG---R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVtelvKGLLRcGQRLDEAMISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd05038    81 RSLRLIMEYLPSGSL----RDYLQ-RHRDQIDLKRLLLFASQIckGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTR--LRRNTSVGTP-FWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL-GDGDPplfDMHPVKTLFKI--PRN 260
Cdd:cd05038   156 AKVLPEDKeyYYVKEPGESPiFWYAPECLR-----ESRFSSASDVWSFGVTLYELfTYGDP---SQSPPALFLRMigIAQ 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  261 PPPTLLH-------------PEKWCEEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd05038   228 GQMIVTRllellksgerlprPPSCPDEVYDLMKECWEYEPQDRPSFSDLIL 278
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
33-302 6.58e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 88.14  E-value: 6.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE-IEAEYNILQFLpNHPNVVKFYGMFYKADHCVggql 111
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKEnIRQEISIMNCL-HHPKLVQCVDAFEEKANIV---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 wLVLELCNGGsvtELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQ 189
Cdd:cd14191    76 -MVLEMVSGG---ELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtkIKLIDFGLARR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRnTSVGTPFWMAPEVIACEQqydSSYDArcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRnppptllhpE 269
Cdd:cd14191   152 LENAGSLK-VLFGTPEFVAPEVINYEP---IGYAT--DMWSIGVICYILVSGLSPFMGDNDNETLANVTS---------A 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  270 KW----------CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14191   217 TWdfddeafdeiSDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
37-244 7.19e-19

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 88.15  E-value: 7.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKvtNKRDGSLAaVKILDPVSDMDEEIEAEYNILQFL--PNHPNVVKFYGMFYKAdhcvggQLWLV 114
Cdd:cd14150     3 SMLKRIGTGSFGTVFR--GKWHGDVA-VKILKVTEPTPEQLQAFKNEMQVLrkTRHVNILLFMGFMTRP------NFAII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAqlTSTR 194
Cdd:cd14150    74 TQWCEGSS---LYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAT--VKTR 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747  195 LRRNTSVGTP----FWMAPEVIacEQQYDSSYDARCDVWSLGITAIELGDGDPP 244
Cdd:cd14150   149 WSGSQQVEQPsgsiLWMAPEVI--RMQDTNPYSFQSDVYAYGVVLYELMSGTLP 200
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
42-297 7.48e-19

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 88.71  E-value: 7.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKvtNKRDGSLAAVKILDPVSDMDEE-----IEAEYNILQFLpNHPNVVKFYGMfykadHCVGGQLWLVLE 116
Cdd:cd14158    23 LGEGGFGVVFK--GYINDKNVAVKKLAAMVDISTEdltkqFEQEIQVMAKC-QHENLVELLGY-----SCDGPQLCLVYT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGL-----LRCGQRLDeamisyILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV---SA 188
Cdd:cd14158    95 YMPNGSLLDRLACLndtppLSWHMRCK------IAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLaraSE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTsVGTPFWMAPEVIACEqqydssYDARCDVWSLGITAIELGDGDPPlFDMHpvktlfkipRNPPPTLLHP 268
Cdd:cd14158   169 KFSQTIMTERI-VGTTAYMAPEALRGE------ITPKSDIFSFGVVLLEIITGLPP-VDEN---------RDPQLLLDIK 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  269 EKWCEE----------------------FNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd14158   232 EEIEDEektiedyvdkkmgdwdstsieaMYSVASQCLNDKKNRRPDIAKVQ 282
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
36-302 7.65e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 88.48  E-value: 7.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD--------PVSDMdEEIEAEYNILQFlpNHPNVVKFYGMFYKADHCV 107
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtnedglPLSTV-REVALLKRLEAF--DHPNIVRLMDVCATSRTDR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 GGQLWLVLELCNGGSVTELVKgLLRCGQRLDEamISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVs 187
Cdd:cd07863    79 ETKVTLVFEHVDQDLRTYLDK-VPPPGLPAET--IKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGL- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKI---------- 257
Cdd:cd07863   155 ARIYSCQMALTPVVVTLWYRAPEVL-----LQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIfdliglpped 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  258 --------------PRNPPPTllhpEKWCEEFNHFISQCLIK----DFERRPSVTHLLDHPFI 302
Cdd:cd07863   230 dwprdvtlprgafsPRGPRPV----QSVVPEIEESGAQLLLEmltfNPHKRISAFRALQHPFF 288
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
34-314 1.10e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 89.37  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP-VSDMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADhcvggQ 110
Cdd:cd05593    15 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKeVIIAKDEVAHTLTESRVLKNtrHPFLTSLKYSFQTKD-----R 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGsvtELVKGLLRcGQRLDEAMISYilYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05593    90 LCFVMEYVNGG---ELFFHLSR-ERVFSEDRTRF--YGAEIvsALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKtLFKIPRNppPTLLHP 268
Cdd:cd05593   164 EGITDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-LFELILM--EDIKFP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  269 EKWCEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05593   236 RTLSADAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFTGVNWQDVYDKK 286
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
21-257 1.13e-18

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 90.07  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   21 PMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILqfLPNHPNVVKF 96
Cdd:cd05623    59 PFTSKVKQMRLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETAcfreERDVL--VNGDSQWITT 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   97 YGMFYKADHcvggQLWLVLELCNGGSVTELvkgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE 176
Cdd:cd05623   137 LHYAFQDDN----NLYLVMDYYVGGDLLTL---LSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMN 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  177 GGVKLVDFGVSAQLTST-RLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLF 255
Cdd:cd05623   210 GHIRLADFGSCLKLMEDgTVQSSVAVGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYG 289

                  ..
gi 578803747  256 KI 257
Cdd:cd05623   290 KI 291
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
34-306 1.25e-18

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 88.89  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILD-PVSDmdeEIEA-----EYNILQFLpNHPNVVKFYGMFYKADHCV 107
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSrPFQS---AIHAkrtyrELRLLKHM-KHENVIGLLDVFTPASSLE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 G-GQLWLVLELCNggsvTELVKgLLRCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd07851    91 DfQDVYLVTHLMG----ADLNN-IVKC-QKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 sAQLTSTRLrrNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLFD----MHPVKTLFKIPRNPP 262
Cdd:cd07851   165 -ARHTDDEM--TGYVATRWYRAPEIMLNWMHYNQT----VDIWSVGCIMAELLTGK-TLFPgsdhIDQLKRIMNLVGTPD 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  263 PTLL-----------------HPEKwceEFNH-----------FISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07851   237 EELLkkissesarnyiqslpqMPKK---DFKEvfsganplaidLLEKMLVLDPDKRITAAEALAHPYLAEYH 305
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
40-303 1.41e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 87.37  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSL-AAVKILDPVSDMDEEI--EAEYNILQFLpNHPNVVKFYGMfykadHCVGGQLWLVLE 116
Cdd:cd14201    12 DLVGHGAFAVVFKGRHRKKTDWeVAIKSINKKNLSKSQIllGKEIKILKEL-QHENIVALYDV-----QEMPNSVFLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELV--KGLLRcgqrldEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG---------GVKLVDFG 185
Cdd:cd14201    86 YCNGGDLADYLqaKGTLS------EDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRLRRnTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHP--VKTLFKIPRNPPP 263
Cdd:cd14201   160 FARYLQSNMMAA-TLCGSPMYMAPEVIMSQH-----YDAKADLWSIGTVIYQCLVGKPPFQANSPqdLRMFYEKNKNLQP 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  264 TLlhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14201   234 SI--PRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
34-305 1.71e-18

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 89.33  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLPNHPNVVKFYGMFYKADhcvgg 109
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEqvghIRAERDILVEADSLWVVKMFYSFQDKLN----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05628    76 -LYLIMEFLPGGDMMTL----LMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 L--------------------------------TSTRLRRN---TSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGIT 234
Cdd:cd05628   151 LkkahrtefyrnlnhslpsdftfqnmnskrkaeTWKRNRRQlafSTVGTPDYIAPEVFM-----QTGYNKLCDWWSLGVI 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  235 AIELGDGDPPLFDMHPVKTLFKIpRNPPPTLLHPE-------------KWCEEFNHFISQclikdferrPSVTHLLDHPF 301
Cdd:cd05628   226 MYEMLIGYPPFCSETPQETYKKV-MNWKETLIFPPevpisekakdlilRFCCEWEHRIGA---------PGVEEIKTNPF 295

                  ....
gi 578803747  302 IKGV 305
Cdd:cd05628   296 FEGV 299
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-304 1.81e-18

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 87.80  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvg 108
Cdd:cd14168     7 DIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIpkKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNH--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELV--KGLLrcgqrlDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---EGGVKLVD 183
Cdd:cd14168    83 --LYLVMQLVSGGELFDRIveKGFY------TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSqdeESKIMISD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSaQLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR---- 259
Cdd:cd14168   155 FGLS-KMEGKGDVMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKadye 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  260 -NPPptllHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKG 304
Cdd:cd14168   229 fDSP----YWDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAG 270
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
21-248 1.98e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 88.94  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   21 PMMLGLESlpdptdtWEIIETIGKGTYGKVYKVTNKRDGSLAAVKIL--DPVSDmDEEI---EAEYNILQFLPNHPNVVK 95
Cdd:cd05618    14 SSSLGLQD-------FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVkkELVND-DEDIdwvQTEKHVFEQASNHPFLVG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   96 FYGMFYKADhcvggQLWLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT 175
Cdd:cd05618    86 LHSCFQTES-----RLFFVIEYVNGG---DLMFHMQR-QRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDS 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  176 EGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDM 248
Cdd:cd05618   157 EGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGE-----DYGFSVDWWALGVLMFEMMAGRSP-FDI 223
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
42-314 2.19e-18

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 88.19  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVS---DMDEEIEAEYNILQFLPNH---PNVVKFYGMFYKADhcvggQLWLVL 115
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPD-----KLCFIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGsvtELVKGLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLtsTRL 195
Cdd:cd05633    88 DLMNGG---DLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDF--SKK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNTSVGTPFWMAPEVIaceqQYDSSYDARCDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPPPTLLH-PEKWCEE 274
Cdd:cd05633   162 KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSP-FRQHKTKDKHEIDRMTLTVNVElPDSFSPE 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  275 FNHFISQCLIKDFERRPSV-----THLLDHPFIKGVHGKVLFLQK 314
Cdd:cd05633   237 LKSLLEGLLQRDVSKRLGChgrgaQEVKEHSFFKGIDWQQVYLQK 281
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
34-297 2.83e-18

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 86.65  E-value: 2.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIE-------TIGKGTYGKVYKvtNKRDGSLAaVKILDPVSDMDEEIEAEYNILQFL--PNHPNVVKFYGMFYKAd 104
Cdd:cd14151     1 DDWEIPDgqitvgqRIGSGSFGTVYK--GKWHGDVA-VKMLNVTAPTPQQLQAFKNEVGVLrkTRHVNILLFMGYSTKP- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 hcvggQLWLVLELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd14151    77 -----QLAIVTQWCEGSS---LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 G---VSAQLTSTRLRRNTSvGTPFWMAPEVIacEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPV-KTLFKIPRN 260
Cdd:cd14151   149 GlatVKSRWSGSHQFEQLS-GSILWMAPEVI--RMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRG 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578803747  261 P-PPTLLHPEKWC-EEFNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd14151   226 YlSPDLSKVRSNCpKAMKRLMAECLKKKRDERPLFPQIL 264
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
41-296 3.86e-18

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 86.56  E-value: 3.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   41 TIGKGTYGKVYKVTNKRDGSLA-----AVKILDPVSDMDE--EIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvgGQLWL 113
Cdd:cd05045     7 TLGEGEFGKVVKATAFRLKGRAgyttvAVKMLKENASSSElrDLLSEFNLLKQV-NHPHVIKLYGACSQD-----GPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVK------------GLLRCGQRLDEAMISYILYGALL--------GLQHLHNNRIIHRDVKGNNILL 173
Cdd:cd05045    81 IVEYAKYGSLRSFLResrkvgpsylgsDGNRNSSYLDNPDERALTMGDLIsfawqisrGMQYLAEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  174 TTEGGVKLVDFGVSAQL--TSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIE---LG----DGDPP 244
Cdd:cd05045   161 AEGRKMKISDFGLSRDVyeEDSYVKRSKGRIPVKWMAIESLF-----DHIYTTQSDVWSFGVLLWEivtLGgnpyPGIAP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747  245 --LFDMhpVKTLFKIPRnppptllhPEKWCEEFNHFISQCLIKDFERRPSVTHL 296
Cdd:cd05045   236 erLFNL--LKTGYRMER--------PENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
34-259 4.10e-18

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 86.43  E-value: 4.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKilDPVSDMDEE-----IEAEYNILQFLPNHPNVVKFYGMFYkADHCVG 108
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALK--KTRLEMEEEgvpstALREVSLLQMLSQSIYIVRLLDVEH-VEENGK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNggsvTELVKGLLRCGQ----RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV-KLVD 183
Cdd:cd07837    78 PLLYLVFEYLD----TDLKKFIDSYGRgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIAD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  184 FGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR 259
Cdd:cd07837   154 LGLGRAFTIPIKSYTHEIVTLWYRAPEVLLGSTHYSTP----VDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFR 225
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
37-301 5.14e-18

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 85.80  E-value: 5.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGmfYKADhCVGGQLWLVL 115
Cdd:cd14037     6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKrVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYID--SSAN-RSGNGVYEVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ---ELCNGGSVTELVKGLLRcgQRLDEAMISYILYGALLGLQHLHNNR--IIHRDVKGNNILLTTEGGVKLVDFG-VSAQ 189
Cdd:cd14037    83 llmEYCKGGGVIDLMNQRLQ--TGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGsATTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTR-----------LRRNTsvgTPFWMAPEVIaceQQYDS-SYDARCDVWSLGITAIELGDGDPPLFDMHPVKTL--- 254
Cdd:cd14037   161 ILPPQtkqgvtyveedIKKYT---TLQYRAPEMI---DLYRGkPITEKSDIWALGCLLYKLCFYTTPFEESGQLAILngn 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  255 FKIPRNPpptllhpeKWCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14037   235 FTFPDNS--------RYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
31-303 5.67e-18

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 85.85  E-value: 5.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIET-------IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQfLPNHPNVVKFYGMFYKa 103
Cdd:cd14149     2 DSSYYWEIEASevmlstrIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLR-KTRHVNILLFMGYMTK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  104 dhcvgGQLWLVLELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd14149    80 -----DNLAIVTQWCEGSS---LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQLT--STRLRRNTSVGTPFWMAPEVIacEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPV-KTLFKIPRN 260
Cdd:cd14149   152 FGLATVKSrwSGSQQVEQPTGSILWMAPEVI--RMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRdQIIFMVGRG 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  261 -PPPTLLHPEKWC-EEFNHFISQCLIKDFERRP------SVTHLLDHPFIK 303
Cdd:cd14149   230 yASPDLSKLYKNCpKAMKRLVADCIKKVKEERPlfpqilSSIELLQHSLPK 280
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
37-302 5.84e-18

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 85.41  E-value: 5.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIEtIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlwLVLE 116
Cdd:cd14113    11 EVAE-LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSL-QHPQLVGLLDTFETPTSYI-----LVLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVkglLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL---TTEGGVKLVDFGVSAQLTST 193
Cdd:cd14113    84 MADQGRLLDYV---VRWGN-LTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdqsLSKPTIKLADFGDAVQLNTT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 RLRRNTsVGTPFWMAPEVIACEQQYDSSydarcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR----NPPPTLLHPE 269
Cdd:cd14113   160 YYIHQL-LGSPEFAAPEIILGNPVSLTS-----DLWSIGVLTYVLLSGVSPFLDESVEETCLNICRldfsFPDDYFKGVS 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  270 KWCEEFNHFISQcliKDFERRPSVTHLLDHPFI 302
Cdd:cd14113   234 QKAKDFVCFLLQ---MDPAKRPSAALCLQEQWL 263
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
42-304 6.73e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 86.08  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHCvggqlWLVLELCNGG 121
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIIS--RRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHT-----YLVMELLRGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  122 SVTELVKGllrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVSaqltstRLRRN 198
Cdd:cd14180    87 ELLDRIKK----KARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA------RLRPQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  199 TS--VGTPF----WMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPL-------FDMHPVKTLFKIPRNPPPtl 265
Cdd:cd14180   157 GSrpLQTPCftlqYAAPELFS-----NQGYDESCDLWSLGVILYTMLSGQVPFqskrgkmFHNHAADIMHKIKEGDFS-- 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  266 LHPEKW---CEEFNHFISQCLIKDFERRPSVTHLLDHPFIKG 304
Cdd:cd14180   230 LEGEAWkgvSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQG 271
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
36-323 1.14e-17

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 86.23  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLPNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEdidwVQTEKHVFEQASSNPFLVGLHSCFQTTS-----RL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05617    92 FLVIEYVNGG---DLMFHMQR-QRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLF------DMHPVKTLFKIPRNPPPTL 265
Cdd:cd05617   168 GPGDTTSTFCGTPNYIAPEILRGEE-----YGFSVDWWALGVLMFEMMAGRSPFDiitdnpDMNTEDYLFQVILEKPIRI 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  266 lhPEKWCEEFNHFISQCLIKDFERR------PSVTHLLDHPFIKGVHGKVLfLQKQLAKVLQDQ 323
Cdd:cd05617   243 --PRFLSVKASHVLKGFLNKDPKERlgcqpqTGFSDIKSHTFFRSIDWDLL-EKKQVTPPFKPQ 303
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
36-266 1.14e-17

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 85.91  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFL-----PNHPNVVKFYGMFYKADHcvggq 110
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILDALrrkdrDNSHNVIHMKEYFYFRNH----- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCnGGSVTELVKGllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGVSA 188
Cdd:cd14225   120 LCITFELL-GMNLYELIKK--NNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGqsSIKVIDFGSSC 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QltsTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGdPPLF----DMHPVKTLFKIPRNPPPT 264
Cdd:cd14225   197 Y---EHQRVYTYIQSRFYRSPEVI-----LGLPYSMAIDMWSLGCILAELYTG-YPLFpgenEVEQLACIMEVLGLPPPE 267

                  ..
gi 578803747  265 LL 266
Cdd:cd14225   268 LI 269
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
32-302 1.28e-17

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 84.10  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggql 111
Cdd:cd14111     1 PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSL-HHERIMALHEAYITPRYLV---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 wLVLELCNGgsvTELVKGLLRCGQRLDEAMISYILYgALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14111    76 -LIAEFCSG---KELLHSLIDRFRYSEDDVVGYLVQ-ILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRR-NTSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNP-PPTLLHPe 269
Cdd:cd14111   151 PLSLRQlGRRTGTLEYMAPEMVKGE-----PVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKfDAFKLYP- 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  270 KWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14111   225 NVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
36-245 1.29e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 85.44  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFY---KADHCVGG 109
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDGFPITAlrEIKILKKL-KHPNVVPLIDMAVerpDKSKRKRG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVL-----ELCnggsvtelvkGLLRCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd07866    89 SVYMVTpymdhDLS----------GLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIAD 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  184 FGVSAQLTSTR----------LRRNTS-VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPL 245
Cdd:cd07866   159 FGLARPYDGPPpnpkggggggTRKYTNlVVTRWYRPPELLLGERRYTTA----VDIWGIGCVFAEMFTRRPIL 227
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
37-304 1.43e-17

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 86.34  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLP--NHPNVVKFYGMFYKADHCVGGQLWLV 114
Cdd:cd07853     3 EPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCffKHDNVLSALDILQPPHIDPFEEIYVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNggsvTELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLTSTR 194
Cdd:cd07853    83 TELMQ----SDLHKIIVS-PQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGL-ARVEEPD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTS--VGTPFWMAPEVIACEQQYDSSydarCDVWSLG-ITAIELGD--------------------GDPPLFDMH-- 249
Cdd:cd07853   157 ESKHMTqeVVTQYYRAPEILMGSRHYTSA----VDIWSVGcIFAELLGRrilfqaqspiqqldlitdllGTPSLEAMRsa 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  250 ---PVKTLFKIPRNPPP---TLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKG 304
Cdd:cd07853   233 cegARAHILRGPHKPPSlpvLYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
32-259 1.58e-17

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 85.02  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKV-------TNKRDGSLAAVKIL-DPVSDMD-EEIEAEYNILQFLPNHPNVVKFYGMfyk 102
Cdd:cd05099    10 PRDRLVLGKPLGEGCFGQVVRAeaygidkSRPDQTVTVAVKMLkDNATDKDlADLISEMELMKLIGKHKNIINLLGV--- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 adhCV-GGQLWLVLELCNGGSVTELVKG-------LLRCGQRLDEAMISY-----ILYGALLGLQHLHNNRIIHRDVKGN 169
Cdd:cd05099    87 ---CTqEGPLYVIVEYAAKGNLREFLRArrppgpdYTFDITKVPEEQLSFkdlvsCAYQVARGMEYLESRRCIHRDLAAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  170 NILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVG-TPF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIE---LGdGDPp 244
Cdd:cd05099   164 NVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGrLPVkWMAPEAL-----FDRVYTHQSDVWSFGILMWEiftLG-GSP- 236
                         250
                  ....*....|....*
gi 578803747  245 lFDMHPVKTLFKIPR 259
Cdd:cd05099   237 -YPGIPVEELFKLLR 250
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
39-246 2.03e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 84.07  E-value: 2.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd07836     5 LEKLGEGTYATVYKGRNRTTGEIVALKEIH--LDAEEGTPStairEISLMKEL-KHENIVRLHDVIHTEN-----KLMLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGgsvtELVKGLLRCGQR--LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd07836    77 FEYMDK----DLKKYMDTHGVRgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGI 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLF 246
Cdd:cd07836   153 PVNTFSNEVVTLWYRAPDVLLGSRTYSTS----IDIWSVGCIMAEMITGR-PLF 201
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
37-301 2.29e-17

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 83.43  E-value: 2.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRD-------GSLAAVKILDPVSDmDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHCVgg 109
Cdd:cd14019     4 RIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSS-PSRILNELECLERLGGSNNVSGLITAFRNEDQVV-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qlwLVLELCNGGSVTELVKgllrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL--TTEGGVkLVDFGVs 187
Cdd:cd14019    81 ---AVLPYIEHDDFRDFYR-------KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYnrETGKGV-LVDFGL- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTRLRRNTS-VGTPFWMAPEVI-ACEQQYDSsydarCDVWSLGITAIELGDGDPPLF----DMHPVKTLFKIprnp 261
Cdd:cd14019   149 AQREEDRPEQRAPrAGTRGFRAPEVLfKCPHQTTA-----IDIWSAGVILLSILSGRFPFFfssdDIDALAEIATI---- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  262 pptllhpekwceeFNH-----FISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14019   220 -------------FGSdeaydLLDKLLELDPSKRITAEEALKHPF 251
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
83-303 2.31e-17

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 85.16  E-value: 2.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   83 ILQFLPNHPNVVKFYGMFYKADHCVGGQ-LWLVLELCNGgSVTELVKgllrcgQRLDEAMISYILYGALLGLQHLHNNRI 161
Cdd:cd07850    51 VLMKLVNHKNIIGLLNVFTPQKSLEEFQdVYLVMELMDA-NLCQVIQ------MDLDHERMSYLLYQMLCGIKHLHSAGI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  162 IHRDVKGNNILLTTEGGVKLVDFGVsAQLTSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLG--------- 232
Cdd:cd07850   124 IHRDLKPSNIVVKSDCTLKILDFGL-ARTAGTSFMMTPYVVTRYYRAPEVI-----LGMGYKENVDIWSVGcimgemirg 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  233 ---------------ITAiELGDGDP-----------------PLFDMHPVKTLFKIPRNPPPTLLHPEKWCEEFNHFIS 280
Cdd:cd07850   198 tvlfpgtdhidqwnkIIE-QLGTPSDefmsrlqptvrnyvenrPKYAGYSFEELFPDVLFPPDSEEHNKLKASQARDLLS 276
                         250       260
                  ....*....|....*....|...
gi 578803747  281 QCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd07850   277 KMLVIDPEKRISVDDALQHPYIN 299
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
39-300 2.56e-17

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 83.92  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMDEEIEA--EYNILQFLPNHPNVVKFYGMFYKADHcvggqLWLVL 115
Cdd:cd14138    10 LEKIGSGEFGSVFKCVKRLDGCIYAIKrSKKPLAGSVDEQNAlrEVYAHAVLGQHSHVVRYYSAWAEDDH-----MLIQN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT---------------TEGGVK 180
Cdd:cd14138    85 EYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaseegdedEWASNK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LV----DFGVSAQLTSTRLRRntsvGTPFWMAPEVIaceqQYDSSYDARCDVWSLGITAIELGDGDP-PLF--DMHPVKT 253
Cdd:cd14138   165 VIfkigDLGHVTRVSSPQVEE----GDSRFLANEVL----QENYTHLPKADIFALALTVVCAAGAEPlPTNgdQWHEIRQ 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  254 lFKIPRNppptllhPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHP 300
Cdd:cd14138   237 -GKLPRI-------PQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
40-302 3.27e-17

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 83.92  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPV-----SDMDEEIEAEYNIlqflPNHPNVVKFYGMFYKADhcvggQLWLV 114
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRpghsrSRVFREVEMLYQC----QGHRNVLELIEFFEEED-----KFYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGLlrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDF------- 184
Cdd:cd14173    79 FEKMRGGSILSHIHRR----RHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqvSPVKICDFdlgsgik 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 --GVSAQLTSTRLRrnTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLF------------DMHP 250
Cdd:cd14173   155 lnSDCSPISTPELL--TPCGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLSGYPPFVgrcgsdcgwdrgEACP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  251 V--KTLFKIPRNPPPTLlhPEK-WCE---EFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14173   233 AcqNMLFESIQEGKYEF--PEKdWAHiscAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
33-302 5.14e-17

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 82.74  E-value: 5.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE--IEAEYNILQFLpNHPNVVKfygMFYKADhcVGGQ 110
Cdd:cd14183     5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmIQNEVSILRRV-KHPNIVL---LIEEMD--MPTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVTELVKGLLRCGQRLDEAMisyiLYGALLGLQHLHNNRIIHRDVKGNNILLTTE----GGVKLVDFGV 186
Cdd:cd14183    79 LYLVMELVKGGDLFDAITSTNKYTERDASGM----LYNLASAIKYLHSLNIVHRDIKPENLLVYEHqdgsKSLKLGDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTRLrrnTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPP----------LFDmhpvKTLFK 256
Cdd:cd14183   155 ATVVDGPLY---TVCGTPTYVAPEIIA-----ETGYGLKVDIWAAGVITYILLCGFPPfrgsgddqevLFD----QILMG 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  257 IPRNPPPtllHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14183   223 QVDFPSP---YWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
34-301 6.24e-17

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 83.36  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMdeEIEAEYNILQFLPNHPNVVKFYGMFYkaDHcVGGQLWL 113
Cdd:cd14132    18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKK--KIKREIKILQNLRGGPNIVKLLDVVK--DP-QSKTPSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVkgllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT-TEGGVKLVDFGVsAQLTS 192
Cdd:cd14132    93 IFEYVNNTDFKTLY-------PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGL-AEFYH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIACEQQYDSSYdarcDVWSLGITAIELGDGDPPLF------DM------------------ 248
Cdd:cd14132   165 PGQEYNVRVASRYYKGPELLVDYQYYDYSL----DMWSLGCMLASMIFRKEPFFhghdnyDQlvkiakvlgtddlyayld 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  249 --------HPVKTLFKIPRNPPPTLLHPE--KWC-EEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14132   241 kygielppRLNDILGRHSKKPWERFVNSEnqHLVtPEALDLLDKLLRYDHQERITAKEAMQHPY 304
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
42-248 6.29e-17

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 83.62  E-value: 6.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEE----IEAEYNILQFLPNHPNVVKFYGMFYKAdhcvgGQLWLVLEL 117
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEdidwVQTEKHVFETASNHPFLVGLHSCFQTE-----SRLFFVIEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVKGLLRcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 197
Cdd:cd05588    78 VNGG---DLMFHMQR-QRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  198 NTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDM 248
Cdd:cd05588   154 STFCGTPNYIAPEILRGED-----YGFSVDWWALGVLMFEMLAGRSP-FDI 198
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
34-305 6.36e-17

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 84.52  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDM---DE--EIEAEYNILQfLPNHPNVVKFYGMFYKADHcvg 108
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLK-SEMfkkDQlaHVKAERDVLA-ESDSPWVVSLYYSFQDAQY--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSV-TELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd05629    76 --LYLIMEFLPGGDLmTMLIKY-----DTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 A-----------------------------------QLT------------STRLRRNTSVGTPFWMAPEVIAceQQyds 220
Cdd:cd05629   149 TgfhkqhdsayyqkllqgksnknridnrnsvavdsiNLTmsskdqiatwkkNRRLMAYSTVGTPDYIAPEIFL--QQ--- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  221 SYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRNPPPTLLHPE--KWCEEFNHFISQCLIKDFER--RPSVTHL 296
Cdd:cd05629   224 GYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKI-INWRETLYFPDdiHLSVEAEDLIRRLITNAENRlgRGGAHEI 302

                  ....*....
gi 578803747  297 LDHPFIKGV 305
Cdd:cd05629   303 KSHPFFRGV 311
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
36-238 6.54e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 82.61  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSDMD-EEIEAEYNILQFLpNHPNVVKFY---------GMFYKAD 104
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELArEKVLREVRALAKL-DHPGIVRYFnawlerppeGWQEKMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCVggqLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALlGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd14048    87 EVY---LYIQMQLCRKENLKDWMNRRCTMESRELFVCLNIFKQIAS-AVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDF 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  185 GVSA------------QLTSTRLRRNTSVGTPFWMAPeviacEQQYDSSYDARCDVWSLGITAIEL 238
Cdd:cd14048   163 GLVTamdqgepeqtvlTPMPAYAKHTGQVGTRLYMSP-----EQIHGNQYSEKVDIFALGLILFEL 223
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
42-246 6.81e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 83.66  E-value: 6.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAA---VKILDPVSDMDEEIEA------------EYNILQFLpNHPNVvkfygMFYKADHC 106
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEI-KHENI-----MGLVDVYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 VGGQLWLVLELCNGGsvtelVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:PTZ00024   91 EGDFINLVMDIMASD-----LKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGL 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  187 -------------SAQLTSTRLRRNTS-VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLF 246
Cdd:PTZ00024  166 arrygyppysdtlSKDETMQRREEMTSkVVTLWYRAPELLMGAEKYHFA----VDMWSVGCIFAELLTGK-PLF 234
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
34-319 6.89e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 82.74  E-value: 6.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPvSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKAdhcvgG 109
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKD-SEENEEVKEttlrELKMLRTL-KQENIVELKEAFRRR-----G 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGgSVTELVKGLLRCGqrLDEAMISYIlYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd07848    74 KLYLVFEYVEK-NMLELLEEMPNGV--PPEKVRSYI-YQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTS-TRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR--NPPPTll 266
Cdd:cd07848   150 LSEgSNANYTEYVATRWYRSPELL-----LGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKvlGPLPA-- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  267 hpekwcEEFNHFISQCLIKDFeRRPSVTH--LLDHPFIKGVHGKVLFLQKQLAKV 319
Cdd:cd07848   223 ------EQMKLFYSNPRFHGL-RFPAVNHpqSLERRYLGILSGVLLDLMKNLLKL 270
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
74-301 7.29e-17

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 81.97  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   74 DEEIEaeynILQFLpNHPNVVKFYGMFYKAdhcVGGQLWLVL--ELCNGGSVtelvKGLLRCGQRLDEAMISYILYGALL 151
Cdd:cd14033    48 SEEVE----MLKGL-QHPNIVRFYDSWKST---VRGHKCIILvtELMTSGTL----KTYLKRFREMKLKLLQRWSRQILK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  152 GLQHLHNNR--IIHRDVKGNNILLT-TEGGVKLVDFGVsAQLTSTRLRRNTsVGTPFWMAPEViaceqqYDSSYDARCDV 228
Cdd:cd14033   116 GLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGL-ATLKRASFAKSV-IGTPEFMAPEM------YEEKYDEAVDV 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  229 WSLGITAIELGDGDPPLFDMHPVKTLF-KIPRNPPPTLLHPEKwCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14033   188 YAFGMCILEMATSEYPYSECQNAAQIYrKVTSGIKPDSFYKVK-VPELKEIIEGCIRTDKDERFTIQDLLEHRF 260
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
30-298 7.93e-17

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 82.85  E-value: 7.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   30 PDPTdtWEI-------IETIGKGTYGKVYKVT-----NKRDGSLA-AVKILD------PVSDMDEEIEaeynILQFLPNH 90
Cdd:cd05053     3 LDPE--WELprdrltlGKPLGEGAFGQVVKAEavgldNKPNEVVTvAVKMLKddatekDLSDLVSEME----MMKMIGKH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   91 PNVVKFYGMfykadhCVG-GQLWLVLELCNGGSVTELVK------------GLLRCGQRLDEAMISYILYGALLGLQHLH 157
Cdd:cd05053    77 KNIINLLGA------CTQdGPLYVVVEYASKGNLREFLRarrppgeeaspdDPRVPEEQLTQKDLVSFAYQVARGMEYLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  158 NNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVG-TPF-WMAPEVIaceqqYDSSYDARCDVWSLGITA 235
Cdd:cd05053   151 SKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGrLPVkWMAPEAL-----FDRVYTHQSDVWSFGVLL 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  236 IE---LGdGDPplFDMHPVKTLFKIPR-----NPPPTLLHpekwceEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd05053   226 WEiftLG-GSP--YPGIPVEELFKLLKeghrmEKPQNCTQ------ELYMLMRDCWHEVPSQRPTFKQLVE 287
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
39-296 9.06e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 82.37  E-value: 9.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKV----YKVTNKRDGSLAAVKIL-----DPVSDMDEEIEaeynILQFLpNHPNVVKFYGMFYKADHcvgG 109
Cdd:cd14205     9 LQQLGKGNFGSVemcrYDPLQDNTGEVVAVKKLqhsteEHLRDFEREIE----ILKSL-QHDNIVKYKGVCYSAGR---R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELvkgLLRCGQRLDEamISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 187
Cdd:cd14205    81 NLRLIMEYLPYGSLRDY---LQKHKERIDH--IKLLQYTSQIckGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  188 AQLTSTrlRRNTSVGTP-----FWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL-----GDGDPPLFDM--------- 248
Cdd:cd14205   156 KVLPQD--KEYYKVKEPgespiFWYAPESLT-----ESKFSVASDVWSFGVVLYELftyieKSKSPPAEFMrmigndkqg 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578803747  249 -----HPVKTLFKIPRNPpptllHPEKWCEEFNHFISQCLIKDFERRPSVTHL 296
Cdd:cd14205   229 qmivfHLIELLKNNGRLP-----RPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
36-187 9.80e-17

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 81.73  E-value: 9.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKIlDPVSDMDEEIEAEYNILQFLPNHPNV--VKFYGMfykadhcVGGQLWL 113
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKI-EKKDSKHPQLEYEAKVYKLLQGGPGIprLYWFGQ-------EGDYNVM 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  114 VLELCnGGSVTELVKgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK---LVDFGVS 187
Cdd:cd14016    74 VMDLL-GPSLEDLFN---KCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLA 146
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
33-302 9.85e-17

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 82.12  E-value: 9.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEII--ETIGKGTYGKVYKVTNKRDGSLAAVKILdpvsdMDE-EIEAEYNILQFLPNHPNVVKFYGMF-----YKAD 104
Cdd:cd14171     3 LEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKIL-----LDRpKARTEVRLHMMCSGHPNIVQIYDVYansvqFPGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCVGGQLWLVLELCNGGsvtELVKgllRCGQR--LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL---TTEGGV 179
Cdd:cd14171    78 SSPRARLLIVMELMEGG---ELFD---RISQHrhFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  180 KLVDFGVsAQLTSTRLRrnTSVGTPFWMAPEVIACEQQYDSS------------YDARCDVWSLGITAIELGDGDPPLFD 247
Cdd:cd14171   152 KLCDFGF-AKVDQGDLM--TPQFTPYYVAPQVLEAQRRHRKErsgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYS 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  248 MHPVKTlfkIPRNPPPTLLH-----PEK-W---CEEFNHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14171   229 EHPSRT---ITKDMKRKIMTgsyefPEEeWsqiSEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
31-297 1.13e-16

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 81.65  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTwEIIETIGKGTYGKVYK---VTNKRDGSLAAVKILDPVSDMDEEIE--AEYNIL-QFlpNHPNVVKFYGMFYKAD 104
Cdd:cd05033     2 DASYV-TIEKVIGGGEFGEVCSgslKLPGKKEIDVAIKTLKSGYSDKQRLDflTEASIMgQF--DHPNVIRLEGVVTKSR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 hcvggQLWLVLELCNGGSvteLVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd05033    79 -----PVMIVTEYMENGS---LDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 GVSAQLTSTRLRRNTSVG-TPF-WMAPEVIAcEQQYDSSydarCDVWSLGITAIE-LGDGDPPLFDM------HPVKTLF 255
Cdd:cd05033   151 GLSRRLEDSEATYTTKGGkIPIrWTAPEAIA-YRKFTSA----SDVWSFGIVMWEvMSYGERPYWDMsnqdviKAVEDGY 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578803747  256 KIPrnPP---PTLLHpekwceefnHFISQCLIKDFERRPSVTHLL 297
Cdd:cd05033   226 RLP--PPmdcPSALY---------QLMLDCWQKDRNERPTFSQIV 259
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
32-238 1.21e-16

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 81.62  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYK------VTNKRDGSLAaVKILDPVSDMDEEIE--AEYNIL-QFlpNHPNVVKFYGMFYK 102
Cdd:cd05032     4 PREKITLIRELGQGSFGMVYEglakgvVKGEPETRVA-IKTVNENASMRERIEflNEASVMkEF--NCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 ADHCVggqlwLVLEL-------------------CNGGSVTELVKGLLRCGQRLDeamisyilygallGLQHLHNNRIIH 163
Cdd:cd05032    81 GQPTL-----VVMELmakgdlksylrsrrpeaenNPGLGPPTLQKFIQMAAEIAD-------------GMAYLAAKKFVH 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  164 RDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIAceqqyDSSYDARCDVWSLGITAIEL 238
Cdd:cd05032   143 RDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLlPVrWMAPESLK-----DGVFTTKSDVWSFGVVLWEM 214
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
59-238 1.32e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 84.30  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   59 GSLAAVKILDPVSDMDEEIEAEY--NILQFLP--NHPNVVKFYGMFYKADhcvggQLWLVLELCNGGSVTELVKGLLRCG 134
Cdd:PTZ00267   89 GSDPKEKVVAKFVMLNDERQAAYarSELHCLAacDHFGIVKHFDDFKSDD-----KLLLIMEYGSGGDLNKQIKQRLKEH 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  135 QRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT-STRLRRNTS-VGTPFWMAPEVi 212
Cdd:PTZ00267  164 LPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSdSVSLDVASSfCGTPYYLAPEL- 242
                         170       180
                  ....*....|....*....|....*.
gi 578803747  213 aCEQQydsSYDARCDVWSLGITAIEL 238
Cdd:PTZ00267  243 -WERK---RYSKKADMWSLGVILYEL 264
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
36-306 1.68e-16

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 82.79  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIE------TIGKGTYGKVYKVTNKRDGSLAAVKILD-PVSDMdeeIEAE--YNILQFLPN--HPNVVKFYGMFYKAD 104
Cdd:cd07878    11 WEVPEryqnltPVGSGAYGSVCSAYDTRLRQKVAVKKLSrPFQSL---IHARrtYRELRLLKHmkHENVIGLLDVFTPAT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCVG-GQLWLVLELCnGGSVTELVKgllrCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd07878    88 SIENfNEVYLVTNLM-GADLNNIVK----C-QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVSAQltsTRLRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLFD----MHPVKTLFKIPR 259
Cdd:cd07878   162 FGLARQ---ADDEMTGYVATRWYRAPEIMLNWMHYNQT----VDIWSVGCIMAELLKGK-ALFPgndyIDQLKRIMEVVG 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  260 NPPPTLL------HPEKWCEEFNH-------------------FISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07878   234 TPSPEVLkkisseHARKYIQSLPHmpqqdlkkifrganplaidLLEKMLVLDSDKRISASEALAHPYFSQYH 305
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
40-238 1.82e-16

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 81.33  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKvtNKRDGSLAAVKILDpvSDMDEEIEAEYNILQfLPN--HPNVVKFYGmfykADHCVGG---QLWLV 114
Cdd:cd13998     1 EVIGKGRFGEVWK--ASLKNEPVAVKIFS--SRDKQSWFREKEIYR-TPMlkHENILQFIA----ADERDTAlrtELWLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGLLRCGQ---RLDEAMISyilygallGLQHLHNN---------RIIHRDVKGNNILLTTEGGVKLV 182
Cdd:cd13998    72 TAFHPNGSL*DYLSLHTIDWVslcRLALSVAR--------GLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIA 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  183 DFGVSAQLTSTR----LRRNTSVGTPFWMAPEVI--ACEQQYDSSYdARCDVWSLGITAIEL 238
Cdd:cd13998   144 DFGLAVRLSPSTgeedNANNGQVGTKRYMAPEVLegAINLRDFESF-KRVDIYAMGLVLWEM 204
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
42-244 1.95e-16

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 81.00  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrDGSLAAVKIL--DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGmfYKADHCVGgqlWLVLELCN 119
Cdd:cd14664     1 IGRGGAGTVYKGVMP-NGTLVAVKRLkgEGTQGGDHGFQAEIQTLGMI-RHRNIVRLRG--YCSNPTTN---LLVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNN---RIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd14664    74 NGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSH 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  197 RNTSV-GTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPP 244
Cdd:cd14664   154 VMSSVaGSYGYIAPEYA-----YTGKVSEKSDVYSYGVVLLELITGKRP 197
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
42-301 2.06e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 81.21  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--------EYNILQFLpNHPNVVKFYGMFyKADH---CVggq 110
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQnyikhalrEYEIHKSL-DHPRIVKLYDVF-EIDTdsfCT--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 lwlVLELCNGgsvTELVKGLLRCGqRLDEAMISYILYGALLGLQHLHN--NRIIHRDVKGNNILL---TTEGGVKLVDFG 185
Cdd:cd13990    83 ---VLEYCDG---NDLDFYLKQHK-SIPEREARSIIMQVVSALKYLNEikPPIIHYDLKPGNILLhsgNVSGEIKITDFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTSTRLRRN----TS--VGTPFWMAPEVIACEQQyDSSYDARCDVWSLGITAIELGDGDPPL-FDMHPVKTLFKIp 258
Cdd:cd13990   156 LSKIMDDESYNSDgmelTSqgAGTYWYLPPECFVVGKT-PPKISSKVDVWSVGVIFYQMLYGRKPFgHNQSQEAILEEN- 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  259 rnpppTLLHPEK--------WCEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd13990   234 -----TILKATEvefpskpvVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
35-238 2.28e-16

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 80.76  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKiLDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHCvggqlWLV 114
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMK-VESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYN-----YIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCnGGSVTELVKGLLR------CGQRLDEAMisyilygaLLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDF 184
Cdd:cd14017    75 MTLL-GPNLAELRRSQPRgkfsvsTTLRLGIQI--------LKAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDF 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  185 GVSAQLTST-----RLRRNTS--VGTPFWMApevIACEQQYDSSYdaRCDVWSLGITAIEL 238
Cdd:cd14017   146 GLARQYTNKdgeveRPPRNAAgfRGTVRYAS---VNAHRNKEQGR--RDDLWSWFYMLIEF 201
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
37-298 3.64e-16

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 80.09  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDgslAAVKILDPVSDMDEEIEAEYNILQFLPN--HPNVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGRWHGD---VAIKLLNIDYLNEEQLEAFKEEVAAYKNtrHDNLVLFMGACMDPPH-----LAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKgllrcgQRLDEAMISYILYGAL---LGLQHLHNNRIIHRDVKGNNILLttEGG-VKLVDFGVS--A 188
Cdd:cd14063    75 TSLCKGRTLYSLIH------ERKEKFDFNKTVQIAQqicQGMGYLHAKGIIHKDLKSKNIFL--ENGrVVITDFGLFslS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFW---MAPEVIA-----CEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR- 259
Cdd:cd14063   147 GLLQPGRREDTLVIPNGWlcyLAPEIIRalspdLDFEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCg 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578803747  260 -NPPPTLLHPEKwceEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd14063   227 kKQSLSQLDIGR---EVKDILMQCWAYDPEKRPTFSDLLR 263
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
42-310 3.74e-16

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 80.48  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFyGMFYKADHCvggqLWLVLEL 117
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmalnEKQILEKV-NSRFVVSL-AYAYETKDA----LCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGSVTELVKGLLRCGQRLDEAmisyILYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 195
Cdd:cd05605    82 MNGGDLKFHIYNMGNPGFEEERA----VFYAAeiTCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGET 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  196 RRNtSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPlFDMHP--VKTLFKIPRNPPPTLLHPEKWCE 273
Cdd:cd05605   158 IRG-RVGTVGYMAPEVVKNER-----YTFSPDWWGLGCLIYEMIEGQAP-FRARKekVKREEVDRRVKEDQEEYSEKFSE 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578803747  274 EFNHFISQCLIKDFE-----RRPSVTHLLDHPFIKGVHGKVL 310
Cdd:cd05605   231 EAKSICSQLLQKDPKtrlgcRGEGAEDVKSHPFFKSINFKRL 272
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
35-310 4.12e-16

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 80.45  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvggQ 110
Cdd:cd05630     1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmalnEKQILEKV-NSRFVVSLAYAYETKD-----A 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVTELVKGLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 190
Cdd:cd05630    75 LCLVLTLMNGGDLKFHIYHMGQAG--FPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNtSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPvktlfKIPRNPPPTLLH--P 268
Cdd:cd05630   153 PEGQTIKG-RVGTVGYMAPEVVKNER-----YTFSPDWWALGCLLYEMIAGQSPFQQRKK-----KIKREEVERLVKevP 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578803747  269 EKWCEEFN----HFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVL 310
Cdd:cd05630   222 EEYSEKFSpqarSLCSMLLCKDPAERlgcrgGGAREVKEHPLFKKLNFKRL 272
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
36-306 4.13e-16

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 81.54  E-value: 4.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEI------IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPN--HPNVVKFYGMFyKADHCV 107
Cdd:cd07880    11 WEVpdryrdLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHmkHENVIGLLDVF-TPDLSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 G--GQLWLVLELCnGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd07880    90 DrfHDFYLVMPFM-GTDLGKLMKH-----EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  186 VSAQLTStrlRRNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLFDMH----PVKTLFKIPRNP 261
Cdd:cd07880   164 LARQTDS---EMTGYVVTRWYRAPEVILNWMHYTQT----VDIWSVGCIMAEMLTGK-PLFKGHdhldQLMEIMKVTGTP 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  262 PPTLLH--------------PEKWCEEFN-----------HFISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07880   236 SKEFVQklqsedaknyvkklPRFRKKDFRsllpnanplavNVLEKMLVLDAESRITAAEALAHPYFEEFH 305
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
42-244 4.63e-16

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 81.00  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD--EEIEAEYNILQFLpNHPNVVKfygMFYKADHCVGGQLWLVLELCN 119
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRplDVQMREFEVLKKL-NHKNIVK---LFAIEEELTTRHKVLVMELCP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  120 GGSVTELvkgllrcgqrLDEAMISY---------ILYGALLGLQHLHNNRIIHRDVKGNNIL-LTTEGG---VKLVDFGV 186
Cdd:cd13988    77 CGSLYTV----------LEEPSNAYglpesefliVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGqsvYKLTDFGA 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  187 SAQLTSTRlRRNTSVGTPFWMAP---EVIACEQQYDSSYDARCDVWSLGITAIELGDGDPP 244
Cdd:cd13988   147 ARELEDDE-QFVSLYGTEEYLHPdmyERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLP 206
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
34-252 5.35e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 80.05  E-value: 5.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFYkADHCvggqL 111
Cdd:cd07871     5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAirEVSLLKNL-KHANIVTLHDIIH-TERC----L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS-AQL 190
Cdd:cd07871    79 TLVFEYLD----SDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLArAKS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  191 TSTRLRRNTSVgTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLFDMHPVK 252
Cdd:cd07871   155 VPTKTYSNEVV-TLWYRPPDVLLGSTEYSTP----IDMWGVGCILYEMATGR-PMFPGSTVK 210
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
38-250 5.80e-16

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 80.18  E-value: 5.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKvtNKRDGSLAAVKILdpvSDMDEEI---EAE-YNILqfLPNHPNVVKFYG--MFYKADhCVggQL 111
Cdd:cd14142     9 LVECIGKGRYGEVWR--GQWQGESVAVKIF---SSRDEKSwfrETEiYNTV--LLRHENILGFIAsdMTSRNS-CT--QL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNN--------RIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd14142    79 WLITHYHENGSLYDYLQR-----TTLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVS---AQLTST-RLRRNTSVGTPFWMAPEVIAcEQQYDSSYDA--RCDVWSLGITAIELG----------DGDPPLFD 247
Cdd:cd14142   154 LGLAvthSQETNQlDVGNNPRVGTKRYMAPEVLD-ETINTDCFESykRVDIYAFGLVLWEVArrcvsggiveEYKPPFYD 232

                  ...
gi 578803747  248 MHP 250
Cdd:cd14142   233 VVP 235
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
42-250 6.05e-16

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 79.11  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKrdGSLAAVK-----ILDPVSDMDEEIEaEYNILQFLpNHPNVVKFYGMfykadhCVG--GQLWLV 114
Cdd:cd14064     1 IGSGSFGKVYKGRCR--NKIVAIKryranTYCSKSDVDMFCR-EVSILCRL-NHPCVIQFVGA------CLDdpSQFAIV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKGLLRCgqrLDEAMISYILYGALLGLQHLHN--NRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd14064    71 TQYVSGGSLFSLLHEQKRV---IDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQS 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSV-GTPFWMAPEVIA-CEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHP 250
Cdd:cd14064   148 LDEDNMTKQpGNLRWMAPEVFTqCTR-----YSIKADVFSYALCLWELLTGEIPFAHLKP 202
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
39-306 6.55e-16

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 79.94  E-value: 6.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKV----YKVTNKRDGSLAAVKIL--DPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvGGQ-L 111
Cdd:cd05080     9 IRDLGEGHFGKVslycYDPTNDGTGEMVAVKALkaDCGPQHRSGWKQEIDILKTL-YHENIVKYKGCCSEQ----GGKsL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGSvteLVKGLLRCGQRLDEAMIsyILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05080    84 QLIMEYVPLGS---LRDYLPKHSIGLAQLLL--FAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 ST----RLRRNTSvgTP-FWMAPEviaCEQQYDSSYDArcDVWSLGITAIEL-----GDGDPP--LFDMHPVKTlFKIPR 259
Cdd:cd05080   159 EGheyyRVREDGD--SPvFWYAPE---CLKEYKFYYAS--DVWSFGVTLYELlthcdSSQSPPtkFLEMIGIAQ-GQMTV 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578803747  260 NPPPTLLH-------PEKWCEEFNHFISQCLIKDFERRPSVTHLLdhPFIKGVH 306
Cdd:cd05080   231 VRLIELLErgerlpcPDKCPQEVYHLMKNCWETEASFRPTFENLI--PILKTVH 282
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
32-299 6.75e-16

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 79.84  E-value: 6.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVT----NKRDG-SLAAVKILDPVSDMDEE--IEAEYNILQFLPNHPNVVKFYGMFYKAd 104
Cdd:cd05054     5 PRDRLKLGKPLGRGAFGKVIQASafgiDKSATcRTVAVKMLKEGATASEHkaLMTELKILIHIGHHLNVVNLLGACTKP- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 hcvGGQLWLVLELCNGGSVTELVKGLLRC--------------GQRLDEAMISYILYGALL--------GLQHLHNNRII 162
Cdd:cd05054    84 ---GGPLMVIVEFCKFGNLSNYLRSKREEfvpyrdkgardveeEEDDDELYKEPLTLEDLIcysfqvarGMEFLASRKCI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  163 HRDVKGNNILLTTEGGVKLVDFGVSAQLTST-RLRRNTSVGTPF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIElgd 240
Cdd:cd05054   161 HRDLAARNILLSENNVVKICDFGLARDIYKDpDYVRKGDARLPLkWMAPESI-----FDKVYTTQSDVWSFGVLLWE--- 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  241 gdpplfdmhpvktLFKIPRNPPPTLLHPEKWCE----------------EFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd05054   233 -------------IFSLGASPYPGVQMDEEFCRrlkegtrmrapeyttpEIYQIMLDCWHGEPKERPTFSELVEK 294
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
40-238 7.92e-16

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 79.68  E-value: 7.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVtnKRDGSLAAVKILdPVSDMDEeIEAEYNILQfLPN--HPNVVKFYGmfykADHCVGG---QLWLV 114
Cdd:cd14053     1 EIKARGRFGAVWKA--QYLNRLVAVKIF-PLQEKQS-WLTEREIYS-LPGmkHENILQFIG----AEKHGESleaEYWLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVKG-LLRCGQ--RLDEAMISyilygallGLQHLHNNR----------IIHRDVKGNNILLTTEGGVKL 181
Cdd:cd14053    72 TEFHERGSLCDYLKGnVISWNElcKIAESMAR--------GLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACI 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  182 VDFGVSAQLTSTRLRRNT--SVGTPFWMAPEVIacEQQYDSSYDA--RCDVWSLGITAIEL 238
Cdd:cd14053   144 ADFGLALKFEPGKSCGDThgQVGTRRYMAPEVL--EGAINFTRDAflRIDMYAMGLVLWEL 202
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
38-306 8.43e-16

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 80.49  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   38 IIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVsdMDEEIEA-----EYNILQFLpNHPNVVKFYGMFYKADHCVGGQLW 112
Cdd:cd07858     9 PIKPIGRGAYGIVCSAKNSETNEKVAIKKIANA--FDNRIDAkrtlrEIKLLRHL-DHENVIAIKDIMPPPHREAFNDVY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNggsvTELVKgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLTS 192
Cdd:cd07858    86 IVYELMD----TDLHQ-IIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL-ARTTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTS-VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGdGDPPLFD----MHPVKTLFKI---PRNPPPT 264
Cdd:cd07858   160 EKGDFMTEyVVTRWYRAPELLLNCSEYTTA----IDVWSVGCIFAELL-GRKPLFPgkdyVHQLKLITELlgsPSEEDLG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  265 LLHPEK---------------WCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFIKGVH 306
Cdd:cd07858   235 FIRNEKarryirslpytprqsFARLFPHanplaidLLEKMLVFDPSKRITVEEALAHPYLASLH 298
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
42-292 8.77e-16

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 78.85  E-value: 8.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYK--VTNKRDGSLAAVKILDPVSD---MDEEIEAEYNILQFLPNhPNVVKFYGMfykadhCVGGQLWLVLE 116
Cdd:cd05116     3 LGSGNFGTVKKgyYQMKKVVKTVAVKILKNEANdpaLKDELLREANVMQQLDN-PYIVRMIGI------CEAESWMLVME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR-- 194
Cdd:cd05116    76 MAELGPLNKF----LQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADEny 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTSVGTPF-WMAPEviaCEQQYdsSYDARCDVWSLGITAIE-LGDGDPPLFDMHPVKTLFKIPRNppPTLLHPEKWC 272
Cdd:cd05116   152 YKAQTHGKWPVkWYAPE---CMNYY--KFSSKSDVWSFGVLMWEaFSYGQKPYKGMKGNEVTQMIEKG--ERMECPAGCP 224
                         250       260
                  ....*....|....*....|
gi 578803747  273 EEFNHFISQCLIKDFERRPS 292
Cdd:cd05116   225 PEMYDLMKLCWTYDVDERPG 244
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
42-185 9.01e-16

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 75.56  E-value: 9.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-EEIEAEYNILQFLPNH-PNVVKFYGmFYKadhcVGGQLWLVLELCN 119
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEgEDLESEMDILRRLKGLeLNIPKVLV-TED----VDGPNILLMELVK 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  120 GGSVTELVKGLLrcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd13968    76 GGTLIAYTQEEE-----LDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
35-301 9.04e-16

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 80.02  E-value: 9.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNK--RDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFY-KADHCV 107
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKFKGDKEQYTGISQsacrEIALLREL-KHENVVSLVEVFLeHADKSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  108 ggqlWLVLE--------LCNGGSVTELVkgllrcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG- 178
Cdd:cd07842    80 ----YLLFDyaehdlwqIIKFHRQAKRV--------SIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPe 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  179 ---VKLVDFGVsAQLTSTRLRR----NTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLF----D 247
Cdd:cd07842   148 rgvVKIGDLGL-ARLFNAPLKPladlDPVVVTIWYRAPELLLGARHYTKA----IDIWAIGCIFAELLTLEPIFKgreaK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  248 MHP--------VKTLFKIPRNPP----PTLLH-PE-------------------KWCEEFN-------HFISQCLIKDFE 288
Cdd:cd07842   223 IKKsnpfqrdqLERIFEVLGTPTekdwPDIKKmPEydtlksdtkastypnsllaKWMHKHKkpdsqgfDLLRKLLEYDPT 302
                         330
                  ....*....|...
gi 578803747  289 RRPSVTHLLDHPF 301
Cdd:cd07842   303 KRITAEEALEHPY 315
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
36-266 9.14e-16

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 80.47  E-value: 9.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEI------IETIGKGTYGKVYKVTNKRDGSLAAVKILD-PVSDMdeeIEAE--YNILQFLPN--HPNVVKFYGMFYKAD 104
Cdd:cd07877    13 WEVperyqnLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSrPFQSI---IHAKrtYRELRLLKHmkHENVIGLLDVFTPAR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 HCVG-GQLWLVLELCnGGSVTELVKgllrCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 183
Cdd:cd07877    90 SLEEfNDVYLVTHLM-GADLNNIVK----C-QKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  184 FGVsAQLTSTRLrrNTSVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGD---PPLFDMHPVKTLFKIPRN 260
Cdd:cd07877   164 FGL-ARHTDDEM--TGYVATRWYRAPEIMLNWMHYNQT----VDIWSVGCIMAELLTGRtlfPGTDHIDQLKLILRLVGT 236

                  ....*.
gi 578803747  261 PPPTLL 266
Cdd:cd07877   237 PGAELL 242
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
39-238 1.69e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 78.40  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKV----YKVTNKRDGSLAAVKILDPVS-DMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvgGQLWL 113
Cdd:cd05081     9 ISQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGpDQQRDFQREIQILKAL-HSDFIVKYRGVSYGPGR---RSLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELvkgLLRCGQRLDEAMIsyILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd05081    85 VMEYLPSGCLRDF---LQRHRARLDASRL--LLYSSQIckGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STR---LRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIEL 238
Cdd:cd05081   160 LDKdyyVVREPGQSPIFWYAPESLS-----DNIFSRQSDVWSFGVVLYEL 204
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
33-301 1.98e-15

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 77.63  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlw 112
Cdd:cd14108     1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVVI----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKGLLRCgqrldEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 190
Cdd:cd14108    75 IVTELCHEELLERITKRPTVC-----ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQEL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRlRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIpRNPPPTLLHP-- 268
Cdd:cd14108   150 TPNE-PQYCKYGTPEFVAPEIVN-----QSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI-RNYNVAFEESmf 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  269 EKWCEEFNHFISQCLIKDfERRPSVTHLLDHPF 301
Cdd:cd14108   223 KDLCREAKGFIIKVLVSD-RLRPDAEETLEHPW 254
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
32-298 2.19e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 79.29  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTD-TWEIIET-------IGKGTYGKVYKV---------TNKrdGSLAAVKIL-DPVSDMD-EEIEAEYNILQFLPNHPN 92
Cdd:cd05100     2 PADpKWELSRTrltlgkpLGEGCFGQVVMAeaigidkdkPNK--PVTVAVKMLkDDATDKDlSDLVSEMEMMKMIGKHKN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   93 VVKFYGMFYKadhcvGGQLWLVLELCNGGSVTELVKGLLRCGQ-------RLDEAMISY-----ILYGALLGLQHLHNNR 160
Cdd:cd05100    80 IINLLGACTQ-----DGPLYVLVEYASKGNLREYLRARRPPGMdysfdtcKLPEEQLTFkdlvsCAYQVARGMEYLASQK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  161 IIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIEL 238
Cdd:cd05100   155 CIHRDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGVLLWEI 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  239 GDGDPPLFDMHPVKTLFKIPRNpPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd05100   230 FTLGGSPYPGIPVEELFKLLKE-GHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVE 288
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
36-323 2.27e-15

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 79.30  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDP----VSDMDEEIEAEYNILQFlPNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKevivAKDEVAHTLTENRVLQN-SRHPFLTALKYSFQTHD-----RL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNGGsvtELVKGLLRcGQRLDEAMISYilYGALL--GLQHLHNNR-IIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05594   101 CFVMEYANGG---ELFFHLSR-ERVFSEDRARF--YGAEIvsALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLF--DMHPVKTLFKIPRNPPPTLL 266
Cdd:cd05594   175 EGIKDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEEIRFPRTL 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  267 HPEKwceefNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVLFlQKQLAKVLQDQ 323
Cdd:cd05594   250 SPEA-----KSLLSGLLKKDPKQRlgggpDDAKEIMQHKFFAGIVWQDVY-EKKLVPPFKPQ 305
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
34-366 2.34e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 78.90  E-value: 2.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHP-----NVVKFYGMFYKADHcvg 108
Cdd:cd14226    13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDtenkyYIVRLKRHFMFRNH--- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLEL-----------CNGGSVTelvkglLRCGQRLDEAMISyilygALLGLQHlHNNRIIHRDVKGNNILLTT-- 175
Cdd:cd14226    90 --LCLVFELlsynlydllrnTNFRGVS------LNLTRKFAQQLCT-----ALLFLST-PELSIIHCDLKPENILLCNpk 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  176 EGGVKLVDFGVSAQLtSTRLRRntSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDpPLFD-MHPVKTL 254
Cdd:cd14226   156 RSAIKIIDFGSSCQL-GQRIYQ--YIQSRFYRSPEVL-----LGLPYDLAIDMWSLGCILVEMHTGE-PLFSgANEVDQM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  255 FKIPR--NPPPtllhpekwceefNHFISQC--LIKDFERRPSVTHLLDhpFIKGVHGKVLFLQKQLAKVLQDQKHqNPVA 330
Cdd:cd14226   227 NKIVEvlGMPP------------VHMLDQApkARKFFEKLPDGTYYLK--KTKDGKKYKPPGSRKLHEILGVETG-GPGG 291
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 578803747  331 KTRHERMHTrrpyhVEDAEKYCledDLVnLEVLDED 366
Cdd:cd14226   292 RRAGEPGHT-----VEDYLKFK---DLI-LRMLDYD 318
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
36-256 2.36e-15

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 79.18  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIET------IGKGTYGKVYKVTNKRDGSLAAVKILDpvSDMDEEIEAE--YNILQFLP--NHPNVVKFYGMFYKADH 105
Cdd:cd07879    11 WELPERytslkqVGSGAYGSVCSAIDKRTGEKVAIKKLS--RPFQSEIFAKraYRELTLLKhmQHENVIGLLDVFTSAVS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  106 CVGGQ-LWLVLELCNggsvTELVKGLlrcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDF 184
Cdd:cd07879    89 GDEFQdFYLVMPYMQ----TDLQKIM---GHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDF 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  185 GVS----AQLTSTrlrrntsVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGdpplfdmhpvKTLFK 256
Cdd:cd07879   162 GLArhadAEMTGY-------VVTRWYRAPEVILNWMHYNQT----VDIWSVGCIMAEMLTG----------KTLFK 216
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
33-245 2.74e-15

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 77.27  E-value: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVggqlw 112
Cdd:cd14110     2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRL-SHPRIAQLHSAYLSPRHLV----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGgsvTELVKGL-LRcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd14110    76 LIEELCSG---PELLYNLaER--NSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  192 STR-LRRNTSVGTPFWMAPEVIacEQQydsSYDARCDVWSLGITAIELGDGDPPL 245
Cdd:cd14110   151 QGKvLMTDKKGDYVETMAPELL--EGQ---GAGPQTDIWAIGVTAFIMLSADYPV 200
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
42-301 3.96e-15

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 77.04  E-value: 3.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDG-SLAAVKILD-PVSDMDEE-IEAEYNILQFLpNHPNVVKFYGMF---YKADHCVggqlWLVL 115
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWvEVAWCELQDrKLTKVERQrFKEEAEMLKGL-QHPNIVRFYDFWescAKGKRCI----VLVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLglQHLHNNRIIHRDVKGNNILLT-TEGGVKLVDFGVsAQLTSTR 194
Cdd:cd14032    84 ELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLF--LHTRTPPIIHRDLKCDNIFITgPTGSVKIGDLGL-ATLKRAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  195 LRRNTsVGTPFWMAPEViaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLF-KIPRNPPPTLLhpEKWCE 273
Cdd:cd14032   161 FAKSV-IGTPEFMAPEM------YEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYrKVTCGIKPASF--EKVTD 231
                         250       260
                  ....*....|....*....|....*....
gi 578803747  274 -EFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14032   232 pEIKEIIGECICKNKEERYEIKDLLSHAF 260
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
42-301 4.16e-15

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 77.07  E-value: 4.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDG-SLAAVKILDPVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMF---YKADHCVggqlWLVL 115
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWvEVAWCELQDRKLTKAEQqrFKEEAEMLKGL-QHPNIVRFYDSWesvLKGKKCI----VLVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRCGQRLDEAMISYILYGallgLQHLHNNR--IIHRDVKGNNILLT-TEGGVKLVDFGVsAQLTS 192
Cdd:cd14031    93 ELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKG----LQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGL-ATLMR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTsVGTPFWMAPEViaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLF-KIPRNPPPTLLHpEKW 271
Cdd:cd14031   168 TSFAKSV-IGTPEFMAPEM------YEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYrKVTSGIKPASFN-KVT 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  272 CEEFNHFISQCLIKDFERRPSVTHLLDHPF 301
Cdd:cd14031   240 DPEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
34-246 4.26e-15

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 78.12  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFYKADHCVGGQL 111
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTlrEIKILLRF-KHENIIGILDIQRPPTFESFKDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKgLLRCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGvsaqlt 191
Cdd:cd07849    84 YIVQELME----TDLYK-LIKT-QHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFG------ 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  192 strLRRNTS------------VGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDpPLF 246
Cdd:cd07849   152 ---LARIADpehdhtgflteyVATRWYRAPEIMLNSKGYTKA----IDIWSVGCILAEMLSNR-PLF 210
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
40-300 4.71e-15

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 76.57  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEaeynilQFLP---------NHPNVVKFYGMFyKADHCVggq 110
Cdd:cd14162     6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQ------KFLPreievikglKHPNLICFYEAI-ETTSRV--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 lWLVLELCNGGSVTELVkgllRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSaql 190
Cdd:cd14162    76 -YIIMELAENGDLLDYI----RKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFA--- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 tstrlRRNTSVGTPFWMAPEVIACEQQYDS-------SYDAR-CDVWSLGITAIELGDGDPPlFDMHPVKTLFKIPRNPP 262
Cdd:cd14162   148 -----RGVMKTKDGKPKLSETYCGSYAYASpeilrgiPYDPFlSDIWSMGVVLYTMVYGRLP-FDDSNLKVLLKQVQRRV 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  263 PTLLHPeKWCEEFNHFISQCLIKdFERRPSVTHLLDHP 300
Cdd:cd14162   222 VFPKNP-TVSEECKDLILRMLSP-VKKRITIEEIKRDP 257
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
36-241 5.46e-15

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 78.15  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLP--NHPNVVKFYGMFYKADHCVGGQ-LW 112
Cdd:cd07876    23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKcvNHKNIISLLNVFTPQKSLEEFQdVY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGgSVTELVKgllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLTS 192
Cdd:cd07876   103 LVMELMDA-NLCQVIH------MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAC 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDG 241
Cdd:cd07876   175 TNFMMTPYVVTRYYRAPEVI-----LGMGYKENVDIWSVGCIMGELVKG 218
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
39-243 5.55e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 76.92  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFYKADhcvggQLWLVLE 116
Cdd:cd07870     5 LEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAirEASLLKGL-KHANIVLLHDIIHTKE-----TLTFVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLR 196
Cdd:cd07870    79 YMH----TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  197 RNTSVGTPFWMAPEVIACEQQYDSSYdarcDVWSLGITAIELGDGDP 243
Cdd:cd07870   155 YSSEVVTLWYRPPDVLLGATDYSSAL----DIWGAGCIFIEMLQGQP 197
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
40-302 5.73e-15

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 76.40  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGS--LAAVKILDPVsdMDEEIEAeYNILqflpNHPNVVKFYGMfYKADhcvGGQLWLVLEL 117
Cdd:cd14109    10 EDEKRAAQGAPFHVTERSTGRnfLAQLRYGDPF--LMREVDI-HNSL----DHPNIVQMHDA-YDDE---KLAVTVIDNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  118 CNGGsvtELVK-GLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEgGVKLVDFGVSAQLTSTRLR 196
Cdd:cd14109    79 ASTI---ELVRdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRRLLRGKLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  197 RNTsVGTPFWMAPEVIACEQQYDSSydarcDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHP-EKWCEEF 275
Cdd:cd14109   155 TLI-YGSPEFVSPEIVNSYPVTLAT-----DMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPlGNISDDA 228
                         250       260
                  ....*....|....*....|....*..
gi 578803747  276 NHFISQCLIKDFERRPSVTHLLDHPFI 302
Cdd:cd14109   229 RDFIKKLLVYIPESRLTVDEALNHPWF 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
48-292 7.32e-15

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 76.27  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   48 GKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKadhcvGGQLWLVLELCNGGSVTELv 127
Cdd:cd13992    14 PKYVKKVGVYGGRTVAIKHITFSRTEKRTILQELNQLKEL-VHDNLNKFIGICIN-----PPNIAVVTEYCTRGSLQDV- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  128 kgLLRCGQRLDEAMISYILYGALLGLQHLHNNRII-HRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTP-- 204
Cdd:cd13992    87 --LLNREIKMDWMFKSSFIKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHkk 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  205 -FWMAPEVIaceQQYDSSY--DARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRN----PPPTLLHPEKWCE-EFN 276
Cdd:cd13992   165 lLWTAPELL---RGSLLEVrgTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGgnkpFRPELAVLLDEFPpRLV 241
                         250
                  ....*....|....*.
gi 578803747  277 HFISQCLIKDFERRPS 292
Cdd:cd13992   242 LLVKQCWAENPEKRPS 257
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
39-238 7.84e-15

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 76.35  E-value: 7.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKR-----DGSLAAVKILDPVSDMDEEIEAEYNILQFLP-NHPNVVKFYGMFYKAD-HCvggql 111
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAKGieeegGETLVLVKALQKTKDENLQSEFRRELDMFRKlSHKNVVRLLGLCREAEpHY----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 wLVLELCNGGSVtelvKGLLRCGQRLDEAMIS---------YILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV 182
Cdd:cd05046    85 -MILEYTDLGDL----KQFLRATKSKDEKLKPpplstkqkvALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  183 DFGVSAQLTSTR--LRRNTSVgtPF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIEL 238
Cdd:cd05046   160 LLSLSKDVYNSEyyKLRNALI--PLrWLAPEAV-----QEDDFSTKSDVWSFGVLMWEV 211
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
40-233 8.34e-15

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 75.81  E-value: 8.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTnKRDGSLAAVKILDpvSDMDEEIE----AEYNIL-QFlpNHPNVVKFYGMfykadhCVGGQ-LWL 113
Cdd:cd05085     2 ELLGKGNFGEVYKGT-LKDKTPVAVKTCK--EDLPQELKikflSEARILkQY--DHPNIVKLIGV------CTQRQpIYI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKgllrcgQRLDEAMISYILYGAL---LGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ- 189
Cdd:cd05085    71 VMELVPGGDFLSFLR------KKKDELKTKQLVKFSLdaaAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQe 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  190 ----LTSTRLRRntsvgTPF-WMAPEVIaceqQYdSSYDARCDVWSLGI 233
Cdd:cd05085   145 ddgvYSSSGLKQ-----IPIkWTAPEAL----NY-GRYSSESDVWSFGI 183
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
34-338 1.17e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 76.94  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKR-DGSLAAVKILDPVSDMDEE----IEAEYNILQFLpNHPNVVKFYGMFYKADHcvg 108
Cdd:PTZ00426   30 EDFNFIRTLGTGSFGRVILATYKNeDFPPVAIKRFEKSKIIKQKqvdhVFSERKILNYI-NHPFCVNLYGSFKDESY--- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gqLWLVLELCNGGSVTELvkglLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsA 188
Cdd:PTZ00426  106 --LYLVLEFVIGGEFFTF----LRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGF-A 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRrnTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNpppTLLHP 268
Cdd:PTZ00426  179 KVVDTRTY--TLCGTPEYIAPEIL-----LNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEG---IIYFP 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  269 EKWCEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGkVLFLQKQLaKVLQDQKHQNPVAKTRHERMH 338
Cdd:PTZ00426  249 KFLDNNCKHLMKKLLSHDLTKRygnlkKGAQNVKEHPWFGNIDW-VSLLHKNV-EVPYKPKYKNVFDSSNFERVQ 321
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
34-241 1.19e-14

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 76.27  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAirEASLLKGL-KHANIVLLHDIIHTKE-----TL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 191
Cdd:cd07869    79 TLVFEYVH----TDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578803747  192 STRLRRNTSVGTPFWMAPEVIACEQQYDSSYdarcDVWSLGITAIELGDG 241
Cdd:cd07869   155 VPSHTYSNEVVTLWYRPPDVLLGSTEYSTCL----DMWGVGCIFVEMIQG 200
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
39-238 1.19e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 76.12  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKV----YKVTNKRDGSLAAVKILDP------VSDMDEEIEaeynILQFLpNHPNVVKFYGMfykADHCVG 108
Cdd:cd05079     9 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPesggnhIADLKKEIE----ILRNL-YHENIVKYKGI---CTEDGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVTELV---KGLLRCGQRLDEAMisyilyGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd05079    81 NGIKLIMEFLPSGSLKEYLprnKNKINLKQQLKYAV------QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  186 VSAQLTSTR--LRRNTSVGTP-FWMAPEVIACEQQYDSSydarcDVWSLGITAIEL 238
Cdd:cd05079   155 LTKAIETDKeyYTVKDDLDSPvFWYAPECLIQSKFYIAS-----DVWSFGVTLYEL 205
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
34-339 1.20e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 76.19  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFYKADhcvggQL 111
Cdd:cd07873     2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAirEVSLLKDL-KHANIVTLHDIIHTEK-----SL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS-AQL 190
Cdd:cd07873    76 TLVFEYLD----KDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLArAKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLRRNTSVgTPFWMAPEVIACEQQYDSsydaRCDVWSLGITAIELGDGDpPLFDMHPVKT----LFKIPRNPP---- 262
Cdd:cd07873   152 IPTKTYSNEVV-TLWYRPPDILLGSTDYST----QIDMWGVGCIFYEMSTGR-PLFPGSTVEEqlhfIFRILGTPTeetw 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  263 PTLLHPEKWcEEFNH--FISQCLIKDFERrpsvthlLDHPFIKgVHGKVLFLQKQlAKVLQDQKHQNPVAKTRHERMHT 339
Cdd:cd07873   226 PGILSNEEF-KSYNYpkYRADALHNHAPR-------LDSDGAD-LLSKLLQFEGR-KRISAEEAMKHPYFHSLGERIHK 294
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
42-291 1.27e-14

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 75.75  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYG----KVYKVTNKR-DGSLAAVKILDPVSDMDEEIEaEYNILQFLPNhPNVVKFYGMfykadhCVGGQLWLVLE 116
Cdd:cd05115    12 LGSGNFGcvkkGVYKMRKKQiDVAIKVLKQGNEKAVRDEMMR-EAQIMHQLDN-PYIVRMIGV------CEAEALMLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGllrcgqRLDEAMISYI---LYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS- 192
Cdd:cd05115    84 MASGGPLNKFLSG------KKDEITVSNVvelMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGAd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 -TRLRRNTSVGTPF-WMAPEVIACEQqydssYDARCDVWSLGITAIE-LGDGDPPLFDMHPVKTLFKIPRNppPTLLHPE 269
Cdd:cd05115   158 dSYYKARSAGKWPLkWYAPECINFRK-----FSSRSDVWSYGVTMWEaFSYGQKPYKKMKGPEVMSFIEQG--KRMDCPA 230
                         250       260
                  ....*....|....*....|..
gi 578803747  270 KWCEEFNHFISQCLIKDFERRP 291
Cdd:cd05115   231 ECPPEMYALMSDCWIYKWEDRP 252
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
41-247 1.32e-14

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 76.10  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   41 TIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd05607     9 VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKmallEKEILEKV-NSPFIVSLAYAFETKTH-----LCLVMS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGsvtELVKGLLRCGQRLDEaMISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 194
Cdd:cd05607    83 LMNGG---DLKYHIYNVGERGIE-MERVIFYSAQItcGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGK 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578803747  195 lRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITAIELGDGDPPLFD 247
Cdd:cd05607   159 -PITQRAGTNGYMAPEILK-----EESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
40-298 1.77e-14

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 75.07  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSL---AAVKIL--DPVSDMD--EEIEAEYNILQFLpNHPNVVKFYGMFYkaDHcvggQLW 112
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSGKviqVAVKCLksDVLSQPNamDDFLKEVNAMHSL-DHPNLIRLYGVVL--SS----PLM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGGSVTELVKglLRCGQRLDEAMISYILYGALlGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd05040    74 MVTELAPLGSLLDRLR--KDQGHFLISTLCDYAVQIAN-GMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 T----RLRRNTSVgtPF-WMAPEVIACEQQYDSSydarcDVWSLGITAIEL-GDGDPPLFDMHPVKTLFKIPRNppPTLL 266
Cdd:cd05040   151 NedhyVMQEHRKV--PFaWCAPESLKTRKFSHAS-----DVWMFGVTLWEMfTYGEEPWLGLNGSQILEKIDKE--GERL 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578803747  267 HPEKWC-EEFNHFISQCLIKDFERRPSVTHLLD 298
Cdd:cd05040   222 ERPDDCpQDIYNVMLQCWAHKPADRPTFVALRD 254
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
32-257 1.84e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 75.82  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVT-------NKRDGSLAAVKIL-DPVSDMD-EEIEAEYNILQFLPNHPNVVKFYGMFYK 102
Cdd:cd05101    22 PRDKLTLGKPLGEGCFGQVVMAEavgidkdKPKEAVTVAVKMLkDDATEKDlSDLVSEMEMMKMIGKHKNIINLLGACTQ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 adhcvGGQLWLVLELCNGGSVTELVKGLLRCGQ-------RLDEAMISY-----ILYGALLGLQHLHNNRIIHRDVKGNN 170
Cdd:cd05101   102 -----DGPLYVIVEYASKGNLREYLRARRPPGMeysydinRVPEEQMTFkdlvsCTYQLARGMEYLASQKCIHRDLAARN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  171 ILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIE---LGdGDPpl 245
Cdd:cd05101   177 VLVTENNVMKIADFGLARDINNIDYYKKTTNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGVLMWEiftLG-GSP-- 248
                         250
                  ....*....|..
gi 578803747  246 FDMHPVKTLFKI 257
Cdd:cd05101   249 YPGIPVEELFKL 260
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
40-233 1.98e-14

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 74.83  E-value: 1.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMD-EEIEAEYNILQFLPNHPNVVKFYGMFYkaDHCVGGQLWLVLELC 118
Cdd:cd13975     6 RELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHwNDLALEFHYTRSLPKHERIVSLHGSVI--DYSYGGGSSIAVLLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  119 NGGSVTELVKGLlRCGQRLDEAMisYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGvsaqLTSTRLRRN 198
Cdd:cd13975    84 MERLHRDLYTGI-KAGLSLEERL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLG----FCKPEAMMS 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 578803747  199 TS-VGTPFWMAPEViaceqqYDSSYDARCDVWSLGI 233
Cdd:cd13975   157 GSiVGTPIHMAPEL------FSGKYDNSVDVYAFGI 186
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
37-238 2.11e-14

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 75.14  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKRDGSLA----AVKIL----DPVSDmdEEIEAEYNILQFLpNHPNVVKFYGMfykadhCVG 108
Cdd:cd05057    10 EKGKVLGSGAFGTVYKGVWIPEGEKVkipvAIKVLreetGPKAN--EEILDEAYVMASV-DHPHLVRLLGI------CLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVTELVKgllrcgQRLDEAMISYILYGALL---GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 185
Cdd:cd05057    81 SQVQLITQLMPLGCLLDYVR------NHRDNIGSQLLLNWCVQiakGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  186 VSAQLTSTRLRRNTSVG-TPF-WMAPEVIaceqQYdSSYDARCDVWSLGITAIEL 238
Cdd:cd05057   155 LAKLLDVDEKEYHAEGGkVPIkWMALESI----QY-RIYTHKSDVWSYGVTVWEL 204
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
33-246 2.22e-14

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 76.07  E-value: 2.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVK-ILDPVSD--MDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd07856     9 TTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKkIMKPFSTpvLAKRTYRELKLLKHL-RHENIISLSDIFISPLE---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCnGGSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS-- 187
Cdd:cd07856    84 DIYFVTELL-GTDLHRLLTS-----RPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAri 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803747  188 --AQLTSTrlrrntsVGTPFWMAPEVIACEQQydssYDARCDVWSLGITAIELGDGDpPLF 246
Cdd:cd07856   158 qdPQMTGY-------VSTRYYRAPEIMLTWQK----YDVEVDIWSAGCIFAEMLEGK-PLF 206
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
39-269 2.40e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 76.59  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDE----EIEAEYNILQFLPNHPnVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd05626     6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRnqvaHVKAERDILAEADNEW-VVKLYYSFQDKDN-----LYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELvkgLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST- 193
Cdd:cd05626    80 MDYIPGGDMMSL---LIRMEV-FPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 ---------------------------------------RLRR-------NTSVGTPFWMAPEVIaceqqYDSSYDARCD 227
Cdd:cd05626   156 nskyyqkgshirqdsmepsdlwddvsncrcgdrlktleqRATKqhqrclaHSLVGTPNYIAPEVL-----LRKGYTQLCD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  228 VWSLGITAIELGDGDPPLFDMHPVKTLFKIP------RNPPPTLLHPE 269
Cdd:cd05626   231 WWSVGVILFEMLVGQPPFLAPTPTETQLKVInwentlHIPPQVKLSPE 278
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
37-297 2.43e-14

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 74.69  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYKVTNKrdGSLAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKADHcvggqLWLVLE 116
Cdd:cd05039     9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAAQAFLAEASVMTTL-RHPNLVQLLGVVLEGNG-----LYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELvkglLRCGQRLDEAMISYILYG--ALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG----VSAQL 190
Cdd:cd05039    81 YMAKGSLVDY----LRSRGRAVITRKDQLGFAldVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGlakeASSNQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  191 TSTRLrrntsvgtPF-WMAPEVIACEQqydssYDARCDVWSLGITAIElgdgdpplfdmhpvktLFKIPRNPPP------ 263
Cdd:cd05039   157 DGGKL--------PIkWTAPEALREKK-----FSTKSDVWSFGILLWE----------------IYSFGRVPYPriplkd 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578803747  264 TLLH---------PEKWCEEFNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd05039   208 VVPHvekgyrmeaPEGCPPEVYKVMKNCWELDPAKRPTFKQLR 250
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
35-310 2.43e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 75.03  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvggQ 110
Cdd:cd05631     1 TFRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmalnEKRILEKV-NSRFVVSLAYAYETKD-----A 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVTELVKGLLRCGqrLDEAmiSYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05631    75 LCLVLTIMNGGDLKFHIYNMGNPG--FDEQ--RAIFYAAELccGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNtSVGTPFWMAPEVIACEqqydsSYDARCDVWSLGITAIELGDGDPPlFDMHP--VKTLFKIPRNPPPTLL 266
Cdd:cd05631   151 QIPEGETVRG-RVGTVGYMAPEVINNE-----KYTFSPDWWGLGCLIYEMIQGQSP-FRKRKerVKREEVDRRVKEDQEE 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578803747  267 HPEKWCEEFNHFISQCLIKDFERRPSVT-----HLLDHPFIKGVHGKVL 310
Cdd:cd05631   224 YSEKFSEDAKSICRMLLTKNPKERLGCRgngaaGVKQHPIFKNINFKRL 272
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
36-305 2.52e-14

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 75.97  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVK----ILDPVSDMdEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVGGQL 111
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKkindVFEHVSDA-TRILREIKLLRLL-RHPDIVEIKHIMLPPSRREFKDI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKgLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG---VSA 188
Cdd:cd07859    80 YVVFELME----SDLHQ-VIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGlarVAF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 QLTSTRLRRNTSVGTPFWMAPEVIACeqqYDSSYDARCDVWSLGITAIELGDGDpPLFD----MHPVKTLFKIPRNPPPT 264
Cdd:cd07859   155 NDTPTAIFWTDYVATRWYRAPELCGS---FFSKYTPAIDIWSIGCIFAEVLTGK-PLFPgknvVHQLDLITDLLGTPSPE 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803747  265 LL------------------HPEKWCEEFNH-------FISQCLIKDFERRPSVTHLLDHPFIKGV 305
Cdd:cd07859   231 TIsrvrnekarrylssmrkkQPVPFSQKFPNadplalrLLERLLAFDPKDRPTAEEALADPYFKGL 296
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
31-297 2.78e-14

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 74.22  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   31 DPTDTWEIIEtIGKGTYGKVYKVT--NKRDgslAAVKILDPVSDMDEEIEAEYNILQFLpNHPNVVKFYGMFYKAdhcvg 108
Cdd:cd05112     2 DPSELTFVQE-IGSGQFGLVHLGYwlNKDK---VAIKTIREGAMSEEDFIEEAEVMMKL-SHPKLVQLYGVCLEQ----- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 GQLWLVLELCNGGSVTELVKGllRCGQRLDEAMISYILyGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 188
Cdd:cd05112    72 APICLVFEFMEHGCLSDYLRT--QRGLFSAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  189 -----QLTStrlrrntSVGTPF---WMAPEVIACeqqydSSYDARCDVWSLGITAIEL-GDGDPPLFDMHPVKTLFKIpr 259
Cdd:cd05112   149 fvlddQYTS-------STGTKFpvkWSSPEVFSF-----SRYSSKSDVWSFGVLMWEVfSEGKIPYENRSNSEVVEDI-- 214
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578803747  260 NPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLL 297
Cdd:cd05112   215 NAGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
42-252 2.79e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 75.00  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVTNKRDGSLAAVKI----LDPVSDmdEEIEAEYNILQFLpNHPNVVKFYGMFYKADHCVGGQL-WLVLE 116
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQcrqeLSPKNR--ERWCLEIQIMKRL-NHPNVVAARDVPEGLQKLAPNDLpLLAME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  117 LCNGGSVTELVKGLLRC-GQRldEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLtTEGGVKLV----DFGVSAQLT 191
Cdd:cd14038    79 YCQGGDLRKYLNQFENCcGLR--EGAILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGEQRLIhkiiDLGYAKELD 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  192 STRLrrNTS-VGTPFWMAPEVIacEQQydsSYDARCDVWSLGITAIELGDG-DPPLFDMHPVK 252
Cdd:cd14038   156 QGSL--CTSfVGTLQYLAPELL--EQQ---KYTVTVDYWSFGTLAFECITGfRPFLPNWQPVQ 211
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
32-267 3.78e-14

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 74.42  E-value: 3.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKV-----YKVTNKRDGSLAAVKILDPVSDMD--EEIEAEYNILQFLpNHPNVVKFYGMfykad 104
Cdd:cd05049     3 KRDTIVLKRELGEGAFGKVflgecYNLEPEQDKMLVAVKTLKDASSPDarKDFEREAELLTNL-QHENIVKFYGV----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  105 hCV-GGQLWLVLELCNGGSVTELVKG-------LLRCGQRLDEAMISYILYGAL---LGLQHLHNNRIIHRDVKGNNILL 173
Cdd:cd05049    77 -CTeGDPLLMVFEYMEHGDLNKFLRShgpdaafLASEDSAPGELTLSQLLHIAVqiaSGMVYLASQHFVHRDLATRNCLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  174 TTEGGVKLVDFGVSAQLTSTRLRRntsVG----TPF-WMAPEVIaceqQYdSSYDARCDVWSLGITAIELGD-GDPPLFD 247
Cdd:cd05049   156 GTNLVVKIGDFGMSRDIYSTDYYR---VGghtmLPIrWMPPESI----LY-RKFTTESDVWSFGVVLWEIFTyGKQPWFQ 227
                         250       260
                  ....*....|....*....|....*...
gi 578803747  248 M--HPV------KTLFKIPRNPPPTLLH 267
Cdd:cd05049   228 LsnTEViecitqGRLLQRPRTCPSEVYA 255
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
32-299 5.00e-14

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 73.96  E-value: 5.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   32 PTDTWEIIETIGKGTYGKVYKVT-NKRDGSLA----AVKILDPV----SDMDEEIEAEYnILQFlpNHPNVVKFYGMFYK 102
Cdd:cd05036     4 PRKNLTLIRALGQGAFGEVYEGTvSGMPGDPSplqvAVKTLPELcseqDEMDFLMEALI-MSKF--NHPNIVRCIGVCFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  103 ADhcvggQLWLVLELCNGGSVtelvKGLLRcGQRLDEAMISYILYGALL--------GLQHLHNNRIIHRDVKGNNILLT 174
Cdd:cd05036    81 RL-----PRFILLELMAGGDL----KSFLR-ENRPRPEQPSSLTMLDLLqlaqdvakGCRYLEENHFIHRDIAARNCLLT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  175 TEGG---VKLVDFGVSAQL-TSTRLRRNTSVGTPF-WMAPEVIaceqqYDSSYDARCDVWSLGITAIElgdgdpplfdmh 249
Cdd:cd05036   151 CKGPgrvAKIGDFGMARDIyRADYYRKGGKAMLPVkWMPPEAF-----LDGIFTSKTDVWSFGVLLWE------------ 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803747  250 pvktLFKIPRNPPPTL--------------LHPEKWC-EEFNHFISQCLIKDFERRPSVTHLLDH 299
Cdd:cd05036   214 ----IFSLGYMPYPGKsnqevmefvtsggrMDPPKNCpGPVYRIMTQCWQHIPEDRPNFSTILER 274
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
34-310 5.40e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 74.62  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKADhcvgg 109
Cdd:cd05632     2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESmalnEKQILEKV-NSQFVVNLAYAYETKD----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELVKGLLRCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05632    76 ALCLVLTIMNGGDLKFHIYNMGNPG--FEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNtSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPT-LLHP 268
Cdd:cd05632   154 IPEGESIRG-RVGTVGYMAPEVLNNQR-----YTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETeEVYS 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578803747  269 EKWCEEFNHFISQCLIKDFERR-----PSVTHLLDHPFIKGVHGKVL 310
Cdd:cd05632   228 AKFSEEAKSICKMLLTKDPKQRlgcqeEGAGEVKRHPFFRNMNFKRL 274
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
36-279 5.94e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.91  E-value: 5.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYkvTNKRDGSLAAV--KILDPVSDMdeeIEAEynILQFLpNHPNVVKFYGM-FYKADHCvggqlw 112
Cdd:PHA03209   68 YTVIKTLTPGSEGRVF--VATKPGQPDPVvlKIGQKGTTL---IEAM--LLQNV-NHPSVIRMKDTlVSGAITC------ 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGvSAQLTS 192
Cdd:PHA03209  134 MVLPHYS----SDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPV 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIAceqqyDSSYDARCDVWSLGITaielgdgdppLFDM--HPvKTLFKiprNPPPTLLHPEK 270
Cdd:PHA03209  209 VAPAFLGLAGTVETNAPEVLA-----RDKYNSKADIWSAGIV----------LFEMlaYP-STIFE---DPPSTPEEYVK 269

                  ....*....
gi 578803747  271 WCEefNHFI 279
Cdd:PHA03209  270 SCH--SHLL 276
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
33-249 7.68e-14

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 74.52  E-value: 7.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   33 TDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNH-----PNVVKFYGMFYKADH-C 106
Cdd:cd14134    11 TNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKdpngkSHCVQLRDWFDYRGHmC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  107 vggqlwLVLELCnGGSVTELVKGLLRCGQRLDE-AMISYILygaLLGLQHLHNNRIIHRDVKGNNILLTTEG-------- 177
Cdd:cd14134    91 ------IVFELL-GPSLYDFLKKNNYGPFPLEHvQHIAKQL---LEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  178 -----------GVKLVDFGvSA--------QLTSTRLRRntsvgtpfwmAPEVIAceqQYDSSYdaRCDVWSLGITAIEL 238
Cdd:cd14134   161 kkrqirvpkstDIKLIDFG-SAtfddeyhsSIVSTRHYR----------APEVIL---GLGWSY--PCDVWSIGCILVEL 224
                         250
                  ....*....|.
gi 578803747  239 GDGDpPLFDMH 249
Cdd:cd14134   225 YTGE-LLFQTH 234
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
34-243 1.20e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 73.49  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEA--EYNILQFLpNHPNVVKFYGMFYkadhcVGGQL 111
Cdd:cd07872     6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAirEVSLLKDL-KHANIVTLHDIVH-----TDKSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  112 WLVLELCNggsvTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS-AQL 190
Cdd:cd07872    80 TLVFEYLD----KDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLArAKS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578803747  191 TSTRLRRNTSVgTPFWMAPEVIACEqqydSSYDARCDVWSLGITAIELGDGDP 243
Cdd:cd07872   156 VPTKTYSNEVV-TLWYRPPDVLLGS----SEYSTQIDMWGVGCIFFEMASGRP 203
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
40-231 1.38e-13

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 73.18  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDGS----LAAVKILDPVS----DMDEEIEAEYNIlqflpNHPNVVKFYGmfyKADHCVGG-- 109
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKQNASgqyeTVAVKIFPYEEyaswKNEKDIFTDASL-----KHENILQFLT---AEERGVGLdr 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCNGGSVTELVKGLLrcgqrLDEAMISYILYGALLGLQHLHNNR---------IIHRDVKGNNILLTTEGGVK 180
Cdd:cd14055    73 QYWLITAYHENGSLQDYLTRHI-----LSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCV 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578803747  181 LVDFGVS----AQLTSTRLRRNTSVGTPFWMAPEVIACE---QQYDSSydARCDVWSL 231
Cdd:cd14055   148 LADFGLAlrldPSLSVDELANSGQVGTARYMAPEALESRvnlEDLESF--KQIDVYSM 203
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
34-259 1.47e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 72.93  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   34 DTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpVSDMDEEIEA----EYNILQFLpNHPNVVKFYGMFYKaDHCvgg 109
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIR-LEQEDEGVPStairEISLLKEM-QHGNIVRLQDVVHS-EKR--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCNggsvTELVKGLLRCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT-TEGGVKLVDFGVs 187
Cdd:PLN00009   76 -LYLVFEYLD----LDLKKHMDSSPDfAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGL- 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  188 AQLTSTRLRRNT-SVGTPFWMAPEVIACEQQYDSSydarCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPR 259
Cdd:PLN00009  150 ARAFGIPVRTFThEVVTLWYRAPEILLGSRHYSTP----VDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFR 218
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
36-238 1.60e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 73.58  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNK-RDGSLAAVKILDPVSDMDEEIEAEYN-ILQFLPNHPNVVKFYGMFYKADHCVGGQ-LW 112
Cdd:cd07874    19 YQNLKPIGSGAQGIVCAAYDAvLDRNVAIKKLSRPFQNQTHAKRAYRElVLMKCVNHKNIISLLNVFTPQKSLEEFQdVY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  113 LVLELCNGgSVTELVKgllrcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLTS 192
Cdd:cd07874    99 LVMELMDA-NLCQVIQ------MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAG 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578803747  193 TRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIEL 238
Cdd:cd07874   171 TSFMMTPYVVTRYYRAPEVI-----LGMGYKENVDIWSVGCIMGEM 211
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
42-250 1.76e-13

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 72.51  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKvtNKRDGSLAAVKILDPVSDMDEEIEAEynILQ-FLPNHPNVVKFYGMFYKADHCVGgQLWLVLELCNG 120
Cdd:cd14144     3 VGKGRYGEVWK--GKWRGEKVAVKIFFTTEEASWFRETE--IYQtVLMRHENILGFIAADIKGTGSWT-QLYLITDYHEN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  121 GSVTELVKGllrcgQRLDEAMISYILYGALLGLQHLHNN--------RIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 192
Cdd:cd14144    78 GSLYDFLRG-----NTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVKFIS 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803747  193 ----TRLRRNTSVGTPFWMAPEVIAcEQQYDSSYDA--RCDVWSLGITAIELG----------DGDPPLFDMHP 250
Cdd:cd14144   153 etneVDLPPNTRVGTKRYMAPEVLD-ESLNRNHFDAykMADMYSFGLVLWEIArrcisggiveEYQLPYYDAVP 225
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
40-298 2.10e-13

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 71.93  E-value: 2.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTNKRDG---SLAAVKILDP--VSDMDEEIEAEYNIL-QFlpNHPNVVKFYGMFYKADHCVggqlwL 113
Cdd:cd05063    11 KVIGAGEFGEVFRGILKMPGrkeVAVAIKTLKPgyTEKQRQDFLSEASIMgQF--SHHNIIRLEGVVTKFKPAM-----I 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  114 VLELCNGGSVTELVKgllrcgqRLDEAMISYILYGAL----LGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 189
Cdd:cd05063    84 ITEYMENGALDKYLR-------DHDGEFSSYQLVGMLrgiaAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  190 LTSTRLRRNTSVGTPF---WMAPEVIACEQQYDSSydarcDVWSLGITAIE-LGDGDPPLFDMHPVKTLFKIprNPPPTL 265
Cdd:cd05063   157 LEDDPEGTYTTSGGKIpirWTAPEAIAYRKFTSAS-----DVWSFGIVMWEvMSFGERPYWDMSNHEVMKAI--NDGFRL 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578803747  266 LHPEKWCEEFNHFISQCLIKDFERRP---SVTHLLD 298
Cdd:cd05063   230 PAPMDCPSAVYQLMLQCWQQDRARRPrfvDIVNLLD 265
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
36-246 2.20e-13

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 73.05  E-value: 2.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFL------PNHPNVVKFYGMFYKADHcvgg 109
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLntkydpEDKHHIVRLLDHFMHHGH---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 qLWLVLELCnGGSVTELVKgllrcgQR----LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT--EGGVKLVD 183
Cdd:cd14212    77 -LCIVFELL-GVNLYELLK------QNqfrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNldSPEIKLID 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  184 FGVSAQLTSTRLrrnTSVGTPFWMAPEVIACEQqydssYDARCDVWSLGITAIELGDGdPPLF 246
Cdd:cd14212   149 FGSACFENYTLY---TYIQSRFYRSPEVLLGLP-----YSTAIDMWSLGCIAAELFLG-LPLF 202
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
40-239 2.52e-13

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 72.39  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKVTnkRDGSLAAVKILDPVSDmdEEIEAEYNILQ-FLPNHPNVVKFYGmfykADHCVGGQLW----LV 114
Cdd:cd14054     1 QLIGQGRYGTVWKGS--LDERPVAVKVFPARHR--QNFQNEKDIYElPLMEHSNILRFIG----ADERPTADGRmeylLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELVK-------GLLRCGQRLDEamisyilygallGLQHLHNNR---------IIHRDVKGNNILLTTEGG 178
Cdd:cd14054    73 LEYAPKGSLCSYLRentldwmSSCRMALSLTR------------GLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGS 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803747  179 VKLVDFGVSAQLTSTRLRRN----------TSVGTPFWMAPEVI--ACEQQYDSSYDARCDVWSLGITAIELG 239
Cdd:cd14054   141 CVICDFGLAMVLRGSSLVRGrpgaaenasiSEVGTLRYMAPEVLegAVNLRDCESALKQVDVYALGLVLWEIA 213
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
35-246 2.69e-13

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 72.03  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   35 TWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDpvsdMDEEIEA------EYNILQFLpNHPNVVKFYGMFYKADhcvg 108
Cdd:cd07844     1 TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIR----LEHEEGApftairEASLLKDL-KHANIVTLHDIIHTKK---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  109 gQLWLVLELCnggsVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS- 187
Cdd:cd07844    72 -TLTLVFEYL----DTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAr 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578803747  188 AQLTSTRLRRNTSVgTPFWMAPEVIACEQQYDSSYdarcDVWSLGITAIELGDGDpPLF 246
Cdd:cd07844   147 AKSVPSKTYSNEVV-TLWYRPPDVLLGSTEYSTSL----DMWGVGCIFYEMATGR-PLF 199
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
40-251 3.39e-13

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 71.70  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   40 ETIGKGTYGKVYKvtNKRDGSLAAVKILdpvSDMDEEI---EAEynILQ-FLPNHPNVVKFYGMFYKaDHCVGGQLWLVL 115
Cdd:cd14143     1 ESIGKGRFGEVWR--GRWRGEDVAVKIF---SSREERSwfrEAE--IYQtVMLRHENILGFIAADNK-DNGTWTQLWLVS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSvteLVKGLLRcgQRLD-EAMISYILYGALlGLQHLHNN--------RIIHRDVKGNNILLTTEGGVKLVDFGV 186
Cdd:cd14143    73 DYHEHGS---LFDYLNR--YTVTvEGMIKLALSIAS-GLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  187 SAQLTSTR----LRRNTSVGTPFWMAPEVIAcEQQYDSSYDA--RCDVWSLGITAIELG----------DGDPPLFDMHP 250
Cdd:cd14143   147 AVRHDSATdtidIAPNHRVGTKRYMAPEVLD-DTINMKHFESfkRADIYALGLVFWEIArrcsiggiheDYQLPYYDLVP 225

                  .
gi 578803747  251 V 251
Cdd:cd14143   226 S 226
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
36-243 4.00e-13

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 72.86  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   36 WEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLP-----NHPNVVKFYGMFYKADH-CVGG 109
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKkqdkdNTMNVIHMLESFTFRNHiCMTF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLwLVLELcnggsvTELVKgllRCG-QRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGV 186
Cdd:cd14224   147 EL-LSMNL------YELIK---KNKfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGrsGIKVIDFGS 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578803747  187 SAqltSTRLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCDVWSLGITAIELGDGDP 243
Cdd:cd14224   217 SC---YEHQRIYTYIQSRFYRAPEVI-----LGARYGMPIDMWSFGCILAELLTGYP 265
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
42-298 5.18e-13

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 71.28  E-value: 5.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYKVtnKRDG------SLAAVKILDP------VSDMDEEIEAEYNILQFLpNHPNVVKFYGmFYKADHcvgG 109
Cdd:cd14001     7 LGYGTGVNVYLM--KRSPrggssrSPWAVKKINSkcdkgqRSLYQERLKEEAKILKSL-NHPNIVGFRA-FTKSED---G 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  110 QLWLVLELCnGGSVTELVKgllrcgQRLDE-------AMISYILYGALLGLQHLHNN-RIIHRDVKGNNILLTTE-GGVK 180
Cdd:cd14001    80 SLCLAMEYG-GKSLNDLIE------ERYEAglgpfpaATILKVALSIARALEYLHNEkKILHGDIKSGNVLIKGDfESVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  181 LVDFGVSAQLTST-RLRRNTS---VGTPFWMAPEVIacEQQYDSSYDArcDVWSLGITAIELGDGDPPLFDMHPVKT--- 253
Cdd:cd14001   153 LCDFGVSLPLTENlEVDSDPKaqyVGTEPWKAKEAL--EEGGVITDKA--DIFAYGLVLWEMMTLSVPHLNLLDIEDdde 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803747  254 --------------LFKIPRNPPptlLHPEKWCEEFNHFI---SQCLIKDFERRPSVTHLLD 298
Cdd:cd14001   229 desfdedeedeeayYGTLGTRPA---LNLGELDDSYQKVIelfYACTQEDPKDRPSAAHIVE 287
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
39-269 6.06e-13

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 72.39  E-value: 6.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   39 IETIGKGTYGKVYKVTNKRDGSLAAVKILDP----VSDMDEEIEAEYNILQFLPNHPnVVKFYGMFYKADHcvggqLWLV 114
Cdd:cd05625     6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKkdvlLRNQVAHVKAERDILAEADNEW-VVRLYYSFQDKDN-----LYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  115 LELCNGGSVTELvkgLLRCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST- 193
Cdd:cd05625    80 MDYIPGGDMMSL---LIRMGV-FPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  194 ----------------------------------------------RLRRNTSVGTPFWMAPEVIaceqqYDSSYDARCD 227
Cdd:cd05625   156 dskyyqsgdhlrqdsmdfsnewgdpencrcgdrlkplerraarqhqRCLAHSLVGTPNYIAPEVL-----LRTGYTQLCD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578803747  228 VWSLGITAIELGDGDPPLFDMHPVKTLFKIPR------NPPPTLLHPE 269
Cdd:cd05625   231 WWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqtslhIPPQAKLSPE 278
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
37-292 8.35e-13

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 70.20  E-value: 8.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   37 EIIETIGKGTYGKVYK--VTNKRDGSLAAVKILDPVSDMDEE--IEAEYNILQFLP--NHPNVVKFYGMfykadhCVGGQ 110
Cdd:cd05037     2 TFHEHLGQGTFTNIYDgiLREVGDGRVQEVEVLLKVLDSDHRdiSESFFETASLMSqiSHKHLVKLYGV------CVADE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  111 LWLVLELCNGGSVTelvKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG------VKLVDF 184
Cdd:cd05037    76 NIMVQEYVRYGPLD---KYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  185 GVSaqltSTRLRRNTSVGTPFWMAPEviaCEQQYDSSYDARCDVWSLGITAIEL-GDGDPPLFDMHPV-KTLFKIPRNPP 262
Cdd:cd05037   153 GVP----ITVLSREERVDRIPWIAPE---CLRNLQANLTIAADKWSFGTTLWEIcSGGEEPLSALSSQeKLQFYEDQHQL 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 578803747  263 PTllhPEkwCEEFNHFISQCLIKDFERRPS 292
Cdd:cd05037   226 PA---PD--CAELAELIMQCWTYEPTKRPS 250
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
42-303 8.93e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 70.46  E-value: 8.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747   42 IGKGTYGKVYK-VTNKRDGSLAAVKILDPVSDMDEE--IEAEYNILQFLpNHPNVVKFYGMF---YKADHCVggqlWLVL 115
Cdd:cd14030    33 IGRGSFKTVYKgLDTETTVEVAWCELQDRKLSKSERqrFKEEAGMLKGL-QHPNIVRFYDSWestVKGKKCI----VLVT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  116 ELCNGGSVTELVKGLLRCGQRLDEAMISYILYGallgLQHLHNNR--IIHRDVKGNNILLT-TEGGVKLVDFGVsAQLTS 192
Cdd:cd14030   108 ELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKG----LQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGL-ATLKR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803747  193 TRLRRNTsVGTPFWMAPEViaceqqYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWC 272
Cdd:cd14030   183 ASFAKSV-IGTPEFMAPEM------YEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVAI 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578803747  273 EEFNHFISQCLIKDFERRPSVTHLLDHPFIK 303
Cdd:cd14030   256 PEVKEIIEGCIRQNKDERYAIKDLLNHAFFQ 286
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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