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Conserved domains on  [gi|526479851|ref|NP_001268364|]
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dual specificity mitogen-activated protein kinase kinase 4 isoform 2 [Homo sapiens]

Protein Classification

dual specificity mitogen-activated protein kinase kinase( domain architecture ID 10159662)

dual specificity mitogen-activated protein kinase kinase (MAP2K) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates; similar to human MAP2K4 that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
106-396 0e+00

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: 624.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd06616    1 YEFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd06616   81 WICMELMDISLDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEER 345
Cdd:cd06616  161 VDSIAKTRDAGCRPYMAPERIDPSASRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGDPPILSNSEER 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKIL 396
Cdd:cd06616  241 EFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVDVAAYVQKIL 291
 
Name Accession Description Interval E-value
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
106-396 0e+00

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: 624.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd06616    1 YEFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd06616   81 WICMELMDISLDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEER 345
Cdd:cd06616  161 VDSIAKTRDAGCRPYMAPERIDPSASRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGDPPILSNSEER 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKIL 396
Cdd:cd06616  241 EFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVDVAAYVQKIL 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
114-378 7.75e-84

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 256.69  E-value: 7.75e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKI-LKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   194 TS--FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK 271
Cdd:smart00220  81 GGdlFDLLKKRGR------LSEDEARFYLRQILSALEYLHSK-GIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   272 TRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEerEFSPSF 351
Cdd:smart00220 154 TTFVGTPEYMAPEVL----LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEW--DISPEA 227
                          250       260
                   ....*....|....*....|....*..
gi 526479851   352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
115-378 2.70e-45

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 155.86  E-value: 2.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:pfam00069   3 VLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKkEKIKKKKDKNILREIKI-LKKLNHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  194 -TSFDKFYKYvysvlDDVIPEEILGKITLATVKALNhlkenlkiihrdikpsnilldrsgniklcdfgiSGQLVDSIAKT 272
Cdd:pfam00069  82 gGSLFDLLSE-----KGAFSEREAKFIMKQILEGLE---------------------------------SGSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  273 RDagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKgDPPQLSNSEEREFSPSFI 352
Cdd:pfam00069 124 PW-----YMAPEVL----GGNPYGPKVDVWSLGCILYELLTGKPPFPGING--NEIYELII-DQPYAFPELPSNLSEEAK 191
                         250       260
                  ....*....|....*....|....*.
gi 526479851  353 NFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
116-367 1.72e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 150.16  E-value: 1.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMS 193
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELaaDPEARERFRREARALARLNH-PNIVRVYDVGEEDGRPYLVMEYVE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 -TSfdkfykyvysvLDDVI-------PEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISgQL 265
Cdd:COG0515   91 gES-----------LADLLrrrgplpPAEAL-RILAQLAEALAAA-HAAGIVHRDIKPANILLTPDGRVKLIDFGIA-RA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRD---AGCRPYMAPERidpsASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDPPQLSnS 342
Cdd:COG0515  157 LGGATLTQTgtvVGTPGYMAPEQ----ARGEPVDPRSDVYSLGVTLYELLTGRPPFDG-DSPAELLRAHLREPPPPPS-E 230
                        250       260
                 ....*....|....*....|....*
gi 526479851 343 EEREFSPSFINFVNLCLTKDESKRP 367
Cdd:COG0515  231 LRPDLPPALDAIVLRALAKDPEERY 255
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
91-379 1.17e-39

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 144.97  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  91 SIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCP 170
Cdd:PLN00034  54 SSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEI-LRDVNHP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 171 YIVQFYGALFREGDCWICMELMST-SFDKFYKYVYSVLDDViPEEILGKItlatvkALNHLKenlKIIHRDIKPSNILLD 249
Cdd:PLN00034 133 NVVKCHDMFDHNGEIQVLLEFMDGgSLEGTHIADEQFLADV-ARQILSGI------AYLHRR---HIVHRDIKPSNLLIN 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 250 RSGNIKLCDFGISGQLvdsiAKTRD-----AGCRPYMAPERIDPSASRQGYD-VRSDVWSLGITLYELATGRFPYP---- 319
Cdd:PLN00034 203 SAKNVKIADFGVSRIL----AQTMDpcnssVGTIAYMSPERINTDLNHGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrq 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 320 -KWNSVfdqLTQVVKGDPPQLSNSEEREFSpsfiNFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:PLN00034 279 gDWASL---MCAICMSQPPEAPATASREFR----HFISCCLQREPAKRWSAMQLLQHPFIL 332
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
170-318 7.25e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 91.40  E-value: 7.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 170 PYIVQFY--GAlfrEGDC-WICMElmstsfdkfykYVY-SVLDDVIPEEilGKITLATV--------KALNHLKENlKII 237
Cdd:NF033483  67 PNIVSVYdvGE---DGGIpYIVME-----------YVDgRTLKDYIREH--GPLSPEEAveimiqilSALEHAHRN-GIV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 238 HRDIKPSNILLDRSGNIKLCDFGI----SGQlvdSIAKTRDA-GCRPYMAPERIdpsasRQGY-DVRSDVWSLGITLYEL 311
Cdd:NF033483 130 HRDIKPQNILITKDGRVKVTDFGIaralSST---TMTQTNSVlGTVHYLSPEQA-----RGGTvDARSDIYSLGIVLYEM 201

                 ....*..
gi 526479851 312 ATGRFPY 318
Cdd:NF033483 202 LTGRPPF 208
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
226-317 6.00e-12

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 67.67  E-value: 6.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  226 ALNHLKENlKIIHRDIKPSNILLDRSGN----IKLCDFGISGQLVDSIaktrDAGCRPYMAPERIDPSASRqgYDVRSDV 301
Cdd:NF033442  619 AVVHLEGQ-GVWHRDIKPDNIGIRPRPSrtlhLVLFDFSLAGAPADNI----EAGTPGYLDPFLGTGTRPR--YDDAAER 691
                          90
                  ....*....|....*.
gi 526479851  302 WSLGITLYELATGRFP 317
Cdd:NF033442  692 YAAAVTLYEMATGTLP 707
 
Name Accession Description Interval E-value
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
106-396 0e+00

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: 624.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd06616    1 YEFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd06616   81 WICMELMDISLDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEER 345
Cdd:cd06616  161 VDSIAKTRDAGCRPYMAPERIDPSASRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGDPPILSNSEER 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKIL 396
Cdd:cd06616  241 EFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVDVAAYVQKIL 291
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
111-397 6.06e-170

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: 476.53  E-value: 6.06e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06617    1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKYVYSVlDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd06617   81 VMDTSLDKFYKKVYDK-GLTIPEDILGKIAVSIVKALEYLHSKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSeerEFSPS 350
Cdd:cd06617  160 KTIDAGCKPYMAPERINPELNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQVVEEPSPQLPAE---KFSPE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKILD 397
Cdd:cd06617  237 FQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVASFVSLILG 283
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
111-383 8.49e-160

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: 450.26  E-value: 8.49e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSsDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKC-NSPYIVGFYGAFYSEGDISICME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMS-TSFDKFYKYVysvldDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06605   80 YMDgGSLDKILKEV-----GRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTrDAGCRPYMAPERIDPSasrqGYDVRSDVWSLGITLYELATGRFPYPKWN-----SVFDQLTQVVKGDPPQLSNSee 344
Cdd:cd06605  155 AKT-FVGTRSYMAPERISGG----KYTVKSDIWSLGLSLVELATGRFPYPPPNakpsmMIFELLSYIVDEPPPLLPSG-- 227
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 345 rEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEE 383
Cdd:cd06605  228 -KFSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRYEY 265
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
96-397 3.81e-141

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: 404.06  E-value: 3.81e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  96 GKLKISPEQhWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQF 175
Cdd:cd06618    1 GYLTIDGKK-YKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 176 YGALFREGDCWICMELMSTSFDKFYKYVYSVlddvIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIK 255
Cdd:cd06618   80 YGYFITDSDVFICMELMSTCLDKLLKRIQGP----IPEDILGKMTVSIVKALHYLKEKHGVIHRDVKPSNILLDESGNVK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 256 LCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGD 335
Cdd:cd06618  156 LCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPP-DNPKYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEE 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526479851 336 PPQLSNSEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKILD 397
Cdd:cd06618  235 PPSLPPNE--GFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYETAEVDVASWFQDVMA 294
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
111-398 6.07e-100

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: 299.07  E-value: 6.07e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICME 190
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVS-PYIVDFYGAFFIEGAVYMCME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKYvySVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06622   80 YMDAgSLDKLYAG--GVATEGIPEDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTrDAGCRPYMAPERI---DPSAsRQGYDVRSDVWSLGITLYELATGRFPYP--KWNSVFDQLTQVVKGDPPQLSNsee 344
Cdd:cd06622  158 AKT-NIGCQSYMAPERIksgGPNQ-NPTYTVQSDVWSLGLSILEMALGRYPYPpeTYANIFAQLSAIVDGDPPTLPS--- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 345 rEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKILDQ 398
Cdd:cd06622  233 -GYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVDMAEWVTGALKR 285
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
111-383 1.42e-91

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: 276.78  E-value: 1.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVmRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTL-RSCESPYVVKCYGAFYKEGEISIVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKYVysvldDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06623   80 YMDGgSLADLLKKV-----GKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDA-GCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPY--PKWNSVFDQLTQVVKGDPPQLsnsEERE 346
Cdd:cd06623  155 DQCNTFvGTVTYMSPERIQGES----YSYAADIWSLGLTLLECALGKFPFlpPGQPSFFELMQAICDGPPPSL---PAEE 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEE 383
Cdd:cd06623  228 FSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
111-396 8.93e-90

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: 273.93  E-value: 8.93e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVmrsSDC--PYIVQFYGALFREGDCWIC 188
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVL---HECnsPYIVGFYGAFYSDGEISIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMST-SFDKFYKYVYSvlddvIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:cd06615   78 MEHMDGgSLDQVLKKAGR-----IPENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRdAGCRPYMAPERIdpsasrQG--YDVRSDVWSLGITLYELATGRFPYPKWNS---------------------- 323
Cdd:cd06615  153 SMANSF-VGTRSYMSPERL------QGthYTVQSDIWSLGLSLVEMAIGRYPIPPPDAkeleamfgrpvsegeakeshrp 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 324 -------------VFDQLTQVVKGDPPQLsnsEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVAC 390
Cdd:cd06615  226 vsghppdsprpmaIFELLDYIVNEPPPKL---PSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAELEEVDFAG 302

                 ....*.
gi 526479851 391 YVCKIL 396
Cdd:cd06615  303 WVCSTM 308
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
107-384 1.40e-88

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: 270.08  E-value: 1.40e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 107 DFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFRE-GDC 185
Cdd:cd06620    1 DLKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILRELQI-LHECHSPYIVSFYGAFLNEnNNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMST-SFDKFYKyvysvLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd06620   80 IICMEYMDCgSLDKILK-----KKGPFPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRdAGCRPYMAPERIdpsasrQG--YDVRSDVWSLGITLYELATGRFPYPKWN----------SVFDQLTQVV 332
Cdd:cd06620  155 LINSIADTF-VGTSTYMSPERI------QGgkYSVKSDVWSLGLSIIELALGEFPFAGSNddddgyngpmGILDLLQRIV 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526479851 333 KGDPPQLSNSeeREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEER 384
Cdd:cd06620  228 NEPPPRLPKD--RIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRA 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
114-378 7.75e-84

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 256.69  E-value: 7.75e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKI-LKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   194 TS--FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK 271
Cdd:smart00220  81 GGdlFDLLKKRGR------LSEDEARFYLRQILSALEYLHSK-GIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   272 TRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEerEFSPSF 351
Cdd:smart00220 154 TTFVGTPEYMAPEVL----LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEW--DISPEA 227
                          250       260
                   ....*....|....*....|....*..
gi 526479851   352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEALQHPFF 254
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
116-396 6.74e-79

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: 245.02  E-value: 6.74e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDC--WICMELMS 193
Cdd:cd06621    6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILRELEI-NKSCASPYIVKYYGAFLDEQDSsiGIAMEYCE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 T-SFDKFYKYVYSvLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06621   85 GgSLDSIYKKVKK-KGGRIGEKVLGKIAESVLKGLSYLHSR-KIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSLAGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSV----FDQLTQVVKGDPPQLSNSEE--RE 346
Cdd:cd06621  163 F-TGTSYYMAPERI----QGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpIELLSYIVNMPNPELKDEPEngIK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKIL 396
Cdd:cd06621  238 WSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAKFVKQVW 287
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
112-378 1.09e-77

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: 240.95  E-value: 1.09e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMEL 191
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKI-NLESKEKKESILNEIAI-LKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MS-TSFDKfykyVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd05122   79 CSgGSLKD----LLKNTNKTLTEQQIAYVCKEVLKGLEYLHSH-GIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvFDQLTQVVKGDPPQLSNSEerEFSPS 350
Cdd:cd05122  154 RNTFVGTPYWMAPEVI----QGKPYGFKADIWSLGITAIEMAEGKPPYSELPP-MKALFLIATNGPPGLRNPK--KWSKE 226
                        250       260
                 ....*....|....*....|....*...
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd05122  227 FKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
111-398 7.04e-74

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: 232.08  E-value: 7.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSsDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06619    1 QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKC-DSPYIIGFYGAFFVENRISICTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKyvysvlddvIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06619   80 FMDGgSLDVYRK---------IPEHVLGRIAVAVVKGLTYL-WSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNS-----VFDQLTQ-VVKGDPPQLSNSe 343
Cdd:cd06619  150 AKTY-VGTNAYMAPERI----SGEQYGIHSDVWSLGISFMELALGRFPYPQIQKnqgslMPLQLLQcIVDEDPPVLPVG- 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 344 erEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVE-VACYVCKILDQ 398
Cdd:cd06619  224 --QFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYNDGNAEvVSMWVCRALEE 277
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
102-378 8.74e-70

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: 220.60  E-value: 8.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 102 PEQHWDFtaedlkdLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE-QKQLlmdldVVMRSSDCPYIVQFYGALF 180
Cdd:cd06612    1 PEEVFDI-------LEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEiIKEI-----SILKQCDSPYIVKYYGSYF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REGDCWICMElmstsfdkfYKYVYSVLD------DVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNI 254
Cdd:cd06612   69 KNTDLWIVME---------YCGAGSVSDimkitnKTLTEEEIAAILYQTLKGLEYLHSN-KKIHRDIKAGNILLNEEGQA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISGQLVDSIAKTRDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK 333
Cdd:cd06612  139 KLADFGVSGQLTDTMAKRNTVIGTPFwMAPEVI----QEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPM-RAIFMIPN 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 334 GDPPQLSNSEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06612  214 KPPPTLSDPE--KWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
111-396 1.14e-68

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: 219.93  E-value: 1.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQV-LHECNSPYIVGFYGAFYSDGEISICME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKYVYSvlddvIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06650   84 HMDGgSLDQVLKKAGR-----IPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIdpsasrQG--YDVRSDVWSLGITLYELATGRFPYPKWN------------------------- 322
Cdd:cd06650  159 ANSF-VGTRSYMSPERL------QGthYSVQSDIWSMGLSLVEMAVGRYPIPPPDakelelmfgcqvegdaaetpprprt 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 323 ----------------SVFDQLTQVVKGDPPQLSNSeerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAV 386
Cdd:cd06650  232 pgrplssygmdsrppmAIFELLDYIVNEPPPKLPSG---VFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEV 308
                        330
                 ....*....|
gi 526479851 387 EVACYVCKIL 396
Cdd:cd06650  309 DFAGWLCSTI 318
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
111-404 2.14e-64

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: 209.52  E-value: 2.14e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQV-LHECNSPYIVGFYGAFYSDGEISICME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKYVYSvlddvIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06649   84 HMDGgSLDQVLKEAKR-----IPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWN--------------------------- 322
Cdd:cd06649  159 ANSF-VGTRSYMSPERLQGTH----YSVQSDIWSMGLSLVELAIGRYPIPPPDakeleaifgrpvvdgeegephsisprp 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 323 ------------------SVFDQLTQVVKGDPPQLSNSeerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEER 384
Cdd:cd06649  234 rppgrpvsghgmdsrpamAIFELLDYIVNEPPPKLPNG---VFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKRSEVE 310
                        330       340
                 ....*....|....*....|.
gi 526479851 385 AVEVACYVCKILD-QMPATPS 404
Cdd:cd06649  311 EVDFAGWLCKTLRlNQPSTPT 331
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
116-378 2.37e-61

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: 199.07  E-value: 2.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRstVDEKE-----QKQLLMdldvvMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06613    5 IQRIGSGTYGDVYKARNIATGELAAVKVIK--LEPGDdfeiiQQEISM-----LKECRHPNIVAYFGSYLRRDKLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LM-STSFDKFYKYVysvldDVIPEEILGKITLATVKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06613   78 YCgGGSLQDIYQVT-----GPLSELQIAYVCRETLKGLAYLHSTGKI-HRDIKGANILLTEDGDVKLADFGVSAQLTATI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPY-MAPERIDpSASRQGYDVRSDVWSLGITLYELATGRFPYpkwnsvFD-----QLTQVVKG--DPPQLSN 341
Cdd:cd06613  152 AKRKSFIGTPYwMAPEVAA-VERKGGYDGKCDIWALGITAIELAELQPPM------FDlhpmrALFLIPKSnfDPPKLKD 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06613  225 KE--KWSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
111-378 5.76e-61

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: 198.62  E-value: 5.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDldvVMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdlEEAEDEIEDIQQEIQ---FLSQCDSPYITKYYGSFLKGSKLWII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSfdkfykyvySVLD----DVIPEEILGKITLATVKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd06609   78 MEYCGGG---------SVLDllkpGPLDETYIAFILREVLLGLEYLHSEGKI-HRDIKAANILLSEEGDVKLADFGVSGQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLsnsE 343
Cdd:cd06609  148 LTSTMSKRNTFVGTPFwMAPEVI----KQSGYDEKADIWSLGITAIELAKGEPPLSDLHPM-RVLFLIPKNNPPSL---E 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 344 EREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06609  220 GNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFI 254
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
115-378 2.64e-58

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: 191.75  E-value: 2.64e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGE-IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQkqLLMDLDVVMRSSDCPYIVQFYGALFREGDC------WI 187
Cdd:cd06608    9 ELVEvIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEE--IKLEINILRKFSNHPNIATFYGAFIKKDPPggddqlWL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSfdkfykyvySVLDDV---------IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd06608   87 VMEYCGGG---------SVTDLVkglrkkgkrLKEEWIAYILRETLRGLAYLHEN-KVIHRDIKGQNILLTEEAEVKLVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSIAKTRDAGCRPY-MAPERIDPSASR-QGYDVRSDVWSLGITLYELATGRFPYpkwnsvFDQ-----LTQV 331
Cdd:cd06608  157 FGVSAQLDSTLGRRNTFIGTPYwMAPEVIACDQQPdASYDARCDVWSLGITAIELADGKPPL------CDMhpmraLFKI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 332 VKGDPPQLSNSEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06608  231 PRNPPPTLKSPE--KWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
111-378 1.24e-56

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: 187.18  E-value: 1.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-----RSTVDE--KEQKqllmdldvVMRSSDCPYIVQFYGAlFREG 183
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIdlekcQTSMDElrKEIQ--------AMSQCNHPNVVSYYTS-FVVG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 184 DC-WICMELMST-SFDKFYKYVYSvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGI 261
Cdd:cd06610   72 DElWLVMPLLSGgSLLDIMKSSYP--RGGLDEAIIATVLKEVLKGLEYLHSN-GQIHRDVKAGNILLGEDGSVKIADFGV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 SGQLVDSIAKTRDA-----GCRPYMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDP 336
Cdd:cd06610  149 SASLATGGDRTRKVrktfvGTPCWMAPEVMEQV---RGYDFKADIWSFGITAIELATGAAPYSKYPPM-KVLMLTLQNDP 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 526479851 337 PQL-SNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06610  225 PSLeTGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
119-378 1.70e-56

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: 186.19  E-value: 1.70e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS---- 193
Cdd:cd06606    8 LGKGSFGSVYLALNLDTGELMAVKEVElSGDSEEELEALEREIRI-LSSLKHPNIVRYLGTERTENTLNIFLEYVPggsl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 ----TSFDKFykyvysvlddviPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06606   87 asllKKFGKL------------PEPVVRKYTRQILEGLEYLHSN-GIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCR---PYMAPEridpSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVK-GDPPQLSNSeer 345
Cdd:cd06606  154 TGEGTKSLRgtpYWMAPE----VIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKIGSsGEPPPIPEH--- 226
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 346 eFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06606  227 -LSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
113-378 1.32e-54

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: 181.25  E-value: 1.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 113 LKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTvdeKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLR---KQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 StsfdkfykyvYSVLDDVI-------PEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd06614   79 D----------GGSLTDIItqnpvrmNESQIAYVCREVLQGLEYL-HSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 vdsiakTRDAGCR------PY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQ 338
Cdd:cd06614  148 ------TKEKSKRnsvvgtPYwMAPEVI----KRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPL-RALFLITTKGIPP 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 339 LSNSEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06614  217 LKNPE--KWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
102-378 1.49e-54

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: 182.25  E-value: 1.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 102 PEQHWDFTaedlkdlGEIGRGAYGSVNKMVHKPSGQIMAVKRIRsTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFR 181
Cdd:cd06611    3 PNDIWEII-------GELGDGAFGKVYKAQHKETGLFAAAKIIQ-IESEEELEDFMVEIDI-LSECKHPNIVGLYEAYFY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 182 EGDCWICMELMST-SFDKfykyVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd06611   74 ENKLWILIEFCDGgALDS----IMLELERGLTEPQIRYVCRQMLEALNFLHSH-KVIHRDLKAGNILLTLDGDVKLADFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQLVDSIAKtRDA--GCRPYMAPERIDPSASR-QGYDVRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGDPP 337
Cdd:cd06611  149 VSAKNKSTLQK-RDTfiGTPYWMAPEVVACETFKdNPYDYKADIWSLGITLIELAQMEPPHHELN-PMRVLLKILKSEPP 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 526479851 338 QLSNSeeREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06611  227 TLDQP--SKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFV 265
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
119-376 2.19e-52

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: 174.38  E-value: 2.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST-SFD 197
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEI-LKKLNHPNIVKLYDVFETENFLYLVMEYCEGgSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYvysvLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGC 277
Cdd:cd00180   80 DLLKE----NKGPLSEEEALSILRQLLSALEYLHSN-GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 ---RPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELatgrfpypkwnsvfdqltqvvkgdppqlsnseerefsPSFINF 354
Cdd:cd00180  155 ttpPYYAPPELL----GGRYYGPKVDIWSLGVILYEL-------------------------------------EELKDL 193
                        250       260
                 ....*....|....*....|..
gi 526479851 355 VNLCLTKDESKRPKYKELLKHP 376
Cdd:cd00180  194 IRRMLQYDPKKRPSAKELLEHL 215
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
116-378 1.03e-51

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: 173.80  E-value: 1.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICME---- 190
Cdd:cd08215    5 IRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlSNMSEKEREEALNEVKL-LSKLKHPNIVKYYESFEENGKLCIVMEyadg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 --LMSTSFDKFYKYVYsvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS 268
Cdd:cd08215   84 gdLAQKIKKQKKKGQP------FPEEQILDWFVQICLALKYLHSR-KILHRDLKTQNIFLTKDGVVKLGDFGISKVLEST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 I--AKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY--PKWNSVFdqlTQVVKGDPPQLSNSee 344
Cdd:cd08215  157 TdlAKTV-VGTPYYLSPELC----ENKPYNYKSDIWALGCVLYELCTLKHPFeaNNLPALV---YKIVKGQYPPIPSQ-- 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 345 reFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08215  227 --YSSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
119-381 5.84e-48

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: 164.96  E-value: 5.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE----QK--QLLMDLdvvmRSSDCPYIVQFYGALFREGDCWICME-- 190
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsdiQKevALLSQL----KLGQPKNIIKYYGSYLKGPSLWIIMDyc 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 -------LMSTSfdkfykyvysvlddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISG 263
Cdd:cd06917   85 eggsirtLMRAG--------------PIAERYIAVIMREVLVALKFIHKD-GIIHRDIKAANILVTNTGNVKLCDFGVAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QLVDSIAKTRDAGCRPY-MAPERIdpsasRQG--YDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDPPQLs 340
Cdd:cd06917  150 SLNQNSSKRSTFVGTPYwMAPEVI-----TEGkyYDTKADIWSLGITTYEMATGNPPYSD-VDALRAVMLIPKSKPPRL- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 526479851 341 nsEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMY 381
Cdd:cd06917  223 --EGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQH 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
100-378 7.80e-48

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: 164.81  E-value: 7.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 100 ISPEQHWDFtaedlkdLGEIGRGAYGSVNKMVHKPSGqIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGAL 179
Cdd:cd06643    1 LNPEDFWEI-------VGELGDGAFGKVYKAQNKETG-ILAAAKVIDTKSEEELEDYMVEIDI-LASCDHPNIVKLLDAF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 FREGDCWICMELMST-SFDKfykyVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd06643   72 YYENNLWILIEFCAGgAVDA----VMLELERPLTEPQIRVVCKQTLEALVYLHEN-KIIHRDLKAGNILFTLDGDIKLAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSIAKtRDA--GCRPYMAPERIDPSASR-QGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGD 335
Cdd:cd06643  147 FGVSAKNTRTLQR-RDSfiGTPYWMAPEVVMCETSKdRPYDYKADVWSLGVTLIEMAQIEPPHHELNPM-RVLLKIAKSE 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 526479851 336 PPQLsnSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06643  225 PPTL--AQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
116-378 1.31e-47

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: 163.16  E-value: 1.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGE-IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGAlFREGD-CWICMELMS 193
Cdd:cd06627    4 LGDlIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGS-VKTKDsLYIILEYVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 T--------SFDKF-----YKYVYSVLddvipeeilgkitlatvKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd06627   83 NgslasiikKFGKFpeslvAVYIYQVL-----------------EGLAYLHEQ-GVIHRDIKGANILTTKDGLVKLADFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQLVDSIAKTRDAGCRPY-MAPERIDPSasrqGYDVRSDVWSLGITLYELATGRFPYpkwnsvFDQ-----LTQVVKG 334
Cdd:cd06627  145 VATKLNEVEKDENSVVGTPYwMAPEVIEMS----GVTTASDIWSVGCTVIELLTGNPPY------YDLqpmaaLFRIVQD 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 335 D-PPQLSNSeerefSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06627  215 DhPPLPENI-----SPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
111-378 2.74e-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: 159.72  E-value: 2.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI----RStvdEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCW 186
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkrgKS---EKELRNLRQEIEI-LRKLNHPNIIEMLDSFETKKEFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSfdkfykyVYSVLDD--VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG---- 260
Cdd:cd14002   77 VVTEYAQGE-------LFQILEDdgTLPEEEVRSIAKQLVSALHYLHSN-RIIHRDMKPQNILIGKGGVVKLCDFGfara 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 --ISGQLVDSIAKTrdagcrP-YMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDPP 337
Cdd:cd14002  149 msCNTLVLTSIKGT------PlYMAPELVQ----EQPYDHTADLWSLGCILYELFVGQPPFYT-NSIYQLVQMIVKDPVK 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 526479851 338 QLSNseereFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14002  218 WPSN-----MSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
119-379 1.54e-45

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: 157.64  E-value: 1.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRstvdekeqKQLLMDLDV---------VMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd14007    8 LGKGKFGNVYLAREKKSGFIVALKVIS--------KSQLQKSGLehqlrreieIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELmsTSFDKFYKYVYSVLddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd14007   80 EY--APNGELYKELKKQK--RFDEKEAAKYIYQLALALDYLHSK-NIIHRDIKPENILLGSNGELKLADFGWSVHAPSNR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDpPQLSNSeereFSP 349
Cdd:cd14007  155 RKTF-CGTLDYLPPEMV----EGKEYDYKVDIWSLGVLCYELLVGKPPFES-KSHQETYKRIQNVD-IKFPSS----VSP 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd14007  224 EAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
100-378 1.86e-45

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: 158.66  E-value: 1.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 100 ISPEQHWDFtaedlkdLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGAL 179
Cdd:cd06644    8 LDPNEVWEI-------IGELGDGAFGKVYKAKNKETGALAAAKVI-ETKSEEELEDYMVEIEI-LATCNHPYIVKLLGAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 FREGDCWICMELM-STSFDKfykyVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd06644   79 YWDGKLWIMIEFCpGGAVDA----IMLELDRGLTEPQIQVICRQMLEALQYL-HSMKIIHRDLKAGNVLLTLDGDIKLAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSIAKtRDA--GCRPYMAPERIDPSASRQG-YDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGD 335
Cdd:cd06644  154 FGVSAKNVKTLQR-RDSfiGTPYWMAPEVVMCETMKDTpYDYKADIWSLGITLIEMAQIEPPHHELNPM-RVLLKIAKSE 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 526479851 336 PPQLSNSEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06644  232 PPTLSQPS--KWSMEFRDFLKTALDKHPETRPSAAQLLEHPFV 272
Pkinase pfam00069
Protein kinase domain;
115-378 2.70e-45

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 155.86  E-value: 2.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:pfam00069   3 VLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKkEKIKKKKDKNILREIKI-LKKLNHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  194 -TSFDKFYKYvysvlDDVIPEEILGKITLATVKALNhlkenlkiihrdikpsnilldrsgniklcdfgiSGQLVDSIAKT 272
Cdd:pfam00069  82 gGSLFDLLSE-----KGAFSEREAKFIMKQILEGLE---------------------------------SGSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  273 RDagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKgDPPQLSNSEEREFSPSFI 352
Cdd:pfam00069 124 PW-----YMAPEVL----GGNPYGPKVDVWSLGCILYELLTGKPPFPGING--NEIYELII-DQPYAFPELPSNLSEEAK 191
                         250       260
                  ....*....|....*....|....*.
gi 526479851  353 NFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
116-377 4.91e-45

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: 156.14  E-value: 4.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14003    5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIdKSKLKEEIEEKIKREIEI-MKLLNHPNIIKLYEVIETENKIYLVMEYASG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 sfDKFYKYVYSvlDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV-DSIAKTR 273
Cdd:cd14003   84 --GELFDYIVN--NGRLSEDEARRFFQQLISAVDYC-HSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRgGSLLKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 dAGCRPYMAPERIdpsaSRQGYDVR-SDVWSLGITLYELATGRFPypkwnsvFDQ------LTQVVKGDPPqlsnsEERE 346
Cdd:cd14003  159 -CGTPAYAAPEVL----LGRKYDGPkADVWSLGVILYAMLTGYLP-------FDDdndsklFRKILKGKYP-----IPSH 221
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14003  222 LSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
116-368 4.92e-45

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: 156.59  E-value: 4.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMElms 193
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaeDEEFRERFLREARALARLSH-PNIVRVYDVGEDDGRPYIVME--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 tsfdkfykYVYSV-LDDVI------PEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgQLV 266
Cdd:cd14014   81 --------YVEGGsLADLLrergplPPREALRILAQIADALAAAHRA-GIVHRDIKPANILLTEDGRVKLTDFGIA-RAL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRD---AGCRPYMAPERidpsASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDPPQLSNSe 343
Cdd:cd14014  151 GDSGLTQTgsvLGTPAYMAPEQ----ARGGPVDPRSDIYSLGVVLYELLTGRPPFDG-DSPAAVLAKHLQEAPPPPSPL- 224
                        250       260
                 ....*....|....*....|....*
gi 526479851 344 EREFSPSFINFVNLCLTKDESKRPK 368
Cdd:cd14014  225 NPDVPPALDAIILRALAKDPEERPQ 249
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
119-377 7.87e-45

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: 155.75  E-value: 7.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTSf 196
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkEIIKRKEVEHTLNERNI-LERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 dKFYKYVYSVLddVIPEE----ILGKITLAtvkaLNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd05123   79 -ELFSHLSKEG--RFPEErarfYAAEIVLA----LEYL-HSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 R-DAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDPPQLSnseeREFSPSF 351
Cdd:cd05123  151 YtFCGTPEYLAPEVL----LGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENR--KEIYEKILKSPLKFP----EYVSPEA 220
                        250       260
                 ....*....|....*....|....*....
gi 526479851 352 INFVNLCLTKDESKRPKYK---ELLKHPF 377
Cdd:cd05123  221 KSLISGLLQKDPTKRLGSGgaeEIKAHPF 249
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
116-378 1.02e-44

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: 155.78  E-value: 1.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGalfREGD-----CWICM 189
Cdd:cd08217    5 LETIGKGSFGTVRKVRRKSDGKILVWKEIDyGKMSEKEKQQLVSEVNI-LRELKHPNIVRYYD---RIVDranttLYIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMST----SFDKFYKYvysvLDDVIPEEILGKITLATVKALN--HLKENL--KIIHRDIKPSNILLDRSGNIKLCDFGI 261
Cdd:cd08217   81 EYCEGgdlaQLIKKCKK----ENQYIPEEFIWKIFTQLLLALYecHNRSVGggKILHRDLKPANIFLDSDNNVKLGDFGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 SGQLVD--SIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNsvFDQLTQVVK-GDPPQ 338
Cdd:cd08217  157 ARVLSHdsSFAKTY-VGTPYYMSPELL----NEQSYDEKSDIWSLGCLIYELCALHPPFQAAN--QLELAKKIKeGKFPR 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 339 LSNseerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08217  230 IPS----RYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
116-384 1.43e-44

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: 155.99  E-value: 1.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd06642    9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEI-TVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdkfykyvySVLDDVIP----EEILGKITLATVKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFGISGQLVDS-IA 270
Cdd:cd06642   88 ---------SALDLLKPgpleETYIATILREILKGLDYLHSERKI-HRDIKAANVLLSEQGDVKLADFGVAGQLTDTqIK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLsnseEREFSPS 350
Cdd:cd06642  158 RNTFVGTPFWMAPEVIKQSA----YDFKADIWSLGITAIELAKGEPPNSDLHPM-RVLFLIPKNSPPTL----EGQHSKP 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPFILMYEER 384
Cdd:cd06642  229 FKEFVEACLNKDPRFRPTAKELLKHKFITRYTKK 262
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
119-374 1.66e-44

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: 154.62  E-value: 1.66e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS-TSfd 197
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPgGS-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyVYSVLDD---VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK-TR 273
Cdd:cd13999   77 -----LYDLLHKkkiPLSWSLRLKIALDIARGMNYLHSP-PIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKmTG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSeereFSPSFIN 353
Cdd:cd13999  151 VVGTPRWMAPEVL----RGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPD----CPPELSK 222
                        250       260
                 ....*....|....*....|.
gi 526479851 354 FVNLCLTKDESKRPKYKELLK 374
Cdd:cd13999  223 LIKRCWNEDPEKRPSFSEIVK 243
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
119-378 3.12e-44

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: 154.77  E-value: 3.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGA-LFREGDCwICMELMST-S 195
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEIRfQDNDPKTIKEIADEMKV-LEGLDHPNLVRYYGVeVHREEVY-IFMEYCQEgT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYKYvysvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDA 275
Cdd:cd06626   86 LEELLRH-----GRILDEAVIRVYTLQLLEGLAYLHEN-GIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTMAPG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 ------GCRPYMAPERIDpSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEerEFSP 349
Cdd:cd06626  160 evnslvGTPAYMAPEVIT-GNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMGHKPPIPDSL--QLSP 236
                        250       260
                 ....*....|....*....|....*....
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06626  237 EGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
111-398 1.61e-43

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: 153.30  E-value: 1.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06641    4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEI-TVLSQCDSPYVTKYYGSYLKDTKLWIIME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdkfykyvySVLDDVIP----EEILGKITLATVKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd06641   83 YLGGG---------SALDLLEPgpldETQIATILREILKGLDYLHSEKKI-HRDIKAANVLLSEHGEVKLADFGVAGQLT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DS-IAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLsnseER 345
Cdd:cd06641  153 DTqIKRN*FVGTPFWMAPEVIKQSA----YDSKADIWSLGITAIELARGEPPHSELHPM-KVLFLIPKNNPPTL----EG 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKYKELLKHPFILmyeeRAVEVACYVCKILDQ 398
Cdd:cd06641  224 NYSKPLKEFVEACLNKEPSFRPTAKELLKHKFIL----RNAKKTSYLTELIDR 272
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
102-378 3.59e-43

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: 152.47  E-value: 3.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 102 PEQHWDFTAEdlkdlgeIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQllMDLDVVMRSSDCPYIVQFYGALFR 181
Cdd:cd06638   16 PSDTWEIIET-------IGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIE--AEYNILKALSDHPNVVKFYGMYYK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 182 E----GD-CWICMELMSTSfdkfykyvySVLD---------DVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNIL 247
Cdd:cd06638   87 KdvknGDqLWLVLELCNGG---------SVTDlvkgflkrgERMEEPIIAYILHEALMGLQHLHVN-KTIHRDVKGNNIL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 248 LDRSGNIKLCDFGISGQLVDS-IAKTRDAGCRPYMAPERIdpsASRQ----GYDVRSDVWSLGITLYELATGRFPYPKWN 322
Cdd:cd06638  157 LTTEGGVKLVDFGVSAQLTSTrLRRNTSVGTPFWMAPEVI---ACEQqldsTYDARCDVWSLGITAIELGDGDPPLADLH 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 323 SVfDQLTQVVKGDPPQLSNSEerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06638  234 PM-RALFKIPRNPPPTLHQPE--LWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
102-378 4.59e-43

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: 152.45  E-value: 4.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 102 PEQHWDFtaedlkdLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQllMDLDVVMRSSDCPYIVQFYGALFR 181
Cdd:cd06639   20 PSDTWDI-------IETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIE--AEYNILRSLPNHPNVVKFYGMFYK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 182 E-----GDCWICMELMSTSfdKFYKYVYSVL--DDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNI 254
Cdd:cd06639   91 AdqyvgGQLWLVLELCNGG--SVTELVKGLLkcGQRLDEAMISYILYGALLGLQHLHNN-RIIHRDVKGNNILLTTEGGV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISGQLVDS-IAKTRDAGCRPYMAPERIdpsASRQ----GYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLT 329
Cdd:cd06639  168 KLVDFGVSAQLTSArLRRNTSVGTPFWMAPEVI---ACEQqydySYDARCDVWSLGITAIELADGDPPLFDMHPV-KALF 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 330 QVVKGDPPQLSNSEE--REFSpsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06639  244 KIPRNPPPTLLNPEKwcRGFS----HFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
111-379 1.10e-42

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: 150.29  E-value: 1.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06648    7 SDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKM--DLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdkfykyvysVLDDVIP-----EEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd06648   85 FLEGG----------ALTDIVThtrmnEEQIATVCRAVLKALSFL-HSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWN-SVFDQLTQVVKGDPPQLSNSe 343
Cdd:cd06648  154 SKEVPRRKSLVGTPYwMAPEVI----SRLPYGTEVDIWSLGIMVIEMVDGEPPY--FNePPLQAMKRIRDNEPPKLKNL- 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 344 eREFSPSFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd06648  227 -HKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
114-379 1.38e-42

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: 149.91  E-value: 1.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQK-QLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME-- 190
Cdd:cd06607    4 EDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEyc 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfDkfykyVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGiSGQLVD--- 267
Cdd:cd06607   84 LGSAS-D-----IVEVHKKPLQEVEIAAICHGALQGLAYL-HSHNRIHRDVKAGNILLTEPGTVKLADFG-SASLVCpan 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTrdagcrPY-MAPERIdpSASRQG-YDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSEer 345
Cdd:cd06607  156 SFVGT------PYwMAPEVI--LAMDEGqYDGKVDVWSLGITCIELAERKPPLFNMNAM-SALYHIAQNDSPTLSSGE-- 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 346 eFSPSFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd06607  225 -WSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
118-377 2.79e-42

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: 149.16  E-value: 2.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYgALFREGDCW-ICMELMS-- 193
Cdd:cd05117    7 VLGRGSFGVVRLAVHKKTGEEYAVKIIdKKKLKSEDEEMLRREIEI-LKRLDHPNIVKLY-EVFEDDKNLyLVMELCTgg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKY-VYSvlddvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL---DRSGNIKLCDFGISGQLVDSI 269
Cdd:cd05117   85 ELFDRIVKKgSFS-------EREAAKIMKQILSAVAYLHSQ-GIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 -AKTRdAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQL-TQVVKGDPpQLSNSEEREF 347
Cdd:cd05117  157 kLKTV-CGTPYYVAPEVLK----GKGYGKKCDIWSLGVILYILLCGYPPF--YGETEQELfEKILKGKY-SFDSPEWKNV 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 348 SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd05117  229 SEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
111-398 1.23e-41

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: 148.28  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06640    4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEI-TVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 ----------LMSTSFDKFYkyVYSVLDDVIpeeilgkitlatvKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd06640   83 ylgggsaldlLRAGPFDEFQ--IATMLKEIL-------------KGLDYLHSEKKI-HRDIKAANVLLSEQGDVKLADFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQLVDS-IAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQL 339
Cdd:cd06640  147 VAGQLTDTqIKRNTFVGTPFWMAPEVIQQSA----YDSKADIWSLGITAIELAKGEPPNSDMHPM-RVLFLIPKNNPPTL 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 340 SNseerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERavevACYVCKILDQ 398
Cdd:cd06640  222 VG----DFSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKK----TSYLTELIDR 272
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
119-378 5.97e-41

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: 145.62  E-value: 5.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDL--DVVMRSSDC-PYIVQFYGALFREGDCWICMELMST- 194
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLeqEIALLSKLRhPNIVQYYGTEREEDNLYIFLEYVPGg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYvYSVLDDVIpeeilgkITLATVKALNHLK--ENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06632   88 SIHKLLQR-YGAFEEPV-------IRLYTRQILSGLAylHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPYMAPERIDPSASrqGYDVRSDVWSLGITLYELATGRFPYpkwnSVFDQLTQVVK----GDPPQLSNSeereFS 348
Cdd:cd06632  160 SFKGSPYWMAPEVIMQKNS--GYGLAVDIWSLGCTVLEMATGKPPW----SQYEGVAAIFKignsGELPPIPDH----LS 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 349 PSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06632  230 PDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
112-376 1.28e-40

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: 144.86  E-value: 1.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMEL 191
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS--I 269
Cdd:cd08529   81 AENG--DLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSK-KILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTtnF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLtQVVKGDPPQLSNSeereFSP 349
Cdd:cd08529  158 AQTI-VGTPYYLSPELCEDKP----YNEKSDVWALGCVLYELCTGKHPFEAQNQGALIL-KIVRGKYPPISAS----YSQ 227
                        250       260
                 ....*....|....*....|....*..
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd08529  228 DLSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
119-378 1.42e-40

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: 145.54  E-value: 1.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLlmDLDVVMRSSDCPYIVQFYGALFREG------DCWICMELM 192
Cdd:cd06636   24 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKL--EINMLKKYSHHRNIATYYGAFIKKSppghddQLWLVMEFC 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06636  102 GAG--SVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAH-KVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERI----DPSASrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLsnsEEREF 347
Cdd:cd06636  179 NTFIGTPYwMAPEVIacdeNPDAT---YDYRSDIWSLGITAIEMAEGAPPLCDMHPM-RALFLIPRNPPPKL---KSKKW 251
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 348 SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06636  252 SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
116-367 1.72e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 150.16  E-value: 1.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMS 193
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELaaDPEARERFRREARALARLNH-PNIVRVYDVGEEDGRPYLVMEYVE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 -TSfdkfykyvysvLDDVI-------PEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISgQL 265
Cdd:COG0515   91 gES-----------LADLLrrrgplpPAEAL-RILAQLAEALAAA-HAAGIVHRDIKPANILLTPDGRVKLIDFGIA-RA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRD---AGCRPYMAPERidpsASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDPPQLSnS 342
Cdd:COG0515  157 LGGATLTQTgtvVGTPGYMAPEQ----ARGEPVDPRSDVYSLGVTLYELLTGRPPFDG-DSPAELLRAHLREPPPPPS-E 230
                        250       260
                 ....*....|....*....|....*
gi 526479851 343 EEREFSPSFINFVNLCLTKDESKRP 367
Cdd:COG0515  231 LRPDLPPALDAIVLRALAKDPEERY 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
119-378 6.80e-40

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: 143.08  E-value: 6.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI---------RSTVDEKEQKQLLMDLD---VVMRSSDCPYIVQFYGALfregDcw 186
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrrEGKNDRGKIKNALDDVRreiAIMKKLDHPNIVRLYEVI----D-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 icmelmstsfDKFYKYVYSVLD----------------DVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDR 250
Cdd:cd14008   75 ----------DPESDKLYLVLEyceggpvmeldsgdrvPPLPEETARKYFRDLVLGLEYLHEN-GIVHRDIKPENLLLTA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 251 SGNIKLCDFGISgQLV----DSIAKTrdAGCRPYMAPERIDPSASrqGYDVR-SDVWSLGITLYELATGRFPYpKWNSVF 325
Cdd:cd14008  144 DGTVKISDFGVS-EMFedgnDTLQKT--AGTPAFLAPELCDGDSK--TYSGKaADIWALGVTLYCLVFGRLPF-NGDNIL 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 326 DQLTQVVKG-DPPQLSnseeREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14008  218 ELYEAIQNQnDEFPIP----PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
91-379 1.17e-39

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 144.97  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  91 SIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCP 170
Cdd:PLN00034  54 SSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEI-LRDVNHP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 171 YIVQFYGALFREGDCWICMELMST-SFDKFYKYVYSVLDDViPEEILGKItlatvkALNHLKenlKIIHRDIKPSNILLD 249
Cdd:PLN00034 133 NVVKCHDMFDHNGEIQVLLEFMDGgSLEGTHIADEQFLADV-ARQILSGI------AYLHRR---HIVHRDIKPSNLLIN 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 250 RSGNIKLCDFGISGQLvdsiAKTRD-----AGCRPYMAPERIDPSASRQGYD-VRSDVWSLGITLYELATGRFPYP---- 319
Cdd:PLN00034 203 SAKNVKIADFGVSRIL----AQTMDpcnssVGTIAYMSPERINTDLNHGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrq 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 320 -KWNSVfdqLTQVVKGDPPQLSNSEEREFSpsfiNFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:PLN00034 279 gDWASL---MCAICMSQPPEAPATASREFR----HFISCCLQREPAKRWSAMQLLQHPFIL 332
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
119-378 3.99e-39

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: 140.95  E-value: 3.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDV---VMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECeiqLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTrda 275
Cdd:cd06625   88 SVKDEIKAYGALT----ENVTRKYTRQILEGLAYLHSN-MIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSST--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRP------YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRfpyPKWN------SVFDQLTQVVKgdpPQLSNse 343
Cdd:cd06625  160 GMKSvtgtpyWMSPEVI----NGEGYGRKADIWSVGCTVVEMLTTK---PPWAefepmaAIFKIATQPTN---PQLPP-- 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 344 erEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06625  228 --HVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
116-377 4.38e-38

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: 138.99  E-value: 4.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMElmsts 195
Cdd:cd07833    6 LGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFE----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdkfykYVYSVLDDVI-------PEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS 268
Cdd:cd07833   81 ------YVERTLLELLeaspgglPPDAVRSYIWQLLQAIAYCHSH-NIIHRDIKPENILVSESGVLKLCDFGFARALTAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAK--TRDAGCRPYMAPERI--DPSasrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--GD-PPQ--- 338
Cdd:cd07833  154 PASplTDYVATRWYRAPELLvgDTN-----YGKPVDVWAIGCIMAELLDGEPLFPGDSDI-DQLYLIQKclGPlPPShqe 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 339 --LSNS----------------EER---EFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07833  228 lfSSNPrfagvafpepsqpeslERRypgKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
118-375 5.38e-38

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: 138.06  E-value: 5.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNK-MVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS- 193
Cdd:cd00192    2 KLGEGAFGEVYKgKLKGGDGKTVdvAVKTLKEDASESERKDFLKEARV-MKKLGHPNVVRLLGVCTEEEPLYLVMEYMEg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYK----YVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-VDS 268
Cdd:cd00192   81 GDLLDFLRksrpVFPSPEPSTLSLKDLLSFAIQIAKGMEYL-ASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIyDDD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP--KWNSVFDQLTQVVKGDPPQLsnse 343
Cdd:cd00192  160 YYRKKTGGKLPirWMAPE----SLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPglSNEEVLEYLRKGYRLPKPEN---- 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 344 ereFSPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd00192  232 ---CPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
119-378 1.69e-37

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: 137.54  E-value: 1.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQkqLLMDLDVVMRSSDCPYIVQFYGALFREG------DCWICMELM 192
Cdd:cd06637   14 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEE--IKQEINMLKKYSHHRNIATYYGAFIKKNppgmddQLWLVMEFC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06637   92 GAG--SVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQH-KVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERI----DPSASrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLsnsEEREF 347
Cdd:cd06637  169 NTFIGTPYwMAPEVIacdeNPDAT---YDFKSDLWSLGITAIEMAEGAPPLCDMHPM-RALFLIPRNPAPRL---KSKKW 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 348 SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06637  242 SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
118-378 3.21e-37

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: 135.83  E-value: 3.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd06647   14 KIGQGASGTVYTAIDVATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvysVLDDVIPEEILGKITLATV-----KALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06647   90 --------SLTDVVTETCMDEGQIAAVcreclQALEFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSEerEFSPSF 351
Cdd:cd06647  161 STMVGTPYwMAPEVV----TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPL-RALYLIATNGTPELQNPE--KLSAIF 233
                        250       260
                 ....*....|....*....|....*..
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06647  234 RDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-378 7.96e-37

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: 134.67  E-value: 7.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQK----QLLMDLDVVMRSsdcPYIVQFYGALF--REGDCWI 187
Cdd:cd05118    2 EVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAAlreiKLLKHLNDVEGH---PNIVKLLDVFEhrGGNHLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFDKFYKYVYSVLddviPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLD-RSGNIKLCDFGiSGQLV 266
Cdd:cd05118   79 VFELMGMNLYELIKDYPRGL----PLDLIKSYLYQLLQALDFLHSN-GIIHRDLKPENILINlELGQLKLADFG-LARSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK--GDPPqlsnsee 344
Cdd:cd05118  153 TSPPYTPYVATRWYRAPEVLLGA---KPYGSSIDIWSLGCILAELLTGRPLFPG-DSEVDQLAKIVRllGTPE------- 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 345 refspsFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd05118  222 ------ALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
118-377 1.49e-36

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: 134.34  E-value: 1.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrstvdEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMEL-----M 192
Cdd:cd14010    7 EIGRGKHSVVYKGRRKGTIEFVAIKCV-----DKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYctggdL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STsfdkfykyvysVL--DDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd14010   82 ET-----------LLrqDGNLPESSVRKFGRDLVRGLHYIHS-KGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEILK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 -----------------KTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLT-QVV 332
Cdd:cd14010  150 elfgqfsdegnvnkvskKQAKRGTPYYMAPELF----QGGVHSFASDLWALGCVLYEMFTGKPPF--VAESFTELVeKIL 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 333 KGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14010  224 NEDPPPPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
117-378 1.72e-36

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: 134.10  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEI-GRGAYGSV-----NKmvhkpsGQIMAVKRIR-STVD----EKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd06631    6 GNVlGKGAYGTVycgltST------GQLIAVKQVElDTSDkekaEKEYEKLQEEVDL-LKTLKHVNIVGYLGTCLEDNVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMEL-----MSTSFDKFykyvysvldDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd06631   79 SIFMEFvpggsIASILARF---------GALEEPVFCRYTKQILEGVAYLHNN-NVIHRDIKGNNIMLMPNGVIKLIDFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 I------------SGQLVDSIAKTrdagcrPY-MAPERIDPSasrqGYDVRSDVWSLGITLYELATGRfpyPKWNSVfDQ 327
Cdd:cd06631  149 CakrlcinlssgsQSQLLKSMRGT------PYwMAPEVINET----GHGRKSDIWSIGCTVFEMATGK---PPWADM-NP 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 328 LTQVV-----KGDPPQLSNSeereFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06631  215 MAAIFaigsgRKPVPRLPDK----FSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
119-378 4.03e-36

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: 132.77  E-value: 4.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMsTSFD 197
Cdd:cd05578    8 IGKGSFGKVCIVQKKDTKKMFAMKYMnKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLL-LGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYvysvlddvipeEILGKITLATVK--------ALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd05578   87 LRYHL-----------QQKVKFSEETVKfyiceivlALDYLHSK-NIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYP-KWNSVFDQLTQVVKGDPPQLSNSeereFS 348
Cdd:cd05578  155 LATSTSGTKPYMAPEVFM----RAGYSFAVDWWSLGVTAYEMLRGKRPYEiHSRTSIEEIRAKFETASVLYPAG----WS 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 349 PSFINFVNLCLTKDESKRPKY-KELLKHPFI 378
Cdd:cd05578  227 EEAIDLINKLLERDPQKRLGDlSDLKNHPYF 257
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
118-378 6.81e-36

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: 133.31  E-value: 6.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd06656   26 KIGQGASGTVYTAIDIATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG-- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvysVLDDVIPEEILGKITLATV-----KALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06656  102 --------SLTDVVTETCMDEGQIAAVcreclQALDFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSEerEFSPSF 351
Cdd:cd06656  173 STMVGTPYwMAPEVV----TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPL-RALYLIATNGTPELQNPE--RLSAVF 245
                        250       260
                 ....*....|....*....|....*..
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06656  246 RDFLNRCLEMDVDRRGSAKELLQHPFL 272
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
113-374 3.54e-35

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 130.34  E-value: 3.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   113 LKDLGEIGRGAYGSVNK----MVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKgklkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARI-MRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   189 MELMST-SFDKFYKYvysvLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:smart00219  80 MEYMEGgDLLSYLRK----NRPKLSLSDLLSFALQIARGMEYL-ESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   268 SIAKTRDAGCRPY--MAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWnSVFDQLTQVVKGD-PPQLSNSe 343
Cdd:smart00219 155 DDYYRKRGGKLPIrwMAPE----SLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGM-SNEEVLEYLKNGYrLPQPPNC- 228
                          250       260       270
                   ....*....|....*....|....*....|.
gi 526479851   344 erefSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:smart00219 229 ----PPELYDLMLQCWAEDPEDRPTFSELVE 255
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
118-378 7.58e-35

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: 130.61  E-value: 7.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd06655   26 KIGQGASGTVFTAIDVATGQEVAIKQI--NLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGG-- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvysVLDDVIPEEILGKITLATV-----KALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06655  102 --------SLTDVVTETCMDEAQIAAVcreclQALEFLHAN-QVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSEerEFSPSF 351
Cdd:cd06655  173 STMVGTPYwMAPEVV----TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPL-RALYLIATNGTPELQNPE--KLSPIF 245
                        250       260
                 ....*....|....*....|....*..
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06655  246 RDFLNRCLEMDVEKRGSAKELLQHPFL 272
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
113-374 7.64e-35

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: 129.59  E-value: 7.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   113 LKDLGEIGRGAYGSVNK----MVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKgtlkGKGDGKEVEVAVKTLKEDASEQQIEEFLREARI-MRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   189 MELMST-SFDKFYKyvySVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISgQLVD 267
Cdd:smart00221  80 MEYMPGgDLLDYLR---KNRPKELSLSDLLSFALQIARGMEYL-ESKNFIHRDLAARNCLVGENLVVKISDFGLS-RDLY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   268 SIAKTRDAGCR-PY--MAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWnSVFDQLTQVVKGD-PPQLSNS 342
Cdd:smart00221 155 DDDYYKVKGGKlPIrwMAPE----SLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGM-SNAEVLEYLKKGYrLPKPPNC 229
                          250       260       270
                   ....*....|....*....|....*....|..
gi 526479851   343 eerefSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:smart00221 230 -----PPELYKLMLQCWAEDPEDRPTFSELVE 256
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
119-378 9.53e-35

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: 129.58  E-value: 9.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR----STVDEKEQKQLLMDLD---VVMRSSDCPYIVQFYGAlfregdcwicmEL 191
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVElpsvSAENKDRKKSMLDALQreiALLRELQHENIVQYLGS-----------SS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSFDKFYKYV-----YSVLDD--VIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd06628   77 DANHLNIFLEYVpggsvATLLNNygAFEESLVRNFVRQILKGLNYL-HNRGIIHRDIKGANILVDNKGGIKISDFGISKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCRP-------YMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWN---SVFdQLTQVVKG 334
Cdd:cd06628  156 LEANSLSTKNNGARPslqgsvfWMAPEVVKQTS----YTRKADIWSLGCLVVEMLTGTHPFPDCTqmqAIF-KIGENASP 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 335 DPPQLSNSEEREFspsfinfvnlcLTK----DESKRPKYKELLKHPFI 378
Cdd:cd06628  231 TIPSNISSEARDF-----------LEKtfeiDHNKRPTADELLKHPFL 267
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
118-378 1.42e-34

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: 129.84  E-value: 1.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd06654   27 KIGQGASGTVYTAMDVATGQEVAIRQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG-- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvysVLDDVIPEEILGKITLATV-----KALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06654  103 --------SLTDVVTETCMDEGQIAAVcreclQALEFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSEerEFSPSF 351
Cdd:cd06654  174 STMVGTPYwMAPEVV----TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPL-RALYLIATNGTPELQNPE--KLSAIF 246
                        250       260
                 ....*....|....*....|....*..
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06654  247 RDFLNRCLEMDVEKRGSAKELLQHQFL 273
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
118-375 2.37e-34

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: 128.00  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  118 EIGRGAYGSVN----KMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:pfam07714   6 KLGEGAFGEVYkgtlKGEGENTKIKVAVKTLKEGADEEEREDFLEEASI-MKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  194 T-SFDKFYKyvysVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:pfam07714  85 GgDLLDFLR----KHKRKLTLKDLLSMALQIAKGMEYL-ESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  273 RDAGCR---PYMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWnSVFDQLTQVVKG---DPPQLSnseer 345
Cdd:pfam07714 160 KRGGGKlpiKWMAPE----SLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGM-SNEEVLEFLEDGyrlPQPENC----- 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 526479851  346 efSPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:pfam07714 230 --PDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
119-377 5.86e-34

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: 127.33  E-value: 5.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSdCPYIVQFYGALFREGDCWICMELMSTSf 196
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIkkRDMIRKNQVDSVLAERNILSQAQ-NPFVVKLYYSFQGKKNLYLVMEYLPGG- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DkfykyVYSVLDDV--IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS------------ 262
Cdd:cd05579   79 D-----LYSLLENVgaLDEDVARIYIAEIVLALEYLHSH-GIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrrqikls 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 ---GQLVDSIAKTRDAGCRP-YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGrfpYPKWNS-----VFDqltQVVK 333
Cdd:cd05579  153 iqkKSNGAPEKEDRRIVGTPdYLAPEIL----LGQGHGKTVDWWSLGVILYEFLVG---IPPFHAetpeeIFQ---NILN 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 526479851 334 GD--PPqlsnsEEREFSPSFINFVNLCLTKDESKRPKYK---ELLKHPF 377
Cdd:cd05579  223 GKieWP-----EDPEVSDEAKDLISKLLTPDPEKRLGAKgieEIKNHPF 266
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
112-376 1.10e-33

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: 126.35  E-value: 1.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNlGSLSQKEREDSVNEIRL-LASVNHPNIIRYKEAFLDGNRLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfDKFYKYV-YSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd08530   80 YAPFG-DLSKLISkRKKKRRLFPEDDIWRIFIQMLRGLKALHDQ-KILHRDLKSANILLSAGDLVKIGDLGISKVLKKNL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPEridpSASRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKGDPPQLSNSeereFSP 349
Cdd:cd08530  158 AKTQ-IGTPLYAAPE----VWKGRPYDYKSDIWSLGCLLYEMATFRPPF-EARTMQELRYKVCRGKFPPIPPV----YSQ 227
                        250       260
                 ....*....|....*....|....*..
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd08530  228 DLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
111-378 1.86e-33

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: 126.31  E-value: 1.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRstVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06645   11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIK--LEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKyvysvLDDVIPEEILGKITLATVKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06645   89 FCGGgSLQDIYH-----VTGPLSESQIAYVSRETLQGLYYLHSKGKM-HRDIKGANILLTDNGHVKLADFGVSAQITATI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPY-MAPErIDPSASRQGYDVRSDVWSLGITLYELATGRFPypkwnsVFD-----QLTQVVKGD--PPQLsn 341
Cdd:cd06645  163 AKRKSFIGTPYwMAPE-VAAVERKGGYNQLCDIWAVGITAIELAELQPP------MFDlhpmrALFLMTKSNfqPPKL-- 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06645  234 KDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
113-379 2.43e-33

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: 126.64  E-value: 2.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 113 LKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd06659   23 LENYVKIGEGSTGVVCIAREKHSGRQVAVKMM--DLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSfdkfykyvysVLDDVIPEEILGKITLATVK-----ALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:cd06659  101 QGG----------ALTDIVSQTRLNEEQIATVCeavlqALAYLHSQ-GVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDPPQLSNSEerE 346
Cdd:cd06659  170 DVPKRKSLVGTPYwMAPEVI----SRCPYGTEVDIWSLGIMVIEMVDGEPPYFS-DSPVQAMKRLRDSPPPKLKNSH--K 242
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd06659  243 ASPVLRDFLERMLVRDPQERATAQELLDHPFLL 275
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
119-378 5.27e-33

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: 124.80  E-value: 5.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI---RSTVDEKEQKQLLMdLDVV------MRSSDCPYIVQFYGalFREGDcwicm 189
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVelpKTSSDRADSRQKTV-VDALkseidtLKDLDHPNIVQYLG--FEETE----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 elmsTSFDKFYKYVY-----SVLDDVIP--EEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd06629   81 ----DYFSIFLEYVPggsigSCLRKYGKfeEDLVRFFTRQILDGLAYL-HSKGILHRDLKADNILVDLEGICKISDFGIS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQ---LVDSIAKTRDAGCRPYMAPERIDpsASRQGYDVRSDVWSLGITLYELATGRFPYPKwnsvfDQLTQVV------K 333
Cdd:cd06629  156 KKsddIYGNNGATSMQGSVFWMAPEVIH--SQGQGYSAKVDIWSLGCVVLEMLAGRRPWSD-----DEAIAAMfklgnkR 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 334 GDPPQlsnSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06629  229 SAPPV---PEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
119-376 1.76e-31

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: 120.18  E-value: 1.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTV-DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMST-SF 196
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFrGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENgSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYvySVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLvDSIAKTRDAG 276
Cdd:cd13997   88 QDALEE--LSPISKLSEAEVWDLLLQVALGLAFIHSK-GIVHLDIKPDNIFISNKGTCKIGDFGLATRL-ETSGDVEEGD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 277 CRpYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGrFPYPKWNSVFDQLTQVVKGDPPQLSNSEErefspsFINFVN 356
Cdd:cd13997  164 SR-YLAPELL---NENYTHLPKADIFSLGVTVYEAATG-EPLPRNGQQWQQLRQGKLPLPPGLVLSQE------LTRLLK 232
                        250       260
                 ....*....|....*....|
gi 526479851 357 LCLTKDESKRPKYKELLKHP 376
Cdd:cd13997  233 VMLDPDPTRRPTADQLLAHD 252
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
116-376 1.82e-31

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: 120.11  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV-DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14050    6 LSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFrGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTELCDT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKfykyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD 274
Cdd:cd14050   86 SLQQ-----YCEETHSLPESEVWNILLDLLKGLKHLHDH-GLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIDPSasrqgYDVRSDVWSLGITLYELATGrFPYPKWNSVFDQLTQvvkGDPPQlsnseerEF----SPS 350
Cdd:cd14050  160 EGDPRYMAPELLQGS-----FTKAADIFSLGITILELACN-LELPSGGDGWHQLRQ---GYLPE-------EFtaglSPE 223
                        250       260
                 ....*....|....*....|....*.
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14050  224 LRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
115-378 2.28e-31

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: 121.68  E-value: 2.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQK-QLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd06633   25 DLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDDVipeEIlGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgqlvdSIAKTR 273
Cdd:cd06633  105 GSASDLLEVHKKPLQEV---EI-AAITHGALQGLAYLHSH-NMIHRDIKAGNILLTEPGQVKLADFGSA-----SIASPA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DA--GCRPYMAPERIDPSASRQgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLsnsEEREFSPSF 351
Cdd:cd06633  175 NSfvGTPYWMAPEVILAMDEGQ-YDGKVDIWSLGITCIELAERKPPLFNMNAM-SALYHIAQNDSPTL---QSNEWTDSF 249
                        250       260
                 ....*....|....*....|....*..
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06633  250 RGFVDYCLQKIPQERPSSAELLRHDFV 276
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
116-378 2.91e-31

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: 2.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCP---YIVQFYGA-LFREGDCwICMEL 191
Cdd:cd14133    4 LEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKAdkyHIVRLKDVfYFKNHLC-IVFEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MST---SFDKFYKYVYSVLddvipeEILGKITLATVKALNHLKEnLKIIHRDIKPSNILL---DRSgNIKLCDFGISGQL 265
Cdd:cd14133   83 LSQnlyEFLKQNKFQYLSL------PRIRKIAQQILEALVFLHS-LGLIHCDLKPENILLasySRC-QIKIIDFGSSCFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIakTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK--GDPPQ--LSN 341
Cdd:cd14133  155 TQRL--YSYIQSRYYRAPEVILGLP----YDEKIDMWSLGCILAELYTGEPLFPG-ASEVDQLARIIGtiGIPPAhmLDQ 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEEREfsPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14133  228 GKADD--ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
118-367 6.72e-31

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: 118.91  E-value: 6.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMEL---- 191
Cdd:cd08224    7 KIGKGQFSVVYRARCLLDGRLVALKKVQifEMMDAKARQDCLKEIDL-LQQLNHPNIIKYLASFIENNELNIVLELadag 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 ----MSTSFDKFYKYvysvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVd 267
Cdd:cd08224   86 dlsrLIKHFKKQKRL--------IPERTIWKYFVQLCSALEHMHSK-RIMHRDIKPANVFITANGVVKLGDLGLGRFFS- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 siAKTRDA----GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN-SVFDQLTQVVKGDPPQLSNS 342
Cdd:cd08224  156 --SKTTAAhslvGTPYYMSPERI----REQGYDFKSDIWSLGCLLYEMAALQSPFYGEKmNLYSLCKKIEKCEYPPLPAD 229
                        250       260
                 ....*....|....*....|....*
gi 526479851 343 eerEFSPSFINFVNLCLTKDESKRP 367
Cdd:cd08224  230 ---LYSQELRDLVAACIQPDPEKRP 251
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
116-377 3.11e-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: 117.32  E-value: 3.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKmVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGA--LFREGDCWICMELM 192
Cdd:cd14131    6 LKQLGKGGSSKVYK-VLNPKKKIYALKRVDlEGADEQTLQSYKNEIELLKKLKGSDRIIQLYDYevTDEDDYLYMVMECG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSFDKFYKyvySVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLdRSGNIKLCDFGISGQL-VDSIAK 271
Cdd:cd14131   85 EIDLATILK---KKRPKPIDPNFIRYYWKQMLEAVHTIHEE-GIVHSDLKPANFLL-VKGRLKLIDFGIAKAIqNDTTSI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDA--GCRPYMAPERI-DPSASRQGYDV-----RSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVkgDP------P 337
Cdd:cd14131  160 VRDSqvGTLNYMSPEAIkDTSASGEGKPKskigrPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAII--DPnheiefP 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 338 QLSNseerefsPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14131  238 DIPN-------PDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
111-378 3.47e-30

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: 117.44  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRstVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06646    9 HDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIK--LEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMST-SFDKFYKyvysvLDDVIPEEILGKITLATVKALNHLKENLKIiHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd06646   87 YCGGgSLQDIYH-----VTGPLSELQIAYVCRETLQGLAYLHSKGKM-HRDIKGANILLTDNGDVKLADFGVAAKITATI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPY-MAPErIDPSASRQGYDVRSDVWSLGITLYELATGRFPypkwnsVFDQ-------LTQVVKGDPPQLsn 341
Cdd:cd06646  161 AKRKSFIGTPYwMAPE-VAAVEKNGGYNQLCDIWAVGITAIELAELQPP------MFDLhpmralfLMSKSNFQPPKL-- 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06646  232 KDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
118-378 4.78e-30

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: 117.43  E-value: 4.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd06657   27 KIGEGSTGIVCIATVKSSGKLVAVKKM--DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG-- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvysVLDDVIP-----EEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd06657  103 --------ALTDIVThtrmnEEQIAAVCLAVLKALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGD-PPQLSNSEerEFSPS 350
Cdd:cd06657  174 KSLVGTPYwMAPELI----SRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPLKAMKMIRDNlPPKLKNLH--KVSPS 245
                        250       260
                 ....*....|....*....|....*...
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06657  246 LKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
91-379 1.07e-29

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: 117.07  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  91 SIESSGKLKiSPEQHWDFTAED----LKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQK--QLLMDLDVVM 164
Cdd:cd06635    2 STSRAGSLK-DPDIAELFFKEDpeklFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqDIIKEVKFLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 165 RSSDcPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYSVLDDVipeEIlGKITLATVKALNHLKENlKIIHRDIKPS 244
Cdd:cd06635   81 RIKH-PNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEI---EI-AAITHGALQGLAYLHSH-NMIHRDIKAG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 245 NILLDRSGNIKLCDFGISgqlvdSIAKTRDA--GCRPYMAPERIDPSASRQgYDVRSDVWSLGITLYELATGRFPYPKWN 322
Cdd:cd06635  155 NILLTEPGQVKLADFGSA-----SIASPANSfvGTPYWMAPEVILAMDEGQ-YDGKVDVWSLGITCIELAERKPPLFNMN 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 323 SVfDQLTQVVKGDPPQLSNSeerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd06635  229 AM-SALYHIAQNESPTLQSN---EWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVL 281
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
116-377 1.20e-29

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: 115.66  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQ-KQLLMDLDVVMRSSDCPYIVQFYGAlFREGDcwicmelms 193
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKkSDMIAKNQvTNVKAERAIMMIQGESPYVAKLYYS-FQSKD--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 tsfdkfykYVYSVLD--------------DVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDF 259
Cdd:cd05611   71 --------YLYLVMEylnggdcasliktlGGLPEDWAKQYIAEVVLGVEDLHQR-GIIHRDIKPENLLIDQTGHLKLTDF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQLVDSIAKTRDAGCRPYMAPERIDPsasrQGYDVRSDVWSLGITLYELATGrfpYPKWNS-----VFDQLTQVVKG 334
Cdd:cd05611  142 GLSRNGLEKRHNKKFVGTPDYLAPETILG----VGDDKMSDWWSLGCVIFEFLFG---YPPFHAetpdaVFDNILSRRIN 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 335 DPpqlsnSEEREF-SPSFINFVNLCLTKDESKR---PKYKELLKHPF 377
Cdd:cd05611  215 WP-----EEVKEFcSPEAVDLINRLLCMDPAKRlgaNGYQEIKSHPF 256
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
111-378 1.35e-29

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: 116.29  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd06658   22 EYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKM--DLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVME 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdkfykyvysVLDDVIP-----EEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd06658  100 FLEGG----------ALTDIVThtrmnEEQIATVCLSVLRALSYL-HNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGD-PPQLSNSE 343
Cdd:cd06658  169 SKEVPKRKSLVGTPYwMAPEVI----SRLPYGTEVDIWSLGIMVIEMIDGEPPY--FNEPPLQAMRRIRDNlPPRVKDSH 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 344 erEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06658  243 --KVSSVLRGFLDLMLVREPSQRATAQELLQHPFL 275
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
119-377 3.90e-29

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: 113.86  E-value: 3.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDvVMRSSDCPYIVQFYGALFREGDCWICMElmstsfd 197
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEIsRKKLNKKLQENLESEIA-ILKSIKHPNIVRLYDVQKTEDFIYLVLE------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvYSVLDDV---------IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCDFGISGQL 265
Cdd:cd14009   73 ------YCAGGDLsqyirkrgrLPEAVARHFMQQLASGLKFLRSK-NIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 V-DSIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfdQLTQVVKGDPPQLSNSEE 344
Cdd:cd14009  146 QpASMAETL-CGSPLYMAPEIL----QFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHV--QLLRNIERSDAVIPFPIA 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 345 REFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14009  219 AQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
119-377 5.79e-29

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: 115.84  E-value: 5.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME------L 191
Cdd:cd05573    9 IGRGAFGEVWLVRDKDTGQVYAMKILRkSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEympggdL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSFDKfykyvysvldDVIPEEI----LGKITLAtvkaLNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-- 265
Cdd:cd05573   89 MNLLIKY----------DVFPEETarfyIAELVLA----LDSL-HKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnk 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 ------------VDSIAKTRDAGCRP----------------YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFP 317
Cdd:cd05573  154 sgdresylndsvNTLFQDNVLARRRPhkqrrvraysavgtpdYIAPEVL----RGTGYGPECDWWSLGVILYEMLYGFPP 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 318 YpkwnsvFDQLTQVVKGdppQLSNSEE-------REFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd05573  230 F------YSDSLVETYS---KIMNWKEslvfpddPDVSPEAIDLIRRLLCDPEDRLGSAEEIKAHPF 287
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
119-318 3.66e-28

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: 112.88  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV---NKMVHKPSGQIMAVK-------RIRSTVDEKEQKQLLMDLDvvmrssdCPYIVQFYGALFREGDCWIC 188
Cdd:cd05582    3 LGQGSFGKVflvRKITGPDAGTLYAMKvlkkatlKVRDRVRTKMERDILADVN-------HPFIVKLHYAFQTEGKLYLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTS--FDKFYKYVYSVLDDVipeeilgKITLATVK-ALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd05582   76 LDFLRGGdlFTRLSKEVMFTEEDV-------KFYLAELAlALDHL-HSLGIIYRDLKPENILLDEDGHIKLTDFGLSKES 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 266 VDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05582  148 IDHEKKAYSfCGTVEYMAPEVV----NRRGHTQSADWWSFGVLMFEMLTGSLPF 197
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
111-377 6.54e-28

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: 111.36  E-value: 6.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMStsfdkfykyvYSVLDDV------IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd07846   81 FVD----------HTVLDDLekypngLDESRVRKYLFQILRGIDFCHSH-NIIHRDIKPENILVSQSGVVKLCDFGFART 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDS-IAKTRDAGCRPYMAPERI--DPSasrqgYDVRSDVWSLGITLYELATGRfPYPKWNSVFDQLTQVVK-------- 333
Cdd:cd07846  150 LAAPgEVYTDYVATRWYRAPELLvgDTK-----YGKAVDVWAVGCLVTEMLTGE-PLFPGDSDIDQLYHIIKclgnlipr 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526479851 334 ------GDP-------PQLSNSE--EREF---SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07846  224 hqelfqKNPlfagvrlPEVKEVEplERRYpklSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
116-378 7.31e-28

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: 111.57  E-value: 7.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIrstvdEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14091    5 KEEIGKGSYSVCKRCIHKATGKEYAVKII-----DKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL-DRSGN---IKLCDFGISGQLvdsi 269
Cdd:cd14091   80 elLDRILRQKF------FSEREASAVMKTLTKTVEYLHSQ-GVVHRDLKPSNILYaDESGDpesLRICDFGFAKQL---- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 akTRDAG-----CRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPkwNSVFDQ----LTQVVKGDPPq 338
Cdd:cd14091  149 --RAENGllmtpCYTanFVAPEVL----KKQGYDAACDIWSLGVLLYTMLAGYTPFA--SGPNDTpeviLARIGSGKID- 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 339 LSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14091  220 LSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWI 259
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
117-378 8.24e-28

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: 110.90  E-value: 8.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQ-KQLLMDLDVVMRSSDCPYIVQFY------------------G 177
Cdd:cd14106   14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCrNEILHEIAVLELCKDCPRVVNLHevyetrselililelaagG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 178 ALFREGDCwicmelmstsfdkfykyvysvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRS---GNI 254
Cdd:cd14106   94 ELQTLLDE----------------------EECLTEADVRRLMRQILEGVQYLHER-NIVHLDLKPQNILLTSEfplGDI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISgQLVDSIAKTRD-AGCRPYMAPERI--DPsasrqgYDVRSDVWSLGITLYELATGRFPY--PKWNSVFDQLT 329
Cdd:cd14106  151 KLCDFGIS-RVIGEGEEIREiLGTPDYVAPEILsyEP------ISLATDMWSIGVLTYVLLTGHSPFggDDKQETFLNIS 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 330 QVvkgdppQLSNSEE--REFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14106  224 QC------NLDFPEElfKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
119-373 1.04e-27

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: 110.24  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRS-TVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST-SF 196
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSsPNCIEERKALLKEAEK-MERARHSYVLPLLGVCVERRSLGLVMEYMENgSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVlddvIPEEILGKITLATVKALNHLKENLK-IIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTR-- 273
Cdd:cd13978   80 KSLLEREIQD----VPWSLRFRIIHEIALGMNFLHNMDPpLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRrr 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 ----DAGCRPYMAPERIDPSASRqgYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQL---SNSEERE 346
Cdd:cd13978  156 gtenLGGTPIYMAPEAFDDFNKK--PTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPSLddiGRLKQIE 233
                        250       260
                 ....*....|....*....|....*..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELL 373
Cdd:cd13978  234 NVQELISLMIRCWDGNPDARPTFLECL 260
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
119-318 1.10e-27

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: 110.01  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYgALFRegdcwicmelmstsf 196
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKkrHIVQTRQQEHIFSEKEI-LEECNSPFIVKLY-RTFK--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKfyKYVYSVLDDVIPEEI------LGKITLAT--------VKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd05572   64 DK--KYLYMLMEYCLGGELwtilrdRGLFDEYTarfytacvVLAFEYL-HSRGIIYRDLKPENLLLDSNGYVKLVDFGFA 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 263 GQLvDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05572  141 KKL-GSGRKTWTfCGTPEYVAPEII----LNKGYDFSVDYWSLGILLYELLTGRPPF 192
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
119-378 1.19e-27

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: 110.09  E-value: 1.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVnKMVHK---PSGQIMAVKRIRSTVDEKEQKQLLMDLD---VVMRSSDCPYIVQFYGALFREGDCWIC-MEL 191
Cdd:cd13994    1 IGKGATSVV-RIVTKknpRSGVLYAVKEYRRRDDESKRKDYVKRLTseyIISSKLHHPNIVKVLDLCQDLHGKWCLvMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MsTSFDKFYkyvYSVLDDVIPEE----ILGKITlatvKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:cd13994   80 C-PGGDLFT---LIEKADSLSLEekdcFFKQIL----RGVAYLHSH-GIAHRDLKPENILLDEDGVLKLTDFGTAEVFGM 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 -----SIAKTRDAGCRPYMAPERIdpsaSRQGYDVRS-DVWSLGITLYELATGRFPY--PKWNSVFDQLTQvVKGDPPQL 339
Cdd:cd13994  151 paekeSPMSAGLCGSEPYMAPEVF----TSGSYDGRAvDVWSCGIVLFALFTGRFPWrsAKKSDSAYKAYE-KSGDFTNG 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 340 SNSEEREFSPSfiNFVNLC---LTKDESKRPKYKELLKHPFI 378
Cdd:cd13994  226 PYEPIENLLPS--ECRRLIyrmLHPDPEKRITIDEALNDPWV 265
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
118-378 1.36e-27

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: 111.23  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGR----GAYGSVNKmvHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWI------ 187
Cdd:cd08216    5 EIGKcfkgGGVVHLAK--HKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVvtplma 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 ---CMELMSTSFDkfykyvysvldDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd08216   83 ygsCRDLLKTHFP-----------EGLPELAIAFILRDVLNALEYI-HSKGYIHRSVKASHILISGDGKVVLSGLRYAYS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTR--------DAGCRPYMAPERIDPSAsrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFdQLTQVVKGDP 336
Cdd:cd08216  151 MVKHGKRQRvvhdfpksSEKNLPWLSPEVLQQNL--LGYNEKSDIYSVGITACELANGVVPFSDMPATQ-MLLEKVRGTT 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526479851 337 PQL-------------SNSEE-----------------REFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08216  228 PQLldcstypleedsmSQSEDsstehpnnrdtrdipyqRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFF 299
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
119-377 2.22e-27

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: 109.41  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV---NKMVHKPSGQIMAVKRIRSTVDEKEQKQL---LMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd05583    2 LGTGAYGKVflvRKVGGHDAGKLYAMKVLKKATIVQKAKTAehtMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STS--FDKFYKYVYSVLDDVipEEILGKITLAtvkaLNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV-DSI 269
Cdd:cd05583   82 NGGelFTHLYQREHFTESEV--RIYIGEIVLA----LEHLHK-LGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpGEN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRD-AGCRPYMAPERIdpSASRQGYDVRSDVWSLGITLYELATGRFPYP---KWNSVFDQLTQVVKGDPPQlsnseER 345
Cdd:cd05583  155 DRAYSfCGTIEYMAPEVV--RGGSDGHDKAVDWWSLGVLTYELLTGASPFTvdgERNSQSEISKRILKSHPPI-----PK 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKYK-----ELLKHPF 377
Cdd:cd05583  228 TFSAEAKDFILKLLEKDPKKRLGAGprgahEIKEHPF 264
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
107-377 2.42e-27

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: 110.86  E-value: 2.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 107 DFtaeDLKDLgeIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd05601    2 DF---EVKNV--IGRGHFGEVQVVKEKATGDIYAMKVLKkSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICME------LMSTsfdkFYKYvysvlDDVIPEEiLGKITLA-TVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd05601   77 YLVMEyhpggdLLSL----LSRY-----DDIFEES-MARFYLAeLVLAIHSLHS-MGYVHRDIKPENILIDRTGHIKLAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLvdSIAKTRDA----GCRPYMAPE---RIDpSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSV--FDQLT 329
Cdd:cd05601  146 FGSAAKL--SSDKTVTSkmpvGTPDYIAPEvltSMN-GGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIktYSNIM 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 330 QVVKgdppQLSNSEEREFSPSFINFVNLCLTkDESKRPKYKELLKHPF 377
Cdd:cd05601  223 NFKK----FLKFPEDPKVSESAVDLIKGLLT-DAKERLGYEGLCCHPF 265
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
117-376 3.04e-27

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: 108.86  E-value: 3.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQ--KQLLMDLDVVM----RSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd14005    6 DLLGKGGFGTVYSGVRIRDGLPVAVKFVpKSRVTEWAMinGPVPVPLEIALllkaSKPGVPGVIRLLDWYERPDGFLLIM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSFDKF-YKYVYsvldDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLD-RSGNIKLCDFGiSGQLVD 267
Cdd:cd14005   86 ERPEPCQDLFdFITER----GALSENLARIIFRQVVEAVRHCHQR-GVLHRDIKDENLLINlRTGEVKLIDFG-CGALLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRPYMAPERIdpsaSRQGYDVRS-DVWSLGITLYELATGRFPYpkwnsVFDQltQVVKGdppqlSNSEERE 346
Cdd:cd14005  160 DSVYTDFDGTRVYSPPEWI----RHGRYHGRPaTVWSLGILLYDMLCGDIPF-----ENDE--QILRG-----NVLFRPR 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14005  224 LSKECCDLISRCLQFDPSKRPSLEQILSHP 253
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
119-378 3.24e-27

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: 108.96  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDV---VMRSSDCPYIVQFYGAL--FREGDCWICMELMS 193
Cdd:cd06653   10 LGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALECeiqLLKNLRHDRIVQYYGCLrdPEEKKLSIFVEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLkIIHRDIKPSNILLDRSGNIKLCDFG---------ISGQ 264
Cdd:cd06653   90 GGSVKDQLKAYGALT----ENVTRRYTRQILQGVSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGaskriqticMSGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTrdagcrPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN---SVFDQLTQVVKGDPPQLS 340
Cdd:cd06653  165 GIKSVTGT------PYwMSPEVI----SGEGYGRKADVWSVACTVVEMLTEKPPWAEYEamaAIFKIATQPTKPQLPDGV 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 526479851 341 NSEEREFSPSFinFVnlcltkDESKRPKYKELLKHPFI 378
Cdd:cd06653  235 SDACRDFLRQI--FV------EEKRRPTAEFLLRHPFV 264
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
116-378 4.11e-27

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: 109.11  E-value: 4.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDE--------KEQKqLLMDLDvvmrssdCPYIVQFYGALFREGDCWI 187
Cdd:cd07829    4 LEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipstalREIS-LLKELK-------HPNIVKLLDVIHTENKLYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFDKFYKYVYSVLddviPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-V 266
Cdd:cd07829   76 VFEYCDQDLKKYLDKRPGPL----PPNLIKSIMYQLLRGLAYCHSH-RILHRDLKPQNLLINRDGVLKLADFGLARAFgI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPErIDPSASRQGYDVrsDVWSLGITLYELATGR--FP--------------------------- 317
Cdd:cd07829  151 PLRTYTHEVVTLWYRAPE-ILLGSKHYSTAV--DIWSVGCIFAELITGKplFPgdseidqlfkifqilgtpteeswpgvt 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526479851 318 -YPKWNSVFDQLtqvvkgdPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd07829  228 kLPDYKPTFPKW-------PKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
113-377 4.47e-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: 109.13  E-value: 4.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 113 LKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrstVDEKEQKQllMDLDVvMRSSDCPYIVQFYGALFREGDCW------ 186
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV---LQDKRYKN--RELQI-MRRLKHPNIVKLKYFFYSSGEKKdevyln 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSFDKFYKYvYSVLDDVIPeeilgkitLATVK--------ALNHLkENLKIIHRDIKPSNILLD-RSGNIKLC 257
Cdd:cd14137   80 LVMEYMPETLYRVIRH-YSKNKQTIP--------IIYVKlysyqlfrGLAYL-HSLGICHRDIKPQNLLVDpETGVLKLC 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 258 DFGISGQLVDSIAKTRDAGCRPYMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--GD 335
Cdd:cd14137  150 DFGSAKRLVPGEPNVSYICSRYYRAPELIFGA---TDYTTAIDIWSAGCVLAELLLGQPLFPGESSV-DQLVEIIKvlGT 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 336 P--PQLS----NSEEREFS----------------PSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14137  226 PtrEQIKamnpNYTEFKFPqikphpwekvfpkrtpPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
119-377 7.11e-27

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: 7.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLdKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYkyVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGC 277
Cdd:cd05577   81 KYH--IYNVGTRGFSEARAIFYAAEIICGLEHL-HNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 RPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFD--QLTQVVKGDPPQLSNSeereFSPSFINFV 355
Cdd:cd05577  158 HGYMAPEVL---QKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDkeELKRRTLEMAVEYPDS----FSPEARSLC 230
                        250       260
                 ....*....|....*....|....*..
gi 526479851 356 NLCLTKDESKR-----PKYKELLKHPF 377
Cdd:cd05577  231 EGLLQKDPERRlgcrgGSADEVKEHPF 257
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
119-378 7.57e-27

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: 107.64  E-value: 7.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGAlFREGDC-WICMELMSTS 195
Cdd:cd14099    9 LGKGGFAKCYEVTDMSTGKVYAGKVVPksSLTKPKQREKLKSEIKI-HRSLKHPNIVKFHDC-FEDEENvYILLELCSNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdkfykyvySVLDDV-----IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd14099   87 ---------SLMELLkrrkaLTEPEVRYFMRQILSGVKYLHSN-RIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRD-AGCRPYMAPERIDpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDppqLSNSEEREFSP 349
Cdd:cd14099  157 RKKTlCGTPNYIAPEVLE---KKKGHSFEVDIWSLGVILYTLLVGKPPFET-SDVKETYKRIKKNE---YSFPSHLSISD 229
                        250       260
                 ....*....|....*....|....*....
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14099  230 EAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
116-377 8.06e-27

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: 108.57  E-value: 8.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRS-TVDEKEQKQLLMDLDVVMRSSDCPYIVQFYgALFREG-DCWICMELMS 193
Cdd:cd07832    5 LGRIGEGAHGIVFKAKDRETGETVALKKVALrKLEGGIPNQALREIKALQACQGHPYVVKLR-DVFPHGtGFVLVFEYML 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSfdkfykyVYSVLDDV---IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd07832   84 SS-------LSEVLRDEerpLTEAQVKRYMRMLLKGVAYMHAN-RIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 K--TRDAGCRPYMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--GDP-----PQLS- 340
Cdd:cd07832  156 RlySHQVATRWYRAPELLYGS---RKYDEGVDLWAVGCIFAELLNGSPLFPGENDI-EQLAIVLRtlGTPnektwPELTs 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 341 ----------NSE----EREF---SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07832  232 lpdynkitfpESKgirlEEIFpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
119-375 1.13e-26

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: 107.41  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRStvDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDk 198
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPK--PSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGD- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 fykyVYSVLDDV--IPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL-DRS-GNIKLCDFGISgQLVDSIAKtRD 274
Cdd:cd13987   78 ----LFSIIPPQvgLPEERVKRCAAQLASALDFM-HSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLT-RRVGSTVK-RV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPE----------RIDPSasrqgydvrSDVWSLGITLYELATGRFPYPKWNSV------FDQLTQVVKGDPPq 338
Cdd:cd13987  151 SGTIPYTAPEvceakknegfVVDPS---------IDVWAFGVLLFCCLTGNFPWEKADSDdqfyeeFVRWQKRKNTAVP- 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 339 lsnSEEREFSPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd13987  221 ---SQWRRFTPKALRMFKKLLAPEPERRCSIKEVFKY 254
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
119-376 1.51e-26

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: 106.58  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFI--PKRDKKKEAVLREISI-LNQLQHPRIIQLHEAYESPTELVLILELCSGGelL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFY-KYVYSVlDDVIpeEILGKItlatVKALNHLkENLKIIHRDIKPSNILLD--RSGNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd14006   78 DRLAeRGSLSE-EEVR--TYMRQL----LEGLQYL-HNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGEELKE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIdpsasrQGYDV--RSDVWSLGITLYELATGRFPYPKWNsvfDQLTQ--VVKGDpPQLSNSEEREFSP 349
Cdd:cd14006  150 IFGTPEFVAPEIV------NGEPVslATDMWSIGVLTYVLLSGLSPFLGED---DQETLanISACR-VDFSEEYFSSVSQ 219
                        250       260
                 ....*....|....*....|....*..
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14006  220 EAKDFIRKLLVKEPRKRPTAQEALQHP 246
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
112-375 1.59e-26

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: 107.45  E-value: 1.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14046    7 DFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNH-QHVVRYYQAWIERANLYIQMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 M--STSFDKFYKYVYSVLDDV--IPEEILgkitlatvKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFG------- 260
Cdd:cd14046   86 CekSTLRDLIDSGLFQDTDRLwrLFRQIL--------EGLAYIHS-QGIIHRDLKPVNIFLDSNGNVKIGDFGlatsnkl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ------------ISGQLVDSIAKTRDAGCRPYMAPERIDPSASRqgYDVRSDVWSLGITLYEL----ATG--RFpypkwn 322
Cdd:cd14046  157 nvelatqdinksTSAALGSSGDLTGNVGTALYVAPEVQSGTKST--YNEKVDMYSLGIIFFEMcypfSTGmeRV------ 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 323 SVFDQLTQVVKGDPPQLSNSE-EREFSpsfinFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14046  229 QILTALRSVSIEFPPDFDDNKhSKQAK-----LIRWLLNHDPAKRPSAQELLKS 277
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
111-377 2.23e-26

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: 106.92  E-value: 2.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWIC 188
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLdkRHIIKEKKVKYVTIEKEVLSRLAH-PGIVKLYYTFQDESKLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMST-SFDKFYKYVYSvLDDVIPEEILGKITLAtvkaLNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS----- 262
Cdd:cd05581   80 LEYAPNgDLLEYIRKYGS-LDEKCTRFYTAEIVLA----LEYLHSK-GIIHRDLKPENILLDEDMHIKITDFGTAkvlgp 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 -----GQLVDSIAKTRDAGCRP--------YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLT 329
Cdd:cd05581  154 dsspeSTKGDADSQIAYNQARAasfvgtaeYVSPELL----NEKPAGKSSDLWALGCIIYQMLTGKPPF-RGSNEYLTFQ 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 330 QVVKGDPPQLSNseereFSPSFINFVNLCLTKDESKRP------KYKELLKHPF 377
Cdd:cd05581  229 KIVKLEYEFPEN-----FPPDAKDLIQKLLVLDPSKRLgvnengGYDELKAHPF 277
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
119-374 2.49e-26

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: 106.37  E-value: 2.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRIRStvdEKEQKQLLMDLDVVMRSsDCPYIVQFYGALFREGDCWICMELMSTSfdK 198
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIES---ESEKKAFEVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGG--S 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 FYKYVYSvlDDVIPEEILGKI---TLATVKALNHLkENLK---IIHRDIKPSNILLDRSG-NIKLCDFGISGQLvdSIAK 271
Cdd:cd14058   73 LYNVLHG--KEPKPIYTAAHAmswALQCAKGVAYL-HSMKpkaLIHRDLKPPNLLLTNGGtVLKICDFGTACDI--STHM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKW-NSVFDQLTQVVKGD-PPQLSNSEERefsp 349
Cdd:cd14058  148 TNNKGSAAWMAPEVFEGSK----YSEKCDVFSWGIILWEVITRRKPFDHIgGPAFRIMWAVHNGErPPLIKNCPKP---- 219
                        250       260
                 ....*....|....*....|....*
gi 526479851 350 sFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14058  220 -IESLMTRCWSKDPEKRPSMKEIVK 243
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-378 8.47e-26

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: 104.81  E-value: 8.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGS---VNKMVHKPSGQIMAVKRI-------RSTVDEKEQKQLLMDLDvvmrssdCPYIVQFYgALFREGD--CW 186
Cdd:cd08222    8 LGSGNFGTvylVSDLKATADEELKVLKEIsvgelqpDETVDANREAKLLSKLD-------HPAIVKFH-DSFVEKEsfCI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 IcmelmsTSF-------DKFYKYVYSvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLdRSGNIKLCDF 259
Cdd:cd08222   80 V------TEYceggdldDKISEYKKS--GTTIDENQILDWFIQLLLAVQYMHER-RILHRDLKAKNIFL-KNNVIKVGDF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQLVDS--IAKTRdAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGDPP 337
Cdd:cd08222  150 GISRILMGTsdLATTF-TGTPYYMSPEVLK----HEGYNSKSDIWSLGCILYEMCCLKHAFDGQN-LLSVMYKIVEGETP 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 526479851 338 QLSNSeereFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08222  224 SLPDK----YSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
112-378 1.43e-25

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: 104.41  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGE---IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEkeQKQLLMD---LDVVMRSSDcpyIVQFYGALFREGDC 185
Cdd:cd06624    6 EYDESGErvvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSR--EVQPLHEeiaLHSRLSHKN---IVQYLGSVSEDGFF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELM-STSFDKFYKYVYSVLDDviPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDR-SGNIKLCDFGISG 263
Cdd:cd06624   81 KIFMEQVpGGSLSALLRSKWGPLKD--NENTIGYYTKQILEGLKYLHDN-KIVHRDIKGDNVLVNTySGVVKISDFGTSK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QL--VDSIAKTRdAGCRPYMAPERIDpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQV--VKGDPP-- 337
Cdd:cd06624  158 RLagINPCTETF-TGTLQYMAPEVID--KGQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVgmFKIHPEip 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 338 -QLSNSEErefspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd06624  235 eSLSEEAK--------SFILRCFEPDPDKRATASDLLQDPFL 268
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
119-375 1.66e-25

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: 104.28  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRH-PNLVRLLGYCLESDEKLLVYEYMPNGslE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKyvySVLDDVIPEEILGKITLATVKALNHL--KENLKIIHRDIKPSNILLDRSGNIKLCDFGIS--GQLVDSIAKT 272
Cdd:cd14066   79 DRLHC---HKGSPPLPWPQRLKIAKGIARGLEYLheECPPPIIHGDIKSSNILLDEDFEPKLTDFGLArlIPPSESVSKT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDA-GCRPYMAPEridpsASRQG-YDVRSDVWSLGITLYELATGRFPY---PKWNSVFDqLTQVVKG----------DP- 336
Cdd:cd14066  156 SAVkGTIGYLAPE-----YIRTGrVSTKSDVYSFGVVLLELLTGKPAVdenRENASRKD-LVEWVESkgkeeledilDKr 229
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 337 PQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14066  230 LVDDDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQM 268
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
118-377 1.80e-25

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: 104.54  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR---STVDE----KEQKQLlmdldvvMRSSDCPYIVQFYgALFREGDC-WICM 189
Cdd:cd07830    6 QLGDGTFGSVYLARNKETGELVAIKKMKkkfYSWEEcmnlREVKSL-------RKLNEHPNIVKLK-EVFRENDElYFVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSFDKFYKyvySVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd07830   78 EYMEGNLYQLMK---DRKGKPFSESVIRSIIYQILQGLAHIHKH-GFFHRDLKPENLLVSGPEVVKIADFGLAREIRSRP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGR--FPypkWNSVFDQLTQVVK--GDP--------P 337
Cdd:cd07830  154 PYTDYVSTRWYRAPEILLRSTS---YSSPVDIWALGCIMAELYTLRplFP---GSSEIDQLYKICSvlGTPtkqdwpegY 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 338 QLSNSEEREF---------------SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07830  228 KLASKLGFRFpqfaptslhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
115-379 2.04e-25

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: 105.10  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQK-QLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd06634   19 DLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKyvysVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSiakTR 273
Cdd:cd06634   99 GSASDLLE----VHKKPLQEVEIAAITHGALQGLAYL-HSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPA---NS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIDPSASRQgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSeerEFSPSFIN 353
Cdd:cd06634  171 FVGTPYWMAPEVILAMDEGQ-YDGKVDVWSLGITCIELAERKPPLFNMNAM-SALYHIAQNESPALQSG---HWSEYFRN 245
                        250       260
                 ....*....|....*....|....*.
gi 526479851 354 FVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd06634  246 FVDSCLQKIPQDRPTSDVLLKHRFLL 271
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
119-378 2.41e-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: 103.62  E-value: 2.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDV-VMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd14073    9 LGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIeIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGG-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYVYSvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGC 277
Cdd:cd14073   87 ELYDYISE--RRRLPEREARRIFRQIVSAVHYCHKN-GVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQTFCGS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 RPYMAPErIDPSASRQGYDVrsDVWSLGITLYELATGRFPY--PKWNSVFDQLTQVVKGDPPQLSNSEerefspsfiNFV 355
Cdd:cd14073  164 PLYASPE-IVNGTPYQGPEV--DCWSLGVLLYTLVYGTMPFdgSDFKRLVKQISSGDYREPTQPSDAS---------GLI 231
                        250       260
                 ....*....|....*....|...
gi 526479851 356 NLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14073  232 RWMLTVNPKRRATIEDIANHWWV 254
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
118-367 3.05e-25

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: 103.57  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST- 194
Cdd:cd08228    9 KIGRGQFSEVYRATCLLDRKPVALKKVQifEMMDAKARQDCVKEIDL-LKQLNHPNVIKYLDSFIEDNELNIVLELADAg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIsGQLVDSiaKTRD 274
Cdd:cd08228   88 DLSQMIKY-FKKQKRLIPERTVWKYFVQLCSAVEHMHSR-RVMHRDIKPANVFITATGVVKLGDLGL-GRFFSS--KTTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 A----GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFP-YPKWNSVFDQLTQVVKGDPPQLSNseeREFSP 349
Cdd:cd08228  163 AhslvGTPYYMSPERI----HENGYNFKSDIWSLGCLLYEMAALQSPfYGDKMNLFSLCQKIEQCDYPPLPT---EHYSE 235
                        250
                 ....*....|....*...
gi 526479851 350 SFINFVNLCLTKDESKRP 367
Cdd:cd08228  236 KLRELVSMCIYPDPDQRP 253
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
119-376 3.21e-25

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: 103.66  E-value: 3.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI---RSTVDEKEQ-KQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVsfcRNSSSEQEEvVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdkfykYVYSVLDD--VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGN-IKLCDFGIS--------- 262
Cdd:cd06630   88 G------SVASLLSKygAFSENVIINYTLQILRGLAYLHDN-QIIHRDLKGANLLVDSTGQrLRIADFGAAarlaskgtg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 -----GQLVDSIAktrdagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRfpyPKWNS--VFDQLTQVVK-- 333
Cdd:cd06630  161 agefqGQLLGTIA---------FMAPEVL----RGEQYGRSCDVWSVGCVIIEMATAK---PPWNAekISNHLALIFKia 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 334 --GDPPQLSNSeereFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd06630  225 saTTPPPIPEH----LSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
119-378 4.64e-25

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: 102.72  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVV-MRSSDCPYIVQFYGALFREGDCWICMELMSTS-- 195
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAiMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGel 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGI-SGQLVDSIAKTrD 274
Cdd:cd14081   89 FD------YLVKKGRLTEKEARKFFRQIISALDYC-HSHSICHRDLKPENLLLDEKNNIKIADFGMaSLQPEGSLLET-S 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIdpsaSRQGYDVR-SDVWSLGITLYELATGRFPYPKWNsvFDQLTQVVKGDPPQLsnseerefsPSFI- 352
Cdd:cd14081  161 CGSPHYACPEVI----KGEKYDGRkADIWSCGVILYALLVGALPFDDDN--LRQLLEKVKRGVFHI---------PHFIs 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 353 ----NFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14081  226 pdaqDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
119-377 5.40e-25

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: 102.94  E-value: 5.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGaLFREGDC-WICMELMSTS 195
Cdd:cd14098    8 LGSGTFAEVKKAVEVETGKMRAIKQIvkRKVAGNDKNLQLFQREINILKSLEHPGIVRLID-WYEDDQHiYLVMEYVEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdkfykyvySVLDDV-----IPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGN--IKLCDFGISG-QLVD 267
Cdd:cd14098   87 ---------DLMDFImawgaIPEQHARELTKQILEAMAYT-HSMGITHRDLKPENILITQDDPviVKISDFGLAKvIHTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRdAGCRPYMAPERIDPSASRQ--GYDVRSDVWSLGITLYELATGRFPYPkwNSVFDQLTQVVKG----DPPQLSN 341
Cdd:cd14098  157 TFLVTF-CGTMAYLAPEILMSKEQNLqgGYSNLVDMWSVGCLVYVMLTGALPFD--GSSQLPVEKRIRKgrytQPPLVDF 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 342 seerEFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14098  234 ----NISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
118-378 8.06e-25

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: 102.30  E-value: 8.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALF-REGDCWICM-ELMST 194
Cdd:cd13983    8 VLGRGSFKTVYRAFDTEEGIEVAWNEIKlRKLPKAERQRFKQEIEI-LKSLKHPNIIKFYDSWEsKSKKEVIFItELMTS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVYSVLDdvipEEILGKITLATVKALNHL-KENLKIIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd13983   87 GTLKQYLKRFKRLK----LKVIKSWCRQILEGLNYLhTRDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQSFAKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RdAGCRPYMAPERIDpsasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQlsnSEEREFSPSFI 352
Cdd:cd13983  163 V-IGTPEFMAPEMYE-----EHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPE---SLSKVKDPELK 233
                        250       260
                 ....*....|....*....|....*.
gi 526479851 353 NFVNLCLTKdESKRPKYKELLKHPFI 378
Cdd:cd13983  234 DFIEKCLKP-PDERPSARELLEHPFF 258
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
119-377 8.06e-25

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: 102.47  E-value: 8.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDV---VMRSSDCPYIVQFYGALFREGD--CWICMELMS 193
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECeiqLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLkIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD---SIA 270
Cdd:cd06651   95 GGSVKDQLKAYGALT----ESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN---SVFDQLTQVVKGDPPQLSNSEERE 346
Cdd:cd06651  170 GIRSVTGTPYwMSPEVI----SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEamaAIFKIATQPTNPQLPSHISEHARD 245
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 347 FSPsfinfvnlCLTKDESKRPKYKELLKHPF 377
Cdd:cd06651  246 FLG--------CIFVEARHRPSAEELLRHPF 268
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
119-378 9.49e-25

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: 102.47  E-value: 9.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI------RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd14084   14 LGSGACGEVKLAYDKSTCKKVAIKIInkrkftIGSRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLELM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STS--FDKfykyvysVLDDVIPEEILGK-ITLATVKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCDFGISGQLV 266
Cdd:cd14084   94 EGGelFDR-------VVSNKRLKEAICKlYFYQMLLAVKYLHSN-GIIHRDLKPENVLLSSQEEeclIKITDFGLSKILG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 -DSIAKTRdAGCRPYMAPErIDPSASRQGYDVRSDVWSLGITLYELATGrfpYPKWNSVFDQLT---QVVKG----DPPQ 338
Cdd:cd14084  166 eTSLMKTL-CGTPTYLAPE-VLRSFGTEGYTRAVDCWSLGVILFICLSG---YPPFSEEYTQMSlkeQILSGkytfIPKA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 339 LSNSEEREFspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14084  241 WKNVSEEAK-----DLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
119-378 1.21e-24

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: 102.62  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDLDVVMRSSDC-----PYIVQFYGALFREGDCWICMELMS 193
Cdd:cd14094   11 IGKGPFSVVRRCIHRETGQQFAVKIV--DVAKFTSSPGLSTEDLKREASIChmlkhPHIVELLETYSSDGMLYMVFEFMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL---DRSGNIKLCDFGISGQLVD--S 268
Cdd:cd14094   89 GADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGEsgL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKG----DPPQLSNsee 344
Cdd:cd14094  168 VAGGR-VGTPHFMAPEVV----KREPYGKPVDVWGCGVILFILLSGCLPF--YGTKERLFEGIIKGkykmNPRQWSH--- 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 345 reFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14094  238 --ISESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
116-377 1.86e-24

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: 102.06  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYgALFREgdcwicmelmSTS 195
Cdd:cd07847    6 LSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLI-EVFRR----------KRK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYKYV-YSVLDDV------IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG----ISGQ 264
Cdd:cd07847   75 LHLVFEYCdHTVLNELeknprgVPEHLIKKIIWQTLQAVNFCHKH-NCIHRDVKPENILITKQGQIKLCDFGfariLTGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 ---LVDSIAKtrdagcRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRfpyPKW--NSVFDQLTQVVK--GD-- 335
Cdd:cd07847  154 gddYTDYVAT------RWYRAPELL---VGDTQYGPPVDVWAIGCVFAELLTGQ---PLWpgKSDVDQLYLIRKtlGDli 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 336 PP--------------QLSNSEERE--------FSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07847  222 PRhqqifstnqffkglSIPEPETREpleskfpnISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
119-381 2.21e-24

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: 101.53  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDL--------DVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd14182   11 LGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEVQELreatlkeiDILRKVSGHPNIIQLKDTYETNTFFFLVFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTS--FDKFYKYVysvlddVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS 268
Cdd:cd14182   91 LMKKGelFDYLTEKV------TLSEKETRKIMRALLEVICAL-HKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERIDPSA--SRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGDPPQLSNSEERE 346
Cdd:cd14182  164 EKLREVCGTPGYLAPEIIECSMddNHPGYGKEVDMWSTGVIMYTLLAGSPPF--WHRKQMLMLRMIMSGNYQFGSPEWDD 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFILMY 381
Cdd:cd14182  242 RSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQY 276
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
119-378 4.17e-24

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: 100.50  E-value: 4.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDV---VMRSSDCPYIVQFYGALF--REGDCWICMELMS 193
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVNALECeiqLLKNLLHERIVQYYGCLRdpQERTLSIFMEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLkIIHRDIKPSNILLDRSGNIKLCDFG---------ISGQ 264
Cdd:cd06652   90 GGSIKDQLKSYGALT----ENVTRKYTRQILEGVHYLHSNM-IVHRDIKGANILRDSVGNVKLGDFGaskrlqticLSGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTrdagcrPY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN---SVFDQLTQVVKGDPPQLS 340
Cdd:cd06652  165 GMKSVTGT------PYwMSPEVI----SGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEamaAIFKIATQPTNPQLPAHV 234
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 341 NSEEREFSPSFinFVnlcltkdESK-RPKYKELLKHPFI 378
Cdd:cd06652  235 SDHCRDFLKRI--FV-------EAKlRPSADELLRHTFV 264
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
119-374 4.34e-24

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: 100.50  E-value: 4.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKE-----QKQLLMDLDVVMRSSDCPYIVQFYgALFREGDC-WICMEL 191
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLyKSGPNSKDgndfqKLPQLREIDLHRRVSRHPNIITLH-DVFETEVAiYIVLEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSfDKFYkyvySVLDD---VIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRS-GNIKLCDFGISGQlvD 267
Cdd:cd13993   87 CPNG-DLFE----AITENriyVGKTELIKNVFLQLIDAVKHC-HSLGIYHRDIKPENILLSQDeGTVKLCDFGLATT--E 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRPYMAPERIDPSA-SRQGYDVRS-DVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSeer 345
Cdd:cd13993  159 KISMDFGVGSEFYMAPECFDEVGrSLKGYPCAAgDIWSLGIILLNLTFGRNPWKIASES-DPIFYDYYLNSPNLFDV--- 234
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 346 eFSPSFINFVNL---CLTKDESKRPKYKELLK 374
Cdd:cd13993  235 -ILPMSDDFYNLlrqIFTVNPNNRILLPELQL 265
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
106-374 6.53e-24

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: 99.73  E-value: 6.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKpsGQIMAVKRIRstvDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd05039    1 WAINKKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLK---DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGisgqL 265
Cdd:cd05039   76 YIVTEYMAKG--SLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESK-KFVHRDLAARNVLVSEDNVAKVSDFG----L 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRP--YMAPEridpsASRQG-YDVRSDVWSLGITLYEL-ATGRFPYPKWnSVFDQLTQVVKG---DPPq 338
Cdd:cd05039  149 AKEASSNQDGGKLPikWTAPE-----ALREKkFSTKSDVWSFGILLWEIySFGRVPYPRI-PLKDVVPHVEKGyrmEAP- 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 339 lsnseerEFSPSFI-NFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05039  222 -------EGCPPEVyKVMKNCWELDPAKRPTFKQLRE 251
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
112-377 7.50e-24

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: 100.05  E-value: 7.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLgeIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQL-------LMDLDVVMRSSDCPYIVQFYGALFREGD 184
Cdd:cd14181   13 DPKEV--IGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLeevrsstLKEIHILRQVSGHPSIITLIDSYESSTF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTS--FDKFYKYVysvlddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd14181   91 IFLVFDLMRRGelFDYLTEKV------TLSEKETRSIMRSLLEAVSYLHAN-NIVHRDLKPENILLDDQLHIKLSDFGFS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLvDSIAKTRD-AGCRPYMAPERIDPS--ASRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGDPPQL 339
Cdd:cd14181  164 CHL-EPGEKLRElCGTPGYLAPEILKCSmdETHPGYGKEVDLWACGVILFTLLAGSPPF--WHRRQMLMLRMIMEGRYQF 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 526479851 340 SNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14181  241 SSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
119-390 8.81e-24

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: 100.68  E-value: 8.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYgALFR------EGDCWICMEL 191
Cdd:cd07834    8 IGSGAYGVVCSAYDKRTGRKVAIKKIsNVFDDLIDAKRILREI-KILRHLKHENIIGLL-DILRppspeeFNDVYIVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTsfDkFYKYVYSvlDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd07834   86 MET--D-LHKVIKS--PQPLTDDHIQYFLYQILRGLKYLHS-AGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDEDK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 --------TrdagcRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGR--FPypkWNSVFDQLTQVVK--GDPP-- 337
Cdd:cd07834  160 gflteyvvT-----RWYRAPELL---LSSKKYTKAIDIWSVGCIFAELLTRKplFP---GRDYIDQLNLIVEvlGTPSee 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 338 ---QLSNSEEREF-------------------SPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVAC 390
Cdd:cd07834  229 dlkFISSEKARNYlkslpkkpkkplsevfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPEDEPVA 303
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
112-385 1.37e-23

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: 99.42  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDlgEIGRGAYGSVNKMVHKPSGQIMAVKRIRS-TVDEKEQKQLLMDLDVVmRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd14086    4 DLKE--ELGKGAFSVVRRCVQKSTGQEFAAKIINTkKLSARDHQKLEREARIC-RLLKHPNIVRLHDSISEEGFHYLVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdkfykyvySVLDDVIPEEILGKITLA-----TVKALNHLKENlKIIHRDIKPSNILL---DRSGNIKLCDFGIS 262
Cdd:cd14086   81 LVTGG---------ELFEDIVAREFYSEADAShciqqILESVNHCHQN-GIVHRDLKPENLLLaskSKGAAVKLADFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLVDSI-AKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGrFPyPKWNSVFDQLTQVVKGDPPQLSN 341
Cdd:cd14086  151 IEVQGDQqAWFGFAGTPGYLSPEVL----RKDPYGKPVDIWACGVILYILLVG-YP-PFWDEDQHRLYAQIKAGAYDYPS 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 526479851 342 SEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERA 385
Cdd:cd14086  225 PEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQRDRVA 268
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
96-378 1.77e-23

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: 99.54  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  96 GKLKISPEQHWDFTAEDLKdlgEIGRGAYGSVNKMV-HKpSGQIMAVKRIRSTvdEKEQKQLLMDLDVV--MRSSDCP-- 170
Cdd:cd14210    1 GDYKVVLGDHIAYRYEVLS---VLGKGSFGQVVKCLdHK-TGQLVAIKIIRNK--KRFHQQALVEVKILkhLNDNDPDdk 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 171 -YIVQFYGA-LFREGDCwICMELMSTSfdkfykyVYSVLDDV----IPEEILGKITLATVKALNHLKENlKIIHRDIKPS 244
Cdd:cd14210   75 hNIVRYKDSfIFRGHLC-IVFELLSIN-------LYELLKSNnfqgLSLSLIRKFAKQILQALQFLHKL-NIIHCDLKPE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 245 NILL--DRSGNIKLCDFGIS---GQLVDSIAKTRDagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYP 319
Cdd:cd14210  146 NILLkqPSKSSIKVIDFGSScfeGEKVYTYIQSRF-----YRAPEVI----LGLPYDTAIDMWSLGCILAELYTGYPLFP 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 320 KWNSVfDQLTQV--VKGDPPQ---------------------LSNSEEREFSPS--------------FINFVNLCLTKD 362
Cdd:cd14210  217 GENEE-EQLACImeVLGVPPKslidkasrrkkffdsngkprpTTNSKGKKRRPGskslaqvlkcddpsFLDFLKKCLRWD 295
                        330
                 ....*....|....*.
gi 526479851 363 ESKRPKYKELLKHPFI 378
Cdd:cd14210  296 PSERMTPEEALQHPWI 311
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
111-377 1.90e-23

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: 99.19  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKR------IRS-----TVDEKEqkqllmdldvVMRSSDCPYIVQFYGAl 179
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKIlkkakiIKLkqvehVLNEKR----------ILSEVRHPFIVNLLGS- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 FRegDCWicmelmstsfdkfykYVYSVLDDVIPEEIL------GKITLATVK--------ALNHLkENLKIIHRDIKPSN 245
Cdd:cd05580   70 FQ--DDR---------------NLYMVMEYVPGGELFsllrrsGRFPNDVAKfyaaevvlALEYL-HSLDIVYRDLKPEN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 246 ILLDRSGNIKLCDFGISGQLVD---SIAKTRDagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGrfpYPKWN 322
Cdd:cd05580  132 LLLDSDGHIKITDFGFAKRVKDrtyTLCGTPE-----YLAPEII----LSKGHGKAVDWWALGILIYEMLAG---YPPFF 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 323 SVFDQLT--QVVKGD---PpqlsnseeREFSPSFINFVNLCLTKDESKR-----PKYKELLKHPF 377
Cdd:cd05580  200 DENPMKIyeKILEGKirfP--------SFFDPDAKDLIKRLLVVDLTKRlgnlkNGVEDIKNHPW 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
111-376 2.00e-23

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: 98.56  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI---RSTVDEKEQKQLLMDLDVVMRSsdcPYIVQFYGALFREGDCWI 187
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkRAPGDCPENIKKEVCIQKMLSH---KNVVRFYGHRREGEFQYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTS--FDKfykyvysVLDDV-IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd14069   78 FLEYASGGelFDK-------IEPDVgMPEDVAQFYFQQLMAGLKYLHSC-GITHRDIKPENLLLDENDNLKISDFGLATV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LV---DSIAKTRDAGCRPYMAPERIdpsaSRQGYDV-RSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDppQLS 340
Cdd:cd14069  150 FRykgKERLLNKMCGTLPYVAPELL----AKKKYRAePVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENK--KTY 223
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 341 NSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14069  224 LTPWKKIDTAALSLLRKILTENPNKRITIEDIKKHP 259
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
118-367 2.17e-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: 98.56  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTvDEKEQKQLLMDLDVVMRSSDCPYIVQFYG-ALFREG---DCWICMELMS 193
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFN-DEEQLRVAIKEIEIMKRLCGHPNIVQYYDsAILSSEgrkEVLLLMEYCP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFdkfYKYVYSVLDDVIPEEILGKITLATVKALNHL-KENLKIIHRDIKPSNILLDRSGNIKLCDFG-ISGQLVdsiAK 271
Cdd:cd13985   86 GSL---VDILEKSPPSPLSEEEVLRIFYQICQAVGHLhSQSPPIIHRDIKIENILFSNTGRFKLCDFGsATTEHY---PL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCR------------PYMAPERIDPSaSRQGYDVRSDVWSLGITLYELATGRFPypkwnsvFDQLTQVvkGDPPQL 339
Cdd:cd13985  160 ERAEEVNiieeeiqknttpMYRAPEMIDLY-SKKPIGEKADIWALGCLLYKLCFFKLP-------FDESSKL--AIVAGK 229
                        250       260
                 ....*....|....*....|....*....
gi 526479851 340 SNSEERE-FSPSFINFVNLCLTKDESKRP 367
Cdd:cd13985  230 YSIPEQPrYSPELHDLIRHMLTPDPAERP 258
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-378 2.19e-23

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: 98.27  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVV-MRSSDcpYIVQFYGALFREGDCWICMELMS--T 194
Cdd:cd08221    8 LGRGAFGEAVLYRKTEDNSLVVWKEVNlSRLSEKERRDALNEIDILsLLNHD--NIITYYNHFLDGESLFIEMEYCNggN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVysvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS------GQLVDS 268
Cdd:cd08221   86 LHDKIAQQK----NQLFPEEVVLWYLYQIVSAVSHIHKA-GILHRDIKTLNIFLTKADLVKLGDFGISkvldseSSMAES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTrdagcrP-YMAPERIdpsasrQG--YDVRSDVWSLGITLYELATgrfpypkWNSVFDQLTQ------VVKGDppql 339
Cdd:cd08221  161 IVGT------PyYMSPELV------QGvkYNFKSDIWAVGCVLYELLT-------LKRTFDATNPlrlavkIVQGE---- 217
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 340 SNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08221  218 YEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
118-367 3.10e-23

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: 98.56  E-value: 3.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST- 194
Cdd:cd08229   31 KIGRGQFSEVYRATCLLDGVPVALKKVQifDLMDAKARADCIKEIDL-LKQLNHPNVIKYYASFIEDNELNIVLELADAg 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIsGQLVDS--IAKT 272
Cdd:cd08229  110 DLSRMIKH-FKKQKRLIPEKTVWKYFVQLCSALEHMHSR-RVMHRDIKPANVFITATGVVKLGDLGL-GRFFSSktTAAH 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFP-YPKWNSVFDQLTQVVKGDPPQLSNSeerEFSPSF 351
Cdd:cd08229  187 SLVGTPYYMSPERI----HENGYNFKSDIWSLGCLLYEMAALQSPfYGDKMNLYSLCKKIEQCDYPPLPSD---HYSEEL 259
                        250
                 ....*....|....*.
gi 526479851 352 INFVNLCLTKDESKRP 367
Cdd:cd08229  260 RQLVNMCINPDPEKRP 275
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
118-377 4.42e-23

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: 98.79  E-value: 4.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRG--AYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYgALFREGD-CWICMELMSt 194
Cdd:cd08226    5 ELGKGfcNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHW-TVFTEGSwLWVISPFMA- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 sfdkfYKYVYSVLDDVIPE----EILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCdfGISG--QLVDS 268
Cdd:cd08226   83 -----YGSARGLLKTYFPEgmneALIGNILYGAIKALNYLHQN-GCIHRSVKASHILISGDGLVSLS--GLSHlySMVTN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTR--------DAGCRPYMAPERIdpsasRQ---GYDVRSDVWSLGITLYELATGRFP-------------------Y 318
Cdd:cd08226  155 GQRSKvvydfpqfSTSVLPWLSPELL-----RQdlhGYNVKSDIYSVGITACELARGQVPfqdmrrtqmllqklkgppyS 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 319 PKWNSVFDQLTQ----------------VVKGDPPQLSNSEE------REFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd08226  230 PLDIFPFPELESrmknsqsgmdsgigesVATSSMTRTMTSERlqtpssKTFSPAFHNLVELCLQQDPEKRPSASSLLSHS 309

                 .
gi 526479851 377 F 377
Cdd:cd08226  310 F 310
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
116-378 4.57e-23

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: 97.19  E-value: 4.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd08218    5 IKKIGEGSFGKALLVKSKEDGKQYVIKEINiSKMSPKEREESRKEVAVLSKMKH-PNIVQYQESFEENGNLYIVMDYCDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD 274
Cdd:cd08218   84 G--DLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDR-KILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELART 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRP-YMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGDPPQLSNseerEFSPSFIN 353
Cdd:cd08218  161 CIGTPyYLSPEICE----NKPYNNKSDIWALGCVLYEMCTLKHAFEAGN-MKNLVLKIIRGSYPPVPS----RYSYDLRS 231
                        250       260
                 ....*....|....*....|....*
gi 526479851 354 FVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08218  232 LVSQLFKRNPRDRPSINSILEKPFI 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
110-311 5.38e-23

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: 97.36  E-value: 5.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd13996    5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREV-KALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMStsfdkfYKYVYSVLDDVIPEEILGK-----ITLATVKALNHLkENLKIIHRDIKPSNILLD-RSGNIKLCDFG--- 260
Cdd:cd13996   84 ELCE------GGTLRDWIDRRNSSSKNDRklaleLFKQILKGVSYI-HSKGIVHRDLKPSNIFLDnDDLQVKIGDFGlat 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 261 -ISGQLVDSI-----------AKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYEL 311
Cdd:cd13996  157 sIGNQKRELNnlnnnnngntsNNSVGIGTPLYASPEQLD----GENYNEKADIYSLGIILFEM 215
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
111-378 6.84e-23

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: 97.89  E-value: 6.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKP-SGQIMAVKRIR------STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGalFREG 183
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVPLRnTGKPVAIKVVRkadlssDNLKGSSRANILKEVQI-MKRLSHPNIVKLLD--FQES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 184 D--CWICMELMSTS--FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDR--------- 250
Cdd:cd14096   78 DeyYYIVLELADGGeiFHQIVRLTY------FSEDLSRHVITQVASAVKYLHEI-GVVHRDIKPENLLFEPipfipsivk 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 251 ------------------------SGNIKLCDFGISGQLVDSIAKTrDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGI 306
Cdd:cd14096  151 lrkadddetkvdegefipgvggggIGIVKLADFGLSKQVWDSNTKT-PCGTVGYTAPEVV----KDERYSKKVDMWALGC 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 307 TLYELATGrFPyPKWNSVFDQLT-QVVKGDPPQLSNSEErEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14096  226 VLYTLLCG-FP-PFYDESIETLTeKISRGDYTFLSPWWD-EISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
116-367 8.80e-23

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: 96.80  E-value: 8.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQ-IMAVKRIRST-----VDEKEQKQ----LLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd08528    5 LELLGSGAFGCVYKVRKKSNGQtLLALKEINMTnpafgRTEQERDKsvgdIISEVNIIKEQLRHPNIVRYYKTFLENDRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELM---------STSFDKFYKYvysvlddviPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd08528   85 YIVMELIegaplgehfSSLKEKNEHF---------TEDRIWNIFVQMVLALRYLHKEKQIVHRDLKPNNIMLGEDDKVTI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQ-LVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGD 335
Cdd:cd08528  156 TDFGLAKQkGPESSKMTSVVGTILYSCPEIV----QNEPYGEKADIWALGCILYQMCTLQPPFYSTN-MLTLATKIVEAE 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 336 PPQLSnseEREFSPSFINFVNLCLTKDESKRP 367
Cdd:cd08528  231 YEPLP---EGMYSDDITFVIRSCLTPDPEARP 259
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
115-377 1.04e-22

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: 97.26  E-value: 1.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd05608    5 DFRVLGKGGFGEVSACQMRATGKLYACKKLnKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd05608   85 GGDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQR-RIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 D-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFD--QLTQVVKGDPPQLSNseerEFSPS 350
Cdd:cd05608  164 GyAGTPGFMAPELL----LGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVEnkELKQRILNDSVTYSE----KFSPA 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 351 FINFVNLCLTKDESKRPKYK-----ELLKHPF 377
Cdd:cd05608  236 SKSICEALLAKDPEKRLGFRdgncdGLRTHPF 267
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
119-341 1.07e-22

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: 97.86  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV---NKMVHKPSGQIMAVKR------IRSTVD-----------EKEQKQLLMDLDVVMRSSDCPYIVQFY-- 176
Cdd:cd05584    4 LGKGGYGKVfqvRKTTGSDKGKIFAMKVlkkasiVRNQKDtahtkaernilEAVKHPFIVDLHYAFQTGGKLYLILEYls 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 177 -GALF----REGdcwICMELMStsfdKFYkyvysvlddvipeeiLGKITLAtvkaLNHLKEnLKIIHRDIKPSNILLDRS 251
Cdd:cd05584   84 gGELFmhleREG---IFMEDTA----CFY---------------LAEITLA----LGHLHS-LGIIYRDLKPENILLDAQ 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 252 GNIKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQ 330
Cdd:cd05584  137 GHVKLTDFGLCKESIHDGTVTHTfCGTIEYMAPEIL----TRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRK-KTIDK 211
                        250
                 ....*....|....
gi 526479851 331 VVKGD---PPQLSN 341
Cdd:cd05584  212 ILKGKlnlPPYLTN 225
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-378 1.26e-22

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: 95.96  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS--TSF 196
Cdd:cd08220    8 VGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPggTLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDDvipEEILGKITLATVkALNHLKENLkIIHRDIKPSNILLDRSGNI-KLCDFGISGQLVD-SIAKTRd 274
Cdd:cd08220   88 EYIQQRKGSLLSE---EEILHFFVQILL-ALHHVHSKQ-ILHRDLKTQNILLNKKRTVvKIGDFGISKILSSkSKAYTV- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGDPPQLSNSeereFSPSFINF 354
Cdd:cd08220  162 VGTPCYISPELCEGKP----YNQKSDIWALGCVLYELASLKRAFEAAN-LPALVLKIMRGTFAPISDR----YSEELRHL 232
                        250       260
                 ....*....|....*....|....
gi 526479851 355 VNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08220  233 ILSMLHLDPNKRPTLSEIMAQPII 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
119-377 1.83e-22

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: 95.43  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHK-PSGQIMAVKRI-RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS--- 193
Cdd:cd14121    3 LGSGTYATVYKAYRKsGAREVVAVKCVsKSSLNKASTENLLTEIEL-LKKLKHPHIVELKDFQWDEEHIYLIMEYCSggd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 -TSFDKFYKyvysvlddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGN--IKLCDFGISGQLVDSIA 270
Cdd:cd14121   82 lSRFIRSRR--------TLPESTVRRFLQQLASALQFLREH-NISHMDLKPQNLLLSSRYNpvLKLADFGFAQHLKPNDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPkwNSVFDQLTQVVKGDPP-QLsnseerefsP 349
Cdd:cd14121  153 AHSLRGSPLYMAPEMI----LKKKYDARVDLWSVGVILYECLFGRAPFA--SRSFEELEEKIRSSKPiEI---------P 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 350 SFINFVNLC-------LTKDESKRPKYKELLKHPF 377
Cdd:cd14121  218 TRPELSADCrdlllrlLQRDPDRRISFEEFFAHPF 252
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
119-377 1.85e-22

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: 95.88  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRS-------SDCPYIVQFYGalFREGDCWICM-- 189
Cdd:cd14093   11 LGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEELREATRREieilrqvSGHPNIIELHD--VFESPTFIFLvf 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTS--FDkfykYVYSVLddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:cd14093   89 ELCRKGelFD----YLTEVV--TLSEKKTRRIMRQLFEAVEFLHSL-NIVHRDLKPENILLDDNLNVKISDFGFATRLDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRPYMAPERI----DPSASrqGYDVRSDVWSLGITLYELATGRFPYpkWNSvfDQ---LTQVVKGDpPQLS 340
Cdd:cd14093  162 GEKLRELCGTPGYLAPEVLkcsmYDNAP--GYGKEVDMWACGVIMYTLLAGCPPF--WHR--KQmvmLRNIMEGK-YEFG 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 341 NSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14093  235 SPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
119-378 2.38e-22

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: 95.20  E-value: 2.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQK------QLLMDLDvvmrssdCPYIVQfYGALFREGDCWICMEL 191
Cdd:cd08223    8 IGKGSYGEVWLVRHKRDRKQYVIKKLNlKNASKRERKaaeqeaKLLSKLK-------HPNIVS-YKESFEGEDGFLYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS--I 269
Cdd:cd08223   80 GFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHER-NILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSsdM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGR--FPYPKWNSVfdqLTQVVKGDPPQLSnseeREF 347
Cdd:cd08223  159 ATTL-IGTPYYMSPELF----SNKPYNHKSDVWALGCCVYEMATLKhaFNAKDMNSL---VYKILEGKLPPMP----KQY 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 348 SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd08223  227 SPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
100-374 2.55e-22

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: 95.95  E-value: 2.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 100 ISPEQHWDFTAEDLKDLGEIGRGAYGSVNK-----MVHKPSGQI-MAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIV 173
Cdd:cd05053    1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKaeavgLDNKPNEVVtVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 174 QFYGALFREGDCWICMELMST----SFDKFYKYV---YSVLDDVIPEEILGKITLAT-----VKALNHLkENLKIIHRDI 241
Cdd:cd05053   81 NLLGACTQDGPLYVVVEYASKgnlrEFLRARRPPgeeASPDDPRVPEEQLTQKDLVSfayqvARGMEYL-ASKKCIHRDL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 242 KPSNILLDRSGNIKLCDFGISGQL--VDSIAKTRDaGCRPY--MAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRF 316
Cdd:cd05053  160 AARNVLVTEDNVMKIADFGLARDIhhIDYYRKTTN-GRLPVkwMAPEALFDRV----YTHQSDVWSFGVLLWEIFTlGGS 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 317 PYP--KWNSVFDQLTQVVKGDPPQLSNSEerefspsFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05053  235 PYPgiPVEELFKLLKEGHRMEKPQNCTQE-------LYMLMRDCWHEVPSQRPTFKQLVE 287
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
110-377 3.72e-22

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: 96.99  E-value: 3.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd05621   51 AEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSFDKFYKYVYSVlddviPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLvDS 268
Cdd:cd05621  131 MEYMPGGDLVNLMSNYDV-----PEKWAKFYTAEVVLALDAI-HSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKM-DE 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTR---DAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKgDPPQLSNSEER 345
Cdd:cd05621  204 TGMVHcdtAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYA-DSLVGTYSKIMD-HKNSLNFPDDV 281
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 346 EFSPSFINFVNLCLTKDESK--RPKYKELLKHPF 377
Cdd:cd05621  282 EISKHAKNLICAFLTDREVRlgRNGVEEIKQHPF 315
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
111-319 4.00e-22

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: 96.14  E-value: 4.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRkSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 E------LMSTSFDKfykyvysvldDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGI-- 261
Cdd:cd05599   81 EflpggdMMTLLMKK----------DTLTEEETRFYIAETVLAIESI-HKLGYIHRDIKPDNLLLDARGHIKLSDFGLct 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 262 ---SGQLVDSIAKTRDagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGrfpYP 319
Cdd:cd05599  150 glkKSHLAYSTVGTPD-----YIAPEVF----LQKGYGKECDWWSLGVIMYEMLIG---YP 198
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
111-375 6.94e-22

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: 94.09  E-value: 6.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLlmdldvvmRSSDCPYIVQFYGALFREGDC--- 185
Cdd:cd14047    6 QDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKlnNEKAEREVKAL--------AKLDHPNIVRYNGCWDGFDYDpet 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 -------------WICME------LMSTSFDKFYKYVYSVLDDVIPEEILgkitlatvKALNHLKENlKIIHRDIKPSNI 246
Cdd:cd14047   78 sssnssrsktkclFIQMEfcekgtLESWIEKRNGEKLDKVLALEIFEQIT--------KGVEYIHSK-KLIHRDLKPSNI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 247 LLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELatgrfpYPKWNSVFD 326
Cdd:cd14047  149 FLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQI----SSQDYGKEVDIYALGLILFEL------LHVCDSAFE 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 526479851 327 Q---LTQVVKGD-PPQLSNSEEREfspsfINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14047  219 KskfWTDLRNGIlPDIFDKRYKIE-----KTIIKKMLSKKPEDRPNASEILRT 266
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
109-377 2.01e-21

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: 94.56  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 109 TAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRST--VDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCW 186
Cdd:cd05610    2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKAdmINKNMVHQVQAERDALALSKS-PFIVHLYYSLQSANNVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS---- 262
Cdd:cd05610   81 LVMEYLIGGDVKSLLHIYGYFD----EEMAVKYISEVALALDYLHRH-GIIHRDLKPDNMLISNEGHIKLTDFGLSkvtl 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 --------------------------GQLVDSIAKTRDAGCRPYMAPERIDPSASR--------------------QGYD 296
Cdd:cd05610  156 nrelnmmdilttpsmakpkndysrtpGQVLSLISSLGFNTPTPYRTPKSVRRGAARvegerilgtpdylapelllgKPHG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 297 VRSDVWSLGITLYELATGRFPY----PKwnSVFDqltQVVKGDPPQlsNSEEREFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05610  236 PAVDWWALGVCLFEFLTGIPPFndetPQ--QVFQ---NILNRDIPW--PEGEEELSVNAQNAIEILLTMDPTKRAGLKEL 308

                 ....*
gi 526479851 373 LKHPF 377
Cdd:cd05610  309 KQHPL 313
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
119-377 2.30e-21

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: 93.14  E-value: 2.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV---NKMVHKPSGQIMAVKRIR-STVDEKEQ--KQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd05613    8 LGTGAYGKVflvRKVSGHDAGKLYAMKVLKkATIVQKAKtaEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLHLILDYI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STS--FDKFYKYVYSVLDDVipEEILGKITLAtvkaLNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVDSI 269
Cdd:cd05613   88 NGGelFTHLSQRERFTENEV--QIYIGEIVLA----LEHLHK-LGIIYRDIKLENILLDSSGHVVLTDFGLSKEfLLDEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRD-AGCRPYMAPERIDPSASrqGYDVRSDVWSLGITLYELATGRFPYP---KWNSVFDQLTQVVKGDPPQlsnseER 345
Cdd:cd05613  161 ERAYSfCGTIEYMAPEIVRGGDS--GHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILKSEPPY-----PQ 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 346 EFSPSFINFVNLCLTKDESKR----PK-YKELLKHPF 377
Cdd:cd05613  234 EMSALAKDIIQRLLMKDPKKRlgcgPNgADEIKKHPF 270
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
119-377 2.32e-21

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: 92.47  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIrstvDEKEQKQLLMDLDV-----VMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd14663    8 LGEGTFAKVKFARNTKTGESVAIKII----DKEQVAREGMVEQIkreiaIMKLLRHPNIVELHEVMATKTKIFFVMELVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TS--FDKFYKyvysvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS----GQLVD 267
Cdd:cd14663   84 GGelFSKIAK------NGRLKEDKARKYFQQLIDAVDYCHSR-GVFHRDLKPENLLLDEDGNLKISDFGLSalseQFRQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRdAGCRPYMAPERIdpsaSRQGYD-VRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGDPPQlsnseERE 346
Cdd:cd14663  157 GLLHTT-CGTPNYVAPEVL----ARRGYDgAKADIWSCGVILFVLLAGYLPFDDEN-LMALYRKIMKGEFEY-----PRW 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14663  226 FSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
116-378 2.59e-21

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: 92.45  E-value: 2.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRstvdekeQKQLLmdLDVVMRSSDC---PYIVQFYGALFREGDCWICMELM 192
Cdd:cd14004    5 LKEMGEGAYGQVNLAIYKSKGKEVVIKFIF-------KERIL--VDTWVRDRKLgtvPLEIHILDTLNKRSHPNIVKLLD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSFDKFYKYVYSV------LDDVIP-----EEILGK-ITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd14004   76 FFEDDEFYYLVMEKhgsgmdLFDFIErkpnmDEKEAKyIFRQVADAVKHLHDQ-GIVHRDIKDENVILDGNGTIKLIDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 iSGQLVDSIAKTRDAGCRPYMAPE--RIDPSASRQgydvrSDVWSLGITLYELATGRFPypkwnsvFDQLTQVVKGDpPQ 338
Cdd:cd14004  155 -SAAYIKSGPFDTFVGTIDYAAPEvlRGNPYGGKE-----QDIWALGVLLYTLVFKENP-------FYNIEEILEAD-LR 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 339 LSNSEEREfspsFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14004  221 IPYAVSED----LIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
119-377 2.63e-21

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: 93.83  E-value: 2.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV---NKMVHKPSGQIMAVKRIRSTV---DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd05614    8 LGTGAYGKVflvRKVSGHDANKLYAMKVLRKAAlvqKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLHLILDYV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STS--FDKFYKYVYSVLDDVipEEILGKITLAtvkaLNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSiA 270
Cdd:cd05614   88 SGGelFTHLYQRDHFSEDEV--RFYSGEIILA----LEHLHK-LGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTE-E 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRD---AGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYP---KWNSVFDQLTQVVKGDPPqlsnsee 344
Cdd:cd05614  160 KERTysfCGTIEYMAPEII---RGKSGHGKAVDWWSLGILMFELLTGASPFTlegEKNTQSEVSRRILKCDPP------- 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 526479851 345 refSPSFINFV-----NLCLTKDESKR----PK-YKELLKHPF 377
Cdd:cd05614  230 ---FPSFIGPVardllQKLLCKDPKKRlgagPQgAQEIKEHPF 269
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
116-377 3.00e-21

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: 93.01  E-value: 3.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRsTVDEKE--------QKQLLMDLDVvmrssdcPYIVQFYgalfregdcwi 187
Cdd:cd07840    4 IAQIGEGTYGQVYKARNKKTGELVALKKIR-MENEKEgfpitairEIKLLQKLDH-------PNVVRLK----------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 cmELM-STSFDKFYKYVYSVLD----DV--IPEEILGKITLATVK--------ALNHLKENlKIIHRDIKPSNILLDRSG 252
Cdd:cd07840   65 --EIVtSKGSAKYKGSIYMVFEymdhDLtgLLDNPEVKFTESQIKcymkqlleGLQYLHSN-GILHRDIKGSNILINNDG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 253 NIKLCDFGisgqLVDSIAKTRDAGCRP------YMAPErIDPSASRQGYDVrsDVWSLGITLYELATGRFPYPKWNSVfD 326
Cdd:cd07840  142 VLKLADFG----LARPYTKENNADYTNrvitlwYRPPE-LLLGATRYGPEV--DMWSVGCILAELFTGKPIFQGKTEL-E 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 327 QLTQVVK--GDP-----PQLSN--------------SEEREF-----SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07840  214 QLEKIFElcGSPteenwPGVSDlpwfenlkpkkpykRRLREVfknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
114-377 4.25e-21

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: 92.34  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR----------STVDEKeqkQLLMDLDvvmrSSDCPYIVQFYG-----A 178
Cdd:cd07838    2 EEVAEIGEGAYGTVYKARDLQDGRFVALKKVRvplseegiplSTIREI---ALLKQLE----SFEHPNVVRLLDvchgpR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 179 LFREGDCWICMELMSTSFDKFYKYVYSvldDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd07838   75 TDRELKLTLVFEHVDQDLATYLDKCPK---PGLPPETIKDLMRQLLRGLDFLHSH-RIVHRDLKPQNILVTSDGQVKLAD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATgRFPYPKWNSVFDQLTQV--VKGDP 336
Cdd:cd07838  151 FGLARIYSFEMALTSVVVTLWYRAPEVL----LQSSYATPVDMWSVGCIFAELFN-RRPLFRGSSEADQLGKIfdVIGLP 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 337 -----PQLSNSEEREFSPSFI---------------NFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07838  226 seeewPRNSALPRSSFPSYTPrpfksfvpeideeglDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
120-373 4.51e-21

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: 91.56  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 120 GRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDvvmrssdcpyIVQFYGALFREGDCWICMELmsTSFDKF 199
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEKEAEILSVLSHRN----------IIQFYGAILEAPNYGIVTEY--ASYGSL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 200 YKYVYSVLDDVIPEEILGKITLATVKALNHLKEN--LKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRdAGC 277
Cdd:cd14060   70 FDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapVKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSL-VGT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 RPYMAPERIdpsasrQGYDVRS--DVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSpsfiNFV 355
Cdd:cd14060  149 FPWMAPEVI------QSLPVSEtcDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPTIPSSCPRSFA----ELM 218
                        250
                 ....*....|....*...
gi 526479851 356 NLCLTKDESKRPKYKELL 373
Cdd:cd14060  219 RRCWEADVKERPSFKQII 236
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
235-378 5.83e-21

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: 91.65  E-value: 5.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK-TRDAGCRPYMAPERIDPsaSRQGYDVRS-DVWSLGITLYELA 312
Cdd:cd14118  135 KIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALlSSTAGTPAFMAPEALSE--SRKKFSGKAlDIWAMGVTLYCFV 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 313 TGRFPYpKWNSVFdQLTQVVKGDPpqLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14118  213 FGRCPF-EDDHIL-GLHEKIKTDP--VVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
114-377 6.84e-21

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: 91.95  E-value: 6.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFRE--GDCWICMEL 191
Cdd:cd07831    2 KILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSPHPNILRLIEVLFDRktGRLALVFEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSfdkfykyVYSVLDD---VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDrSGNIKLCDFGISGQLVDS 268
Cdd:cd07831   82 MDMN-------LYELIKGrkrPLPEKRVKNYMYQLLKSLDHMHRN-GIFHRDIKPENILIK-DDILKLADFGSCRGIYSK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQV--VKGDPPQ-----LSN 341
Cdd:cd07831  153 PPYTEYISTRWYRAPECLLTDGY---YGPKMDIWAVGCVFFEILSLFPLFPGTNEL-DQIAKIhdVLGTPDAevlkkFRK 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 526479851 342 SEEREF-----------------SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07831  229 SRHMNYnfpskkgtglrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
118-379 7.24e-21

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: 92.78  E-value: 7.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrstvdEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd14176   26 DIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfykyvySVLDDVIPEEILGK-----ITLATVKALNHLKENlKIIHRDIKPSNIL-LDRSGN---IKLCDFGISGQL-VD 267
Cdd:cd14176   99 -------ELLDKILRQKFFSEreasaVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLrAE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKW-NSVFDQLTQVVKGDPPQLSNSEERE 346
Cdd:cd14176  171 NGLLMTPCYTANFVAPEVL----ERQGYDAACDIWSLGVLLYTMLTGYTPFANGpDDTPEEILARIGSGKFSLSGGYWNS 246
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd14176  247 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIV 279
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
118-378 7.36e-21

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: 91.29  E-value: 7.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIrstvdekEQKQLLMDLDVV------MRSSDCPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14078   10 TIGSGGFAKVKLATHILTGEKVAIKIM-------DKKALGDDLPRVkteieaLKNLSHQHICRLYHVIETDNKIFMVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTS--FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIsgqlvdsI 269
Cdd:cd14078   83 CPGGelFD------YIVAKDRLSEDEARVFFRQIVSAVAYV-HSQGYAHRDLKPENLLLDEDQNLKLIDFGL-------C 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDA---------GCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSV--FDQLTQVVKGDPPQ 338
Cdd:cd14078  149 AKPKGGmdhhletccGSPAYAAPELI---QGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMalYRKIQSGKYEEPEW 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 339 LsnseerefSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14078  226 L--------SPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
119-318 7.85e-21

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: 92.63  E-value: 7.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSS--DCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLskKVIVAKKEVAHTIGERNILVRTAldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdkfyKYVYSVLDDVIPEEILGKITLAT-VKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS-GQLVDSIAKT 272
Cdd:cd05586   81 G-----ELFWHLQKEGRFSEDRAKFYIAElVLALEHLHKN-DIVYRDLKPENILLDANGHIALCDFGLSkADLTDNKTTN 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 526479851 273 RDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05586  155 TFCGTTEYLAPEVL---LDEKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
119-378 8.49e-21

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: 91.63  E-value: 8.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQkqllmdLDVVMRSSDCPYIVQFYGaLFREGD-CWICMELMSTSf 196
Cdd:cd14175    9 IGVGSYSVCKRCVHKATNMEYAVKVIdKSKRDPSEE------IEILLRYGQHPNIITLKD-VYDDGKhVYLVTELMRGG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 dkfykyvySVLDDVIPEEILGKITLATV-----KALNHLKENlKIIHRDIKPSNIL-LDRSGN---IKLCDFGISGQL-V 266
Cdd:cd14175   81 --------ELLDKILRQKFFSEREASSVlhticKTVEYLHSQ-GVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLrA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPkwNSVFDQLTQV---VKGDPPQLSNSE 343
Cdd:cd14175  152 ENGLLMTPCYTANFVAPEVL----KRQGYDEGCDIWSLGILLYTMLAGYTPFA--NGPSDTPEEIltrIGSGKFTLSGGN 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 344 EREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14175  226 WNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWI 260
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
116-387 9.54e-21

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: 92.31  E-value: 9.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRG--AYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd08227    3 LTVIGRGfeDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKfyKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSG---------NIKLCDFGISGQ 264
Cdd:cd08227   83 YGSAK--DLICTHFMDGMSELAIAYILQGVLKALDYI-HHMGYVHRSVKASHILISVDGkvylsglrsNLSMINHGQRLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKtRDAGCRPYMAPERIDPSAsrQGYDVRSDVWSLGITLYELATGRFPY---PKWNSVFDQLTQVVK-------- 333
Cdd:cd08227  160 VVHDFPK-YSVKVLPWLSPEVLQQNL--QGYDAKSDIYSVGITACELANGHVPFkdmPATQMLLEKLNGTVPclldttti 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 334 ------------------GDPPQLSNSE-----------EREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEER 384
Cdd:cd08227  237 paeeltmkpsrsgansglGESTTVSTPRpsngessshpyNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRR 316

                 ...
gi 526479851 385 AVE 387
Cdd:cd08227  317 ASE 319
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
112-377 1.08e-20

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: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEK--EQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05600   12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKlnEVNHVLTERDI-LTTTNSPWLVKLLYAFQDPENVYLAM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 E---------LMSTS------FDKFYkyvysvlddvIPEEILgkitlatvkALNHLKEnLKIIHRDIKPSNILLDRSGNI 254
Cdd:cd05600   91 EyvpggdfrtLLNNSgilseeHARFY----------IAEMFA---------AISSLHQ-LGYIHRDLKPENFLIDSSGHI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFG-----ISGQLVDSIAKTRDA---------------------------------GCRPYMAPERIDPsasrQGYD 296
Cdd:cd05600  151 KLTDFGlasgtLSPKKIESMKIRLEEvkntafleltakerrniyramrkedqnyansvvGSPDYMAPEVLRG----EGYD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 297 VRSDVWSLGITLYELATGrfpYPKW-----NSVFDQL---TQVVKGdPPQLSNSEEREFSPSFINFVNLCLTKDESKRPK 368
Cdd:cd05600  227 LTVDYWSLGCILFECLVG---FPPFsgstpNETWANLyhwKKTLQR-PVYTDPDLEFNLSDEAWDLITKLITDPQDRLQS 302

                 ....*....
gi 526479851 369 YKELLKHPF 377
Cdd:cd05600  303 PEQIKNHPF 311
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
110-372 1.25e-20

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: 90.94  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGE-IGRGAYGSVNKMV-HKPSGQIMAVK-RIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGaLFREGDCW 186
Cdd:cd05056    4 QREDITLGRcIGEGQFGDVYQGVyMSPENEKIAVAvKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIG-VITENPVW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSFDKFYKYVYSvldDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd05056   83 IVMELAPLGELRSYLQVNK---YSLDLASLILYAYQLSTALAYL-ESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYME 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRP--YMAPERIDpsaSRQgYDVRSDVWSLGITLYE-LATGRFPYpKWNSVFDQLTQVVKGD-PPQLSNS 342
Cdd:cd05056  159 DESYYKASKGKLPikWMAPESIN---FRR-FTSASDVWMFGVCMWEiLMLGVKPF-QGVKNNDVIGRIENGErLPMPPNC 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 343 eerefSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05056  234 -----PPTLYSLMTKCWAYDPSKRPRFTEL 258
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
118-378 1.35e-20

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: 90.75  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQK-QLLMDLDVVMRSSDCPYIVQFYGALfrEGDCWICMELMSTSF 196
Cdd:cd14198   15 ELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRaEILHEIAVLELAKSNPRVVNLHEVY--ETTSEIILILEYAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRS---GNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd14198   93 GEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQN-NIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHACELRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIDpsasrqgYD---VRSDVWSLGITLYELATGRFPYPKWNS--VFDQLTQVvkgdppQLSNSEE--RE 346
Cdd:cd14198  172 IMGTPEYLAPEILN-------YDpitTATDMWNIGVIAYMLLTHESPFVGEDNqeTFLNISQV------NVDYSEEtfSS 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14198  239 VSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
119-378 1.38e-20

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: 91.85  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI----RSTVDEKEQKQLLMDLDVVmrsSDCPYIVQFYGALFREG--DCWICMELM 192
Cdd:cd07852   15 LGKGAYGIVWKAIDKKTGEVVALKKIfdafRNATDAQRTFREIMFLQEL---NDHPNIIKLLNVIRAENdkDIYLVFEYM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSfdkfykyvysvLDDVIPEEILGK-----ITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGisgqLVD 267
Cdd:cd07852   92 ETD-----------LHAVIRANILEDihkqyIMYQLLKALKYLHSG-GVIHRDLKPSNILLNSDCRVKLADFG----LAR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRP----------YMAPERIdpSASRQgYDVRSDVWSLGITLYELATGR--FPypkWNSVFDQLTQVVKGD 335
Cdd:cd07852  156 SLSQLEEDDENPvltdyvatrwYRAPEIL--LGSTR-YTKGVDMWSVGCILGEMLLGKplFP---GTSTLNQLEKIIEVI 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 336 PP-------------------QLSNSEEREF-------SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd07852  230 GRpsaediesiqspfaatmleSLPPSRPKSLdelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYV 298
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
106-375 1.67e-20

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk 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: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 90.04  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVnkMVHKPSGQIMAVKRIRSTVdekeQKQLLMDLDVVMRSSDCPYIVQFYGALFRE-GD 184
Cdd:cd05082    1 WALNMKELKLLQTIGKGEFGDV--MLGDYRGNKVAVKCIKNDA----TAQAFLAEASVMTQLRHSNLVQLLGVIVEEkGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGisgq 264
Cdd:cd05082   75 LYIVTEYMAKG--SLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGN-NFVHRDLAARNVLVSEDNVAKVSDFG---- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYPK--WNSVFDQLTQVVKGDPPQl 339
Cdd:cd05082  148 LTKEASSTQDTGKLPvkWTAPEAL----REKKFSTKSDVWSFGILLWEIYSfGRVPYPRipLKDVVPRVEKGYKMDAPD- 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 340 snseerEFSPSFINFVNLCLTKDESKRPKY---KELLKH 375
Cdd:cd05082  223 ------GCPPAVYDVMKNCWHLDAAMRPSFlqlREQLEH 255
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
113-372 2.04e-20

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: 90.55  E-value: 2.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 113 LKDLGEIGRGAYGSVNKMVHKPSG---QI-MAVKRIRSTVDEKEQKQLLmDLDVVMRSSDCPYIVQFYGalfregdcwIC 188
Cdd:cd05057    9 LEKGKVLGSGAFGTVYKGVWIPEGekvKIpVAIKVLREETGPKANEEIL-DEAYVMASVDHPHLVRLLG---------IC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 M--------ELMStsFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd05057   79 LssqvqlitQLMP--LGCLLDYVRNHRDNIGSQLLL-NWCVQIAKGMSYLEEK-RLVHRDLAARNVLVKTPNHVKITDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQL-VDSIAKTRDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNSVfdqltqvvkgDP 336
Cdd:cd05057  155 LAKLLdVDEKEYHAEGGKVPikWMALESI----QYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAV----------EI 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 337 PQLSNSEEREFSPSfINFVNL------CLTKDESKRPKYKEL 372
Cdd:cd05057  221 PDLLEKGERLPQPP-ICTIDVymvlvkCWMIDAESRPTFKEL 261
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
116-378 2.10e-20

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: 90.02  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME----- 190
Cdd:cd08225    5 IKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEycdgg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 -LMStSFDKFYKYVYSvlddviPEEILG---KITLAtvkaLNHLKENlKIIHRDIKPSNILLDRSGNI-KLCDFGISGQL 265
Cdd:cd08225   85 dLMK-RINRQRGVLFS------EDQILSwfvQISLG----LKHIHDR-KILHRDIKSQNIFLSKNGMVaKLGDFGIARQL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRD-AGCRPYMAPEridpSASRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKGDPPQLSNSEE 344
Cdd:cd08225  153 NDSMELAYTcVGTPYYLSPE----ICQNRPYNNKTDIWSLGCVLYELCTLKHPF-EGNNLHQLVLKICQGYFAPISPNFS 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 345 REFSpSFINFVNLCLTKDeskRPKYKELLKHPFI 378
Cdd:cd08225  228 RDLR-SLISQLFKVSPRD---RPSITSILKRPFL 257
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
110-377 2.18e-20

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: 92.38  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd05622   72 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSfdkfyKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-VD 267
Cdd:cd05622  152 MEYMPGG-----DLVNLMSNYDVPEKWARFYTAEVVLALDAI-HSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnKE 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDA-GCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKgDPPQLSNSEERE 346
Cdd:cd05622  226 GMVRCDTAvGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTYSKIMN-HKNSLTFPDDND 303
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 347 FSPSFINFVNLCLTKDESK--RPKYKELLKHPF 377
Cdd:cd05622  304 ISKEAKNLICAFLTDREVRlgRNGVEEIKRHLF 336
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
112-376 2.22e-20

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: 90.82  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDlGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLmdldvvmrsSDC---PYIVQFYGALFREGDCWIC 188
Cdd:cd14092    8 DLRE-EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREVQLL---------RLCqghPNIVKLHEVFQDELHTYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMS-----------TSFDkfykyvysvlddvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL---DRSGNI 254
Cdd:cd14092   78 MELLRggellerirkkKRFT---------------ESEASRIMRQLVSAVSFMHSK-GVVHRDLKPENLLFtdeDDDAEI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPY---PKWNSVFDQLTQV 331
Cdd:cd14092  142 KIVDFGFARLKPENQPLKTPCFTLPYAAPEVLKQALSTQGYDESCDLWSLGVILYTMLSGQVPFqspSRNESAAEIMKRI 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 332 VKGDpPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14092  222 KSGD-FSFDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHP 265
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
119-318 2.32e-20

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: 89.50  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14072    8 IGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGevF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DkfykyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAG 276
Cdd:cd14072   88 D------YLVAHGRMKEKEARAKFRQIVSAVQYCHQK-RIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFCG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 277 CRPYMAPERIdpsasrQG--YD-VRSDVWSLGITLYELATGRFPY 318
Cdd:cd14072  161 SPPYAAPELF------QGkkYDgPEVDVWSLGVILYTLVSGSLPF 199
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
119-318 3.06e-20

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: 89.96  E-value: 3.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE--QKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd05607   10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKsgEKMALLEKEILEKVNS-PFIVSLAYAFETKTHLCLVMSLMNGGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYkyVYSVLDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAG 276
Cdd:cd05607   89 LKYH--IYNVGERGIEMERVIFYSAQITCGILHLHS-LKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQRAG 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 526479851 277 CRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05607  166 TNGYMAPEIL----KEESYSYPVDWFAMGCSIYEMVAGRTPF 203
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
110-381 4.03e-20

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: 90.44  E-value: 4.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI----RSTVDEKEQKQLlmdldVVMRSSDCPYIVQFYGAL------ 179
Cdd:cd07849    4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfeHQTYCLRTLREI-----KILLRFKHENIIGILDIQrpptfe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 -FRegDCWICMELMSTSFdkfYKYVYS--VLDDVIPEEILGkiTLATVKALNhlkeNLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd07849   79 sFK--DVYIVQELMETDL---YKLIKTqhLSNDHIQYFLYQ--ILRGLKYIH----SANVLHRDLKPSNLLLNTNCDLKI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGI----------SGQLVDSIAKtrdagcRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGR--FPypkWNSV 324
Cdd:cd07849  148 CDFGLariadpehdhTGFLTEYVAT------RWYRAPEIM---LNSKGYTKAIDIWSVGCILAEMLSNRplFP---GKDY 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 325 FDQLTQV--VKGDPPQ-----LSNSEEREF-------------------SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd07849  216 LHQLNLIlgILGTPSQedlncIISLKARNYikslpfkpkvpwnklfpnaDPKALDLLDKMLTFNPHKRITVEEALAHPYL 295

                 ...
gi 526479851 379 LMY 381
Cdd:cd07849  296 EQY 298
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
119-318 4.84e-20

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: 88.32  E-value: 4.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVnkMVHKPSGQIMAVKRIRstvDEKEQ--KQLlmdldvvmRSSDCPYIVQFYGALfREGDCW-ICMELMSts 195
Cdd:cd14059    1 LGSGAQGAV--FLGKFRGEEVAVKKVR---DEKETdiKHL--------RKLNHPNIIKFKGVC-TQAPCYcILMEYCP-- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdkfYKYVYSVLDD--VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd14059   65 ----YGQLYEVLRAgrEITPSLLVDWSKQIASGMNYLHLH-KIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMS 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 274 DAGCRPYMAPE--RIDPSASrqgydvRSDVWSLGITLYELATGRFPY 318
Cdd:cd14059  140 FAGTVAWMAPEviRNEPCSE------KVDIWSFGVVLWELLTGEIPY 180
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
116-333 5.02e-20

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: 89.28  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd07848    6 LGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FdkfYKYVYSVLDDVIPEEILGKItLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD--SIAKTR 273
Cdd:cd07848   86 M---LELLEEMPNGVPPEKVRSYI-YQLIKAIHWCHKN-DIVHRDIKPENLLISHNDVLKLCDFGFARNLSEgsNANYTE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK 333
Cdd:cd07848  161 YVATRWYRSPELLLGAP----YGKAVDMWSVGCILGELSDGQPLFPG-ESEIDQLFTIQK 215
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
119-374 5.74e-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: 88.66  E-value: 5.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTvDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfdK 198
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGG--S 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 FYKYVYSVLDDVIPEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDaGCR 278
Cdd:cd05041   80 LLTFLRKKGARLTVKQLL-QMCLDAAAGMEYL-ESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSD-GLK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 279 ----PYMAPEridpsASRQG-YDVRSDVWSLGITLYELAT-GRFPYPKWNSVfDQLTQVVKG---DPPQLSNSEEREfsp 349
Cdd:cd05041  157 qipiKWTAPE-----ALNYGrYTSESDVWSFGILLWEIFSlGATPYPGMSNQ-QTREQIESGyrmPAPELCPEAVYR--- 227
                        250       260
                 ....*....|....*....|....*
gi 526479851 350 sfinFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05041  228 ----LMLQCWAYDPENRPSFSEIYN 248
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
119-335 6.08e-20

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: 89.00  E-value: 6.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQ-KQLLMDLDVvMRSSDCPYIVQFYGALfrEGDCWICMeLMstsf 196
Cdd:cd05609    8 ISNGAYGAVYLVRHRETRQRFAMKKInKQNLILRNQiQQVFVERDI-LTFAENPFVVSMYCSF--ETKRHLCM-VM---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 dkfyKYV-----YSVLDDV--IPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd05609   80 ----EYVeggdcATLLKNIgpLPVDMARMYFAETVLALEYL-HSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKT-------RDA---------GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK 333
Cdd:cd05609  155 TTNlyeghieKDTrefldkqvcGTPEYIAPEVI----LRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEELFGQVIS 229

                 ..
gi 526479851 334 GD 335
Cdd:cd05609  230 DE 231
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
170-318 7.25e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 91.40  E-value: 7.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 170 PYIVQFY--GAlfrEGDC-WICMElmstsfdkfykYVY-SVLDDVIPEEilGKITLATV--------KALNHLKENlKII 237
Cdd:NF033483  67 PNIVSVYdvGE---DGGIpYIVME-----------YVDgRTLKDYIREH--GPLSPEEAveimiqilSALEHAHRN-GIV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 238 HRDIKPSNILLDRSGNIKLCDFGI----SGQlvdSIAKTRDA-GCRPYMAPERIdpsasRQGY-DVRSDVWSLGITLYEL 311
Cdd:NF033483 130 HRDIKPQNILITKDGRVKVTDFGIaralSST---TMTQTNSVlGTVHYLSPEQA-----RGGTvDARSDIYSLGIVLYEM 201

                 ....*..
gi 526479851 312 ATGRFPY 318
Cdd:NF033483 202 LTGRPPF 208
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
118-382 7.26e-20

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: 89.30  E-value: 7.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQkqllmdLDVVMRSSDCPYIVQFYGaLFREGD-CWICMELMSTS 195
Cdd:cd14178   10 DIGIGSYSVCKRCVHKATSTEYAVKIIdKSKRDPSEE------IEILLRYGQHPNIITLKD-VYDDGKfVYLVMELMRGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdkfykyvySVLDDVIPEEILGKITLATV-----KALNHLKENlKIIHRDIKPSNIL-LDRSGN---IKLCDFGISGQL- 265
Cdd:cd14178   83 ---------ELLDRILRQKCFSEREASAVlctitKTVEYLHSQ-GVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLr 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKW-NSVFDQLTQVVKGDPPQLSNSEE 344
Cdd:cd14178  153 AENGLLMTPCYTANFVAPEVL----KRQGYDAACDIWSLGILLYTMLAGFTPFANGpDDTPEEILARIGSGKYALSGGNW 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 526479851 345 REFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYE 382
Cdd:cd14178  229 DSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNRE 266
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
119-377 7.85e-20

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: 89.58  E-value: 7.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRstvdekeqKQLLMDLD----------VVMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKVLK--------KEVIIEDDdvectmtekrVLALANRHPFLTGLHACFQTEDRLYFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 ME------LM-----STSFD----KFYKyvysvlddvipeeilGKITLAtvkaLNHLKENlKIIHRDIKPSNILLDRSGN 253
Cdd:cd05570   75 MEyvnggdLMfhiqrARRFTeeraRFYA---------------AEICLA----LQFLHER-GIIYRDLKLDNVLLDAEGH 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 254 IKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVV 332
Cdd:cd05570  135 IKIADFGMCKEGIWGGNTTSTfCGTPDYIAPEIL----REQDYGFSVDWWALGVLLYEMLAGQSPFEGDDE--DELFEAI 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 333 KGDPPQLSNSeereFSPSFINFVNLCLTKDESKR----PKYK-ELLKHPF 377
Cdd:cd05570  209 LNDEVLYPRW----LSREAVSILKGLLTKDPARRlgcgPKGEaDIKAHPF 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
119-378 8.71e-20

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: 88.01  E-value: 8.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVN--KMVHKPSGQIMAVKRIRSTVDEKE--QKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14080    8 IGEGSYSKVKlaEYTKSGLKEKVACKIIDKKKAPKDflEKFLPRELEILRKLRH-PNIIQVYSIFERGSKVFIFMEYAEH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdkfykyvySVLDDV-----IPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS- 268
Cdd:cd14080   87 G---------DLLEYIqkrgaLSESQARIWFRQLALAVQYLHS-LDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDd 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 ---IAKTRdAGCRPYMAPERIdpsasrQG--YDVR-SDVWSLGITLYELATGRFPYPKWNsvfdqLTQVVKgdpPQLSN- 341
Cdd:cd14080  157 gdvLSKTF-CGSAAYAAPEIL------QGipYDPKkYDIWSLGVILYIMLCGSMPFDDSN-----IKKMLK---DQQNRk 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 526479851 342 ----SEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14080  222 vrfpSSVKKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
110-318 1.36e-19

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: 89.36  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-------RSTV----DEKEqkqllmdldvVMRSSDCPYIVQFYGA 178
Cdd:cd05596   25 AEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLskfemikRSDSaffwEERD----------IMAHANSEWIVQLHYA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 179 lFREGdcwicmelmstsfdkfyKYVYSVLDDV-------------IPEEILGKITLATVKALNHLkENLKIIHRDIKPSN 245
Cdd:cd05596   95 -FQDD-----------------KYLYMVMDYMpggdlvnlmsnydVPEKWARFYTAEVVLALDAI-HSMGFVHRDVKPDN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 246 ILLDRSGNIKLCDFGI------SGQLV-DSIAKTRDagcrpYMAPERIDpSASRQGYDVRS-DVWSLGITLYELATGRFP 317
Cdd:cd05596  156 MLLDASGHLKLADFGTcmkmdkDGLVRsDTAVGTPD-----YISPEVLK-SQGGDGVYGREcDWWSVGVFLYEMLVGDTP 229

                 .
gi 526479851 318 Y 318
Cdd:cd05596  230 F 230
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
119-313 1.44e-19

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: 87.86  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHK-PSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSD--CPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14052    8 IGSGEFSQVYKVSERvPTGKVYAVKKLKpNYAGAKDRLRRLEEVSILRELTLdgHDNIVQLIDSWEYHGHLYIQTELCEN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 -SFDKFYKYV--YSVLDDVIPEEILGKITLAtvkaLNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14052   88 gSLDVFLSELglLGRLDEFRVWKILVELSLG----LRFI-HDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLIRGI 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 526479851 272 TRDaGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT 313
Cdd:cd14052  163 ERE-GDREYIAPEIL----SEHMYDKPADIFSLGLILLEAAA 199
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
106-373 1.81e-19

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: 87.78  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHK--PSGQI---MAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALF 180
Cdd:cd05032    1 WELPREKITLIRELGQGSFGMVYEGLAKgvVKGEPetrVAIKTVNENASMRERIEFLNEASV-MKEFNCHHVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REGDCWICMELMSTSFDKFY------KYVYSVLDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNI 254
Cdd:cd05032   80 TGQPTLVVMELMAKGDLKSYlrsrrpEAENNPGLGPPTLQKFIQMAAEIADGMAYLAA-KKFVHRDLAARNCMVAEDLTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGIsgqlvdsiakTRDAGCRPY-------------MAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP- 319
Cdd:cd05032  159 KIGDFGM----------TRDIYETDYyrkggkgllpvrwMAPE----SLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQg 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 320 KWNsvfDQLTQVVKG----DPPqlsnseerEFSPSFI-NFVNLCLTKDESKRPKYKELL 373
Cdd:cd05032  225 LSN---EEVLKFVIDgghlDLP--------ENCPDKLlELMRMCWQYNPKMRPTFLEIV 272
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
119-377 1.85e-19

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: 88.40  E-value: 1.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRST--VDEKEQKQLLMDLDVVMRSsDCPYIV----------QFY--------GA 178
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAhiVSRSEVTHTLAERTVLAQV-DCPFIVplkfsfqspeKLYlvlafingGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 179 LF----REGDcwicmelMSTSFDKFYkyvysvlddvipeeilgkiTLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNI 254
Cdd:cd05585   81 LFhhlqREGR-------FDLSRARFY-------------------TAELLCALECLHK-FNVIYRDLKPENILLDYTGHI 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVK 333
Cdd:cd05585  134 ALCDFGLCKLNMKDDDKTNTfCGTPEYLAPELL----LGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENT--NEMYRKIL 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 334 GDPPQLSNSEEREFSPSFINFvnlcLTKDESKRPKY---KELLKHPF 377
Cdd:cd05585  208 QEPLRFPDGFDRDAKDLLIGL----LNRDPTKRLGYngaQEIKNHPF 250
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
119-372 2.04e-19

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 87.16  E-value: 2.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRST-VDEKEQKQLLMDLDVvMRSSDCPYIVQFYGAlfregdC----WICMELMS 193
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWKTWLAIKCPPSLhVDDSERMELLEEAKK-MEMAKFRHILPVYGI------CsepvGLVMEYME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 T-SFDKFykyvysVLDDVIPEEILGKITLATVKALNHLKE-NLKIIHRDIKPSNILLDRSGNIKLCDFGIS--GQLVDSI 269
Cdd:cd14025   77 TgSLEKL------LASEPLPWELRFRIIHETAVGMNFLHCmKPPLLHLDLKPANILLDAHYHVKISDFGLAkwNGLSHSH 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCR--PYMAPERIdpSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSN-SEERE 346
Cdd:cd14025  151 DLSRDGLRGtiAYLPPERF--KEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRPSLSPiPRQRP 228
                        250       260
                 ....*....|....*....|....*..
gi 526479851 347 FSPS-FINFVNLCLTKDESKRPKYKEL 372
Cdd:cd14025  229 SECQqMICLMKRCWDQDPRKRPTFQDI 255
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
116-342 2.08e-19

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: 86.93  E-value: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKpSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDC-PYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14161    8 LETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNhPHIISVYEVFENSSKIVIVMEYASR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdKFYKYV--YSVLDDVIPEEILGKItlatVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-VDSIAK 271
Cdd:cd14161   87 G--DLYDYIseRQRLSELEARHFFRQI----VSAVHYCHAN-GIVHRDLKLENILLDANGNIKIADFGLSNLYnQDKFLQ 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 272 TRdAGCRPYMAPERIDPSASRqGYDVrsDVWSLGITLYELATGRFPYP--KWNSVFDQLTQVVKGDPPQLSNS 342
Cdd:cd14161  160 TY-CGSPLYASPEIVNGRPYI-GPEV--DSWSLGVLLYILVHGTMPFDghDYKILVKQISSGAYREPTKPSDA 228
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
119-377 2.82e-19

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: 87.35  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKIRlETEDEGVPSTAIREISLLKELNH-PNIVRLLDVVHSENKLYLVFEFLDLDLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KfykYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-VDSIAKTRDAG 276
Cdd:cd07835   86 K---YMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSH-RVLHRDLKPQNLLIDTEGALKLADFGLARAFgVPVRTYTHEVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 277 CRPYMAPERIdpSASRQgYDVRSDVWSLGITLYELATGR--FPypkWNSVFDQLTQVVK--GDP---------------- 336
Cdd:cd07835  162 TLWYRAPEIL--LGSKH-YSTPVDIWSVGCIFAEMVTRRplFP---GDSEIDQLFRIFRtlGTPdedvwpgvtslpdykp 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 337 --PQLSNSEEREFSPSF----INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07835  236 tfPKWARQDLSKVVPSLdedgLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
111-356 3.17e-19

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: 88.91  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR--------STVDEKEQKQLLMDldvvmrsSDCPYIVQFYGALFRE 182
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNkwemlkraETACFREERNVLVN-------GDCQWITTLHYAFQDE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 183 GDCWICMEL-----MSTSFDKFykyvysvlDDVIPEEI----LGKITLATvkalnHLKENLKIIHRDIKPSNILLDRSGN 253
Cdd:cd05624  145 NYLYLVMDYyvggdLLTLLSKF--------EDKLPEDMarfyIGEMVLAI-----HSIHQLHYVHRDIKPDNVLLDMNGH 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 254 IKLCDFGISGQLVD--SIAKTRDAGCRPYMAPERIDPSASRQG-YDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQ 330
Cdd:cd05624  212 IRLADFGSCLKMNDdgTVQSSVAVGTPDYISPEILQAMEDGMGkYGPECDWWSLGVCMYEMLYGETPFYA-ESLVETYGK 290
                        250       260
                 ....*....|....*....|....*.
gi 526479851 331 VVkgdppqlsNSEEREFSPSFINFVN 356
Cdd:cd05624  291 IM--------NHEERFQFPSHVTDVS 308
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-373 3.41e-19

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: 86.57  E-value: 3.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIR----STVDEKEQKQLlmdldVVMRSSDCPYIVQFYGALFREGDCWICME---- 190
Cdd:cd08219    8 VGEGSFGRALLVQHVNSDQKYAMKEIRlpksSSAVEDSRKEA-----VLLAKMKHPNIVAFKESFEADGHLYIVMEycdg 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 --LMSTSFDKFYKyvysvlddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS 268
Cdd:cd08219   83 gdLMQKIKLQRGK--------LFPEDTILQWFVQMCLGVQHIHEK-RVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKG--DPPQLSNSEERE 346
Cdd:cd08219  154 GAYACTYVGTPYYVPPEI---WENMPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGsyKPLPSHYSYELR 229
                        250       260
                 ....*....|....*....|....*..
gi 526479851 347 FspsfinFVNLCLTKDESKRPKYKELL 373
Cdd:cd08219  230 S------LIKQMFKRNPRSRPSATTIL 250
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
116-377 3.92e-19

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: 86.17  E-value: 3.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGE-IGRGAYGSVNKMVHKPSGQIMAVKRIrstvDEKEQKQLLMDLDV-----VMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd14079    6 LGKtLGVGSFGKVKLAEHELTGHKVAVKIL----NRQKIKSLDMEEKIrreiqILKLFRHPHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTS--FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:cd14079   82 EYVSGGelFD------YIVQKGRLSEDEARRFFQQIISGVEYCHRH-MVVHRDLKPENLLLDSNMNVKIADFGLSNIMRD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 -SIAKTrDAGCRPYMAPERIDpSASRQGYDVrsDVWSLGITLYELATGRFPYPKWN--SVFDQLTQVVKGDPPQLsnsee 344
Cdd:cd14079  155 gEFLKT-SCGSPNYAAPEVIS-GKLYAGPEV--DVWSCGVILYALLCGSLPFDDEHipNLFKKIKSGIYTIPSHL----- 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 345 refSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14079  226 ---SPGARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
119-374 5.01e-19

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: 86.02  E-value: 5.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIrstvDEKEQKQ---LLMDLDV---VMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVI----DKKKAKKdsyVTKNLRRegrIQQMIRHPNITQLLDILETENSYYLVMELC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STS--FDKFYKyvysvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS---GQLVD 267
Cdd:cd14070   86 PGGnlMHRIYD------KKRLEEREARRYIRQLVSAVEHLHRA-GVVHRDLKIENLLLDENDNIKLIDFGLSncaGILGY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQ-VVKGD----PPQLsns 342
Cdd:cd14070  159 SDPFSTQCGSPAYAAPELL----ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQkMVDKEmnplPTDL--- 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 343 eerefSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14070  232 -----SPGAISFLRSLLEPDPLKRPNIKQALA 258
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
119-378 5.54e-19

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: 87.45  E-value: 5.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTvdEKEQKQLLMDLDVV--MRSSD---CPYIVQ----FYgalFREGDCwICM 189
Cdd:cd14225   51 IGKGSFGQVVKALDHKTNEHVAIKIIRNK--KRFHHQALVEVKILdaLRRKDrdnSHNVIHmkeyFY---FRNHLC-ITF 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSFDKFYK----YVYSVlddvipeEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSG--NIKLCDFGIS- 262
Cdd:cd14225  125 ELLGMNLYELIKknnfQGFSL-------SLIRRFAISLLQCLRLLYRE-RIIHCDLKPENILLRQRGqsSIKVIDFGSSc 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 --GQLVDSIAKTRDagcrpYMAPERIdpsasrQG--YDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVV------ 332
Cdd:cd14225  197 yeHQRVYTYIQSRF-----YRSPEVI------LGlpYSMAIDMWSLGCILAELYTGYPLFPGENEV-EQLACIMevlglp 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 333 -----------------KGDPPQLSNSEEREFSPS--------------FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14225  265 ppelienaqrrrlffdsKGNPRCITNSKGKKRRPNskdlasalktsdplFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
111-318 8.63e-19

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: 86.63  E-value: 8.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-------RSTVDE-KEQKqllmdlDVVMRSsDCPYIVQFYGALFRE 182
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILnkwemlkRAETACfREER------DVLVNG-DRRWITKLHYAFQDE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 183 GDCWICMEL-----MSTSFDKFykyvysvlDDVIPEEILgKITLA-TVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05597   74 NYLYLVMDYycggdLLTLLSKF--------EDRLPEEMA-RFYLAeMVLAIDSIHQ-LGYVHRDIKPDNVLLDRNGHIRL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 257 CDFGI------SGQLVDSIAktrdAGCRPYMAPERIDPSASRQG-YDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05597  144 ADFGSclklreDGTVQSSVA----VGTPDYISPEILQAMEDGKGrYGPECDWWSLGVCMYEMLYGETPF 208
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
111-318 9.21e-19

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: 87.38  E-value: 9.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDLDVVMrSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd05623   72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNkwEMLKRAETACFREERDVLV-NGDSQWITTLHYAFQDDNNLYLV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MEL-----MSTSFDKFykyvysvlDDVIPEEiLGKITLA-TVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd05623  151 MDYyvggdLLTLLSKF--------EDRLPED-MARFYLAeMVLAIDSVHQ-LHYVHRDIKPDNILMDMNGHIRLADFGSC 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 263 GQLVD--SIAKTRDAGCRPYMAPERIDPSASRQG-YDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05623  221 LKLMEdgTVQSSVAVGTPDYISPEILQAMEDGKGkYGPECDWWSLGVCMYEMLYGETPF 279
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
211-378 9.33e-19

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; 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 three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 85.29  E-value: 9.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 211 IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAKTRDaGCRPYMAPERIdps 289
Cdd:cd14101  105 LDESLARRFFKQVVEAVQHCHSK-GVVHRDIKDENILVDlRTGDIKLIDFGSGATLKDSMYTDFD-GTRVYSPPEWI--- 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 290 aSRQGYD-VRSDVWSLGITLYELATGRFPypkwnsvFDQLTQVVKGDPpqlsnSEEREFSPSFINFVNLCLTKDESKRPK 368
Cdd:cd14101  180 -LYHQYHaLPATVWSLGILLYDMVCGDIP-------FERDTDILKAKP-----SFNKRVSNDCRSLIRSCLAYNPSDRPS 246
                        170
                 ....*....|
gi 526479851 369 YKELLKHPFI 378
Cdd:cd14101  247 LEQILLHPWM 256
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
114-377 1.10e-18

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: 86.54  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVV--MRSSDCPYIVQFYGA---LFREGDCWI 187
Cdd:cd07880   18 RDLKQVGSGAYGTVCSALDRRTGAKVAIKKLyRPFQSELFAKRAYRELRLLkhMKHENVIGLLDVFTPdlsLDRFHDFYL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFDKFYKYvysvldDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQlVD 267
Cdd:cd07880   98 VMPFMGTDLGKLMKH------EKLSEDRIQFLVYQMLKGLKYI-HAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ-TD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SiAKTRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRfPYPKWNSVFDQLTQVVK--GDPPQ-----LS 340
Cdd:cd07880  170 S-EMTGYVVTRWYRAPEVI---LNWMHYTQTVDIWSVGCIMAEMLTGK-PLFKGHDHLDQLMEIMKvtGTPSKefvqkLQ 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 341 NSEEREF-------------------SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07880  245 SEDAKNYvkklprfrkkdfrsllpnaNPLAVNVLEKMLVLDAESRITAAEALAHPY 300
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
106-378 1.12e-18

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: 85.06  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLkdlgeIGRGAYGSVNKMVHKPSGQI-MAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGalFRE-- 182
Cdd:cd14202    2 FEFSRKDL-----IGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLGKEIKI-LKELKHENIVALYD--FQEia 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 183 GDCWICMELMSTSFDKFYKYVYSVLDD----VIPEEILGKITLATVKAlnhlkenlkIIHRDIKPSNILLDRSGN----- 253
Cdd:cd14202   74 NSVYLVMEYCNGGDLADYLHTMRTLSEdtirLFLQQIAGAMKMLHSKG---------IIHRDLKPQNILLSYSGGrksnp 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 254 ----IKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKwnSVFDQLT 329
Cdd:cd14202  145 nnirIKIADFGFARYLQNNMMAATLCGSPMYMAPEVI----MSQHYDAKADLWSIGTIIYQCLTGKAPFQA--SSPQDLR 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 526479851 330 QVVKGDpPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14202  219 LFYEKN-KSLSPNIPRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
119-318 1.58e-18

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: 85.62  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTvdekeqkQLLMDLDVVMRSSDC------PYIVQFYGA---LFREGDCwICM 189
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNL-------SFMRPLDVQMREFEVlkklnhKNIVKLFAIeeeLTTRHKV-LVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSfdkfykYVYSVLDDV-----IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL----DRSGNIKLCDFG 260
Cdd:cd13988   73 ELCPCG------SLYTVLEEPsnaygLPESEFLIVLRDVVAGMNHLREN-GIVHRDIKPGNIMRvigeDGQSVYKLTDFG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526479851 261 ISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQG----YDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd13988  146 AARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDhqkkYGATVDLWSIGVTFYHAATGSLPF 207
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
119-318 1.95e-18

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: 85.40  E-value: 1.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYgalfregdcwicmelmsTSF 196
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVilNRKEQKHIMAERNVLLKNVKHPFLVGLH-----------------YSF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKyVYSVLDDVIPEEILGKI----TLATVKALNHLKE---------NLKIIHRDIKPSNILLDRSGNIKLCDFGISG 263
Cdd:cd05604   67 QTTDK-LYFVLDFVNGGELFFHLqrerSFPEPRARFYAAEiasalgylhSINIVYRDLKPENILLDSQGHIVLTDFGLCK 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 264 Q-LVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05604  146 EgISNSDTTTTFCGTPEYLAPEVI----RKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
112-378 2.12e-18

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: 85.07  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGE-IGRGAYGSVNKMVHKPSGQIMAVKRIrstvdEKEQKQLLMDLDVVMRSSDCPYIVQFYGaLFREGD-CWICM 189
Cdd:cd14177    4 DVYELKEdIGVGSYSVCKRCIHRATNMEFAVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKD-VYDDGRyVYLVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTS--FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNIL-LDRSGN---IKLCDFGISG 263
Cdd:cd14177   78 ELMKGGelLDRILRQKF------FSEREASAVLYTITKTVDYLHCQ-GVVHRDLKPSNILyMDDSANadsIRICDFGFAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QLV-DSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKW-NSVFDQLTQVVKGDPPQLSN 341
Cdd:cd14177  151 QLRgENGLLLTPCYTANFVAPEVL----MRQGYDAACDIWSLGVLLYTMLAGYTPFANGpNDTPEEILLRIGSGKFSLSG 226
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14177  227 GNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
235-378 2.17e-18

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: 84.62  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK-TRDAGCRPYMAPERIdpSASRQGYDVRS-DVWSLGITLYELA 312
Cdd:cd14200  144 KIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALlSSTAGTPAFMAPETL--SDSGQSFSGKAlDVWAMGVTLYCFV 221
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 313 TGRFPYpkWNSVFDQLTQVVKGDPPQLsnSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14200  222 YGKCPF--IDEFILALHNKIKNKPVEF--PEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
118-377 2.31e-18

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: 84.48  E-value: 2.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd07860    7 KIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFykyvysvLDDVIPEEIlgkiTLATVKA-LNHLKENL------KIIHRDIKPSNILLDRSGNIKLCDFGISGQL-VDSI 269
Cdd:cd07860   87 KF-------MDASALTGI----PLPLIKSyLFQLLQGLafchshRVLHRDLKPQNLLINTEGAIKLADFGLARAFgVPVR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPYMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVV----------------- 332
Cdd:cd07860  156 TYTHEVVTLWYRAPEILLGC---KYYSTAVDIWSLGCIFAEMVTRRALFPG-DSEIDQLFRIFrtlgtpdevvwpgvtsm 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526479851 333 ---KGDPPQLSNSEEREFSPSF----INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07860  232 pdyKPSFPKWARQDFSKVVPPLdedgRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
119-376 2.90e-18

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: 83.85  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVK-----RIRSTVD-----EKEQKqllmdldvVMRSSDCPYIVQFYGALFRE--GDCW 186
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKilkkrKLRRIPNgeanvKREIQ--------ILRRLNHRNVIKLVDVLYNEekQKLY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMElmstsfdkfykYVYSVLDDVIPEEILGKITLAT--------VKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd14119   73 MVME-----------YCVGGLQEMLDSAPDKRLPIWQahgyfvqlIDGLEYL-HSQGIIHKDIKPGNLLLTTDGTLKISD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQL---VDSIAKTRDAGCRPYMAPERIDPSASRQGYDVrsDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKGD 335
Cdd:cd14119  141 FGVAEALdlfAEDDTCTTSQGSPAFQPPEIANGQDSFSGFKV--DIWSAGVTLYNMTTGKYPF-EGDNIYKLFENIGKGE 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 526479851 336 ---PPQLsnseerefSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14119  218 ytiPDDV--------DPDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
118-377 3.08e-18

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: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHK-------PSGQIMAVKRIRSTVdekEQKQLLMDLDVVMRSSDCPYIVQFYGAlFREGD-CWICM 189
Cdd:cd14019    8 KIGEGTFSSVYKAEDKlhdlydrNKGRLVALKHIYPTS---SPSRILNELECLERLGGSNNVSGLITA-FRNEDqVVAVL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMS-TSFDKFYKyvysvldDVIPEEIlgKITL-ATVKALNHLKENlKIIHRDIKPSNILLDR-SGNIKLCDFGISGQLV 266
Cdd:cd14019   84 PYIEhDDFRDFYR-------KMSLTDI--RIYLrNLFKALKHVHSF-GIIHRDVKPGNFLYNReTGKGVLVDFGLAQREE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 D-SIAKTRDAGCRPYMAPERIDPSaSRQGYDVrsDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVK--Gdppqlsnse 343
Cdd:cd14019  154 DrPEQRAPRAGTRGFRAPEVLFKC-PHQTTAI--DIWSAGVILLSILSGRFPFFFSSDDIDALAEIATifG--------- 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 344 erefSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14019  222 ----SDEAYDLLDKLLELDPSKRITAEEALKHPF 251
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
211-378 3.17e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 83.48  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 211 IPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLD-RSGNIKLCDFGiSGQLVDSIAKTRDAGCRPYMAPERIdps 289
Cdd:cd14100  103 LPEELARSFFRQVLEAVRHC-HNCGVLHRDIKDENILIDlNTGELKLIDFG-SGALLKDTVYTDFDGTRVYSPPEWI--- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 290 aSRQGYDVRS-DVWSLGITLYELATGRFPypkwnsvFDQLTQVVKGDPpqlsnSEEREFSPSFINFVNLCLTKDESKRPK 368
Cdd:cd14100  178 -RFHRYHGRSaAVWSLGILLYDMVCGDIP-------FEHDEEIIRGQV-----FFRQRVSSECQHLIKWCLALRPSDRPS 244
                        170
                 ....*....|
gi 526479851 369 YKELLKHPFI 378
Cdd:cd14100  245 FEDIQNHPWM 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
115-318 3.32e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 84.87  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGE-IGRGAYGSVNKMVHKPSGQIMAVK--RIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMEL 191
Cdd:PTZ00263  21 EMGEtLGTGSFGRVRIAKHKGTGEYYAIKclKKREILKMKQVQHVAQEKSILMELSH-PFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 -----MSTSFDKFYKYvysvlddviPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:PTZ00263 100 vvggeLFTHLRKAGRF---------PNDVAKFYHAELVLAFEYL-HSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526479851 267 DSIAKTrdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:PTZ00263 170 DRTFTL--CGTPEYLAPEVI----QSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
116-378 3.54e-18

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: 83.79  E-value: 3.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIrSTVDEKEQKQLLMDLDvVMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14114    7 LEELGTGAFGVVHRCTERATGNNFAAKFI-MTPHESDKETVRKEIQ-IMNQLHHPKLINLHDAFEDDNEMVLILEFLSGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDKFYKYVYSVLDDvipeEILGKITLAtVKALNHLKENlKIIHRDIKPSNILLD--RSGNIKLCDFGISGQL-VDSIA 270
Cdd:cd14114   85 elFERIAAEHYKMSEA----EVINYMRQV-CEGLCHMHEN-NIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLdPKESV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTrDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDPPQLSNSEEREFSPS 350
Cdd:cd14114  159 KV-TTGTAEFAAPEIVE----REPVGFYTDMWAVGVLSYVLLSGLSPFAGEND--DETLRNVKSCDWNFDDSAFSGISEE 231
                        250       260
                 ....*....|....*....|....*...
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14114  232 AKDFIRKLLLADPNKRMTIHQALEHPWL 259
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
116-372 3.59e-18

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk 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: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 83.38  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGE-IGRGAYGSVnkMVHKPSGQIMAVKRIRSTVdekeQKQLLMDLDVVMRSSDCPYIVQFYGALFREGdCWICMELMST 194
Cdd:cd05083   10 LGEiIGEGEFGAV--LQGEYMGQKVAVKNIKCDV----TAQAFLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGisgqLVDSIAKTRD 274
Cdd:cd05083   83 G--NLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYL-ESKKLVHRDLAARNILVSEDGVAKISDFG----LAKVGSMGVD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYEL-ATGRFPYPKW--NSVFDQLTQVVKGDPPQlsnseerEFSP 349
Cdd:cd05083  156 NSRLPvkWTAPEAL----KNKKFSSKSDVWSYGVLLWEVfSYGRAPYPKMsvKEVKEAVEKGYRMEPPE-------GCPP 224
                        250       260
                 ....*....|....*....|...
gi 526479851 350 SFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05083  225 DVYSIMTSCWEAEPGKRPSFKKL 247
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
97-377 4.21e-18

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: 83.48  E-value: 4.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  97 KLKISPEqhwdftaedlkdlgEIGRGAYGSVnkmVHKPS--GQIMAVKRIRS---TVDEKEQkQLLmdldvvmRSSDC-P 170
Cdd:cd13982    1 KLTFSPK--------------VLGYGSEGTI---VFRGTfdGRPVAVKRLLPeffDFADREV-QLL-------RESDEhP 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 171 YIVQFYGalfREGD---CWICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNIL 247
Cdd:cd13982   56 NVIRYFC---TEKDrqfLYIALELCAASLQDLVESPRESKLFLRPGLEPVRLLRQIASGLAHLHS-LNIVHRDLKPQNIL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 248 LDRS-----GNIKLCDFGISGQLVD----SIAKTRDAGCRPYMAPERI-DPSASRQGYDVrsDVWSLG-ITLYELATGRF 316
Cdd:cd13982  132 ISTPnahgnVRAMISDFGLCKKLDVgrssFSRRSGVAGTSGWIAPEMLsGSTKRRQTRAV--DIFSLGcVFYYVLSGGSH 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 317 PYpkwNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd13982  210 PF---GDKLEREANILKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
112-377 5.18e-18

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: 84.30  E-value: 5.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLqkKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSfdkfyKYVYSVLDDVIPEEILGKITLATV-KALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS 268
Cdd:cd05602   88 DYINGG-----ELFYHLQRERCFLEPRARFYAAEIaSALGYL-HSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNS--VFDQLTQVVKGDPPQLSNSEEr 345
Cdd:cd05602  162 NGTTSTfCGTPEYLAPEVL----HKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTaeMYDNILNKPLQLKPNITNSAR- 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 346 efspsfiNFVNLCLTKDESKRPKYK----ELLKHPF 377
Cdd:cd05602  237 -------HLLEGLLQKDRTKRLGAKddftEIKNHIF 265
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
112-377 6.90e-18

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: 83.83  E-value: 6.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYgALFREGD--CWI 187
Cdd:cd05574    2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLdkEEMIKRNKVKRVLTEREI-LATLDHPFLPTLY-ASFQTSThlCFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 ---CM--ELmstsfdkfykyvYSVL----DDVIPEEILgKITLATVK-ALNHLkENLKIIHRDIKPSNILLDRSGNIKLC 257
Cdd:cd05574   80 mdyCPggEL------------FRLLqkqpGKRLPEEVA-RFYAAEVLlALEYL-HLLGFVYRDLKPENILLHESGHIMLT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 258 DFGISGQLVDSIAKTRDAGCRP------------------------------YMAPERIdpSASRQGYDVrsDVWSLGIT 307
Cdd:cd05574  146 DFDLSKQSSVTPPPVRKSLRKGsrrssvksieketfvaepsarsnsfvgteeYIAPEVI--KGDGHGSAV--DWWTLGIL 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 308 LYELATGRFPYpKWNSVFDQLTQVVKGDppqLSNSEEREFSPSFINFVNLCLTKDESKRPKYK----ELLKHPF 377
Cdd:cd05574  222 LYEMLYGTTPF-KGSNRDETFSNILKKE---LTFPESPPVSSEAKDLIRKLLVKDPSKRLGSKrgasEIKRHPF 291
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
112-380 7.06e-18

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 83.15  E-value: 7.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQ----IMAVKRIRSTVDEKEQKQLLmDLDVVMRSSDCPYIVQFYGALFrEGDCWI 187
Cdd:cd05109    8 ELKKVKVLGSGAFGTVYKGIWIPDGEnvkiPVAIKVLRENTSPKANKEIL-DEAYVMAGVGSPYVCRLLGICL-TSTVQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMStsFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-V 266
Cdd:cd05109   86 VTQLMP--YGCLLDYVRENKDRIGSQDLL-NWCVQIAKGMSYL-EEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLdI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNSvfdqltqvvkGDPPQLSNSE 343
Cdd:cd05109  162 DETEYHADGGKVPikWMALESI----LHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPA----------REIPDLLEKG 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 526479851 344 EREFSPS------FINFVNlCLTKDESKRPKYKELLkHPFILM 380
Cdd:cd05109  228 ERLPQPPictidvYMIMVK-CWMIDSECRPRFRELV-DEFSRM 268
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
122-371 7.18e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 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: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 82.93  E-value: 7.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 122 GAYGSVNKMVHKPSGqIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfdkfyk 201
Cdd:cd14027    4 GGFGKVSLCFHRTQG-LVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKG------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 202 YVYSVLDDV-IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISG---------------QL 265
Cdd:cd14027   77 NLMHVLKKVsVPLSVKGRIILEIIEGMAYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwskltkeehneqRE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKtRDAGCRPYMAPERIDPSASRQGYdvRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQ-VVKGDPPQLSNSEE 344
Cdd:cd14027  156 VDGTAK-KNAGTLYYMAPEHLNDVNAKPTE--KSDVYSFAIVLWAIFANKEPYENAINE-DQIIMcIKSGNRPDVDDITE 231
                        250       260
                 ....*....|....*....|....*..
gi 526479851 345 rEFSPSFINFVNLCLTKDESKRPKYKE 371
Cdd:cd14027  232 -YCPREIIDLMKLCWEANPEARPTFPG 257
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
114-375 8.36e-18

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: 82.69  E-value: 8.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKrirstVDEKEQKQ--LLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14017    3 KVVKKIGGGGFGEIYKVRDVVDGEEVAMK-----VESKSQPKqvLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSfdkfykyvysvLDDVIPEEILGKITLAT--------VKALNHLKENlKIIHRDIKPSNILLDRSG----NIKLCDF 259
Cdd:cd14017   78 LGPN-----------LAELRRSQPRGKFSVSTtlrlgiqiLKAIEDIHEV-GFLHRDVKPSNFAIGRGPsderTVYILDF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQLVDSiaktRDAGCRP------YMAPERIDPSASRQGYDV--RSDVWSLGITLYELATGRFPypkWNSVFDQlTQV 331
Cdd:cd14017  146 GLARQYTNK----DGEVERPprnaagFRGTVRYASVNAHRNKEQgrRDDLWSWFYMLIEFVTGQLP---WRKLKDK-EEV 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 332 ----VKGDPPQLSNSEEREFSPsfinFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14017  218 gkmkEKIDHEELLKGLPKEFFQ----ILKHIRSLSYFDTPDYKKLHSL 261
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
111-367 8.88e-18

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: 82.43  E-value: 8.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKpsGQIMAVKRIRSTVDEKEQKQLL-MDLDVV-MRSSDcpyIVQFYGALFREGDC--- 185
Cdd:cd13979    3 EPLRLQEPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFwAELNAArLRHEN---IVRVLAAETGTDFAslg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfdKFYKYVYSVLDDVIPEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd13979   78 LIIMEYCGNG--TLQQLIYEGSEPLPLAHRI-LISLDIARALRFC-HSHGIVHLDVKPANILISEQGVCKLCDFGCSVKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDA----GCRPYMAPERI---DPSAsrqgydvRSDVWSLGITLYELATGRFPYPKWNSVFdqLTQVVKGD-PP 337
Cdd:cd13979  154 GEGNEVGTPRshigGTYTYRAPELLkgeRVTP-------KADIYSFGITLWQMLTRELPYAGLRQHV--LYAVVAKDlRP 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 338 QLSNSEEREFSPSFINFVNLCLTKDESKRP 367
Cdd:cd13979  225 DLSGLEDSEFGQRLRSLISRCWSAQPAERP 254
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
112-373 8.94e-18

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 83.53  E-value: 8.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQ----IMAVKRIRSTVDEKEQKQLLmDLDVVMRSSDCPYIVQFYGalfregdcwI 187
Cdd:cd05108    8 EFKKIKVLGSGAFGTVYKGLWIPEGEkvkiPVAIKELREATSPKANKEIL-DEAYVMASVDNPHVCRLLG---------I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CM--------ELMStsFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDF 259
Cdd:cd05108   78 CLtstvqlitQLMP--FGCLLDYVREHKDNIGSQYLL-NWCVQIAKGMNYLEDR-RLVHRDLAARNVLVKTPQHVKITDF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQL-VDSIAKTRDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYpkwnsvfdqltqvvKGD 335
Cdd:cd05108  154 GLAKLLgAEEKEYHAEGGKVPikWMALESI----LHRIYTHQSDVWSYGVTVWELMTfGSKPY--------------DGI 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 336 PPQ-----LSNSEEREFSPSFINFVNLCLTK----DESKRPKYKELL 373
Cdd:cd05108  216 PASeissiLEKGERLPQPPICTIDVYMIMVKcwmiDADSRPKFRELI 262
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
115-386 1.02e-17

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 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: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 82.66  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVK--RIRSTVDEKEQKQLLMDLDVVMRSSdCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd14026    1 DLRYLSRGAFGTVSRARHADWRVTVAIKclKLDSPVGDSERNCLLKEAEILHKAR-FSYILPILGICNEPEFLGIVTEYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 ST-SFDKFY--KYVYSVLDDVIPEEILGKITLAtVKALNHLkeNLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd14026   80 TNgSLNELLheKDIYPDVAWPLRLRILYEIALG-VNYLHNM--SPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRP------YMAPERIDPSASRQGyDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSE 343
Cdd:cd14026  157 SQSRSSKSAPeggtiiYMPPEEYEPSQKRRA-SVKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQGHRPDTGEDS 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 344 EREFSPS---FINFVNLCLTKDESKRPKYKELL--KHPFILMYEERAV 386
Cdd:cd14026  236 LPVDIPHratLINLIESGWAQNPDERPSFLKCLieLEPVLRTFDEIDV 283
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
119-377 1.19e-17

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: 81.92  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQkqlLMDLDV-VMRSSDCPYIVQFYGALFREGDCWICMELMSTSf 196
Cdd:cd14185    8 IGDGNFAVVKECRHWNENQEYAMKIIdKSKLKGKED---MIESEIlIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVlddVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL----DRSGNIKLCDFGISGQLVDSIAKT 272
Cdd:cd14185   84 DLFDAIIESV---KFTEHDAALMIIDLCEALVYIHSK-HIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGPIFTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 rdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGD-----PPQLSNseereF 347
Cdd:cd14185  160 --CGTPTYVAPEIL----SEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQEELFQIIQLGhyeflPPYWDN-----I 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 348 SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14185  229 SEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
119-376 1.23e-17

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: 81.95  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTvdEKEQKQLlmdlDVVMRSSDCPYIVQF---YGALFREGDCW-ICMELMST 194
Cdd:cd14089    9 LGLGINGKVLECFHKKTGEKFALKVLRDN--PKARREV----ELHWRASGCPHIVRIidvYENTYQGRKCLlVVMECMEG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 S--FDKFYKYVysvlDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL-DRSGN--IKLCDFGISgQLVDSI 269
Cdd:cd14089   83 GelFSRIQERA----DSAFTEREAAEIMRQIGSAVAHL-HSMNIAHRDLKPENLLYsSKGPNaiLKLTDFGFA-KETTTK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRP-YMAPERIDPsasrQGYDVRSDVWSLGITLYELATG-------------------------RFPYPKWNS 323
Cdd:cd14089  157 KSLQTPCYTPyYVAPEVLGP----EKYDKSCDMWSLGVIMYILLCGyppfysnhglaispgmkkrirngqyEFPNPEWSN 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 526479851 324 VFDQLTQVVKGdppqlsnseerefspsfinfvnlCLTKDESKRPKYKELLKHP 376
Cdd:cd14089  233 VSEEAKDLIRG-----------------------LLKTDPSERLTIEEVMNHP 262
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
111-323 1.68e-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: 83.36  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKR-IRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTlLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 E------LMsTSFDKFYKYVYSVLDDVIPEEILGkitLATVkalnhlkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS- 262
Cdd:cd05629   81 EflpggdLM-TMLIKYDTFSEDVTRFYMAECVLA---IEAV-------HKLGFIHRDIKPDNILIDRGGHIKLSDFGLSt 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 ----------------------------GQLVDSIAKT---RD----------------AGCRPYMAPERIdpsaSRQGY 295
Cdd:cd05629  150 gfhkqhdsayyqkllqgksnknridnrnSVAVDSINLTmssKDqiatwkknrrlmaystVGTPDYIAPEIF----LQQGY 225
                        250       260
                 ....*....|....*....|....*...
gi 526479851 296 DVRSDVWSLGITLYELATGRFPYPKWNS 323
Cdd:cd05629  226 GQECDWWSLGAIMFECLIGWPPFCSENS 253
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
117-375 1.70e-17

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: 81.59  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLlmDLDVVMRSSDcpyIVQFYGALFREGDCWICMELMSTSf 196
Cdd:cd13995   10 DFIPRGAFGKVYLAQDTKTKKRMACKLI--PVEQFKPSDV--EIQACFRHEN---IAELYGALLWEETVHLFMEAGEGG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 dkfykYVYSVLDDVIPE---EILGkITLATVKALNHLKENlKIIHRDIKPSNILLdRSGNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd13995   82 -----SVLEKLESCGPMrefEIIW-VTKHVLKGLDFLHSK-NIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDVYVPK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 D-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFP----YPKwnSVFDQLTQVVKGDPPQLSNSEErEFS 348
Cdd:cd13995  154 DlRGTEIYMSPEVI----LCRGHNTKADIYSLGATIIHMQTGSPPwvrrYPR--SAYPSYLYIIHKQAPPLEDIAQ-DCS 226
                        250       260
                 ....*....|....*....|....*..
gi 526479851 349 PSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd13995  227 PAMRELLEAALERNPNHRSSAAELLKH 253
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
106-374 1.72e-17

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. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 83.13  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNK-----MVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALF 180
Cdd:cd14207    2 WEFARERLKLGKSLGRGAFGKVVQasafgIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGACT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REG------------------------------DCWICMELMS------------------TSFDKFYKYVYS---VLDD 209
Cdd:cd14207   82 KSGgplmviveyckygnlsnylkskrdffvtnkDTSLQEELIKekkeaeptggkkkrlesvTSSESFASSGFQedkSLSD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 210 VIPEE--------------ILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDA 275
Cdd:cd14207  162 VEEEEedsgdfykrpltmeDLISYSFQVARGMEFLSSR-KCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCR---PYMAPERIdpsaSRQGYDVRSDVWSLGITLYEL-ATGRFPYPKWN---SVFDQLTQVVKGDPPQLSNSEerefs 348
Cdd:cd14207  241 DARlplKWMAPESI----FDKIYSTKSDVWSYGVLLWEIfSLGASPYPGVQideDFCSKLKEGIRMRAPEFATSE----- 311
                        330       340
                 ....*....|....*....|....*..
gi 526479851 349 psfINFVNL-CLTKDESKRPKYKELLK 374
Cdd:cd14207  312 ---IYQIMLdCWQGDPNERPRFSELVE 335
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
108-378 1.78e-17

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: 81.54  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSS-DCPYIVQFYGALFREGDCW 186
Cdd:cd14116    2 WALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHlRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMEL--MSTSFDKFYKYvySVLDDvipEEILGKIT-LATVKALNHLKenlKIIHRDIKPSNILLDRSGNIKLCDFGISG 263
Cdd:cd14116   82 LILEYapLGTVYRELQKL--SKFDE---QRTATYITeLANALSYCHSK---RVIHRDIKPENLLLGSAGELKIADFGWSV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QlVDSIAKTRDAGCRPYMAPERIDPsasrQGYDVRSDVWSLGITLYELATGRFPYP--KWNSVFDQLTQVVKGDPPQLSN 341
Cdd:cd14116  154 H-APSSRRTTLCGTLDYLPPEMIEG----RMHDEKVDLWSLGVLCYEFLVGKPPFEanTYQETYKRISRVEFTFPDFVTE 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEErefspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14116  229 GAR--------DLISRLLKHNPSQRPMLREVLEHPWI 257
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
112-374 2.50e-17

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They 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, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-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: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 80.96  E-value: 2.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNkmVHKPSGQI-MAVKRIR----STVDEKEQKQLLMDLDvvmrssdCPYIVQFYGALFREGDCW 186
Cdd:cd05059    5 ELTFLKELGSGQFGVVH--LGKWRGKIdVAIKMIKegsmSEDDFIEEAKVMMKLS-------HPKLVQLYGVCTKQRPIF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMST-SFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd05059   76 IVTEYMANgCLLNYLRERRGKFQ----TEQLLEMCKDVCEAMEYLESN-GFIHRDLAARNCLVGEQNVVKVSDFGLARYV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSiAKTRDAGCR---PYMAPERIDpsasRQGYDVRSDVWSLGITLYELAT-GRFPYPKW-NS-VFDQLTQVVKGDPPQL 339
Cdd:cd05059  151 LDD-EYTSSVGTKfpvKWSPPEVFM----YSKFSSKSDVWSFGVLMWEVFSeGKMPYERFsNSeVVEHISQGYRLYRPHL 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 340 SnseerefSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05059  226 A-------PTEVYTIMYSCWHEKPEERPTFKILLS 253
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
211-375 2.70e-17

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: 81.57  E-value: 2.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 211 IPEEILGKITLATVKALNHLKENLKI--IHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDA----------GCR 278
Cdd:cd13986  103 FPEDRILHIFLGICRGLKAMHEPELVpyAHRDIKPGNVLLSEDDEPILMDLGSMNPARIEIEGRREAlalqdwaaehCTM 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 279 PYMAPERIDPSaSRQGYDVRSDVWSLGITLYELATGrfpypkwNSVFDQLTQvvKGDP-------PQLSNSEEREFSPSF 351
Cdd:cd13986  183 PYRAPELFDVK-SHCTIDEKTDIWSLGCTLYALMYG-------ESPFERIFQ--KGDSlalavlsGNYSFPDNSRYSEEL 252
                        170       180
                 ....*....|....*....|....
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd13986  253 HQLVKSMLVVNPAERPSIDDLLSR 276
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
118-378 2.98e-17

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: 81.13  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE-QKQLLMDLDVVMRSSDCPYIVQFYGALfrEGDCWICMELMSTSF 196
Cdd:cd14197   16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcRMEIIHEIAVLELAQANPWVINLHEVY--ETASEMILVLEYAAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRS---GNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd14197   94 GEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNN-NVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELRE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY--PKWNSVFDQLTQVvkgdppQLSNSEErEF---S 348
Cdd:cd14197  173 IMGTPEYVAPEIL----SYEPISTATDMWSIGVLAYVMLTGISPFlgDDKQETFLNISQM------NVSYSEE-EFehlS 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 349 PSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14197  242 ESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
111-318 3.15e-17

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: 81.33  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVK--RIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWIC 188
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKvmAIPEVIRLKQEQHVHNEKRVLKEVSH-PFIIRLFWTEHDQRFLYML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELM---------------STSFDKFYKyvysvlddvipEEIlgkitlatVKALNHLkENLKIIHRDIKPSNILLDRSGN 253
Cdd:cd05612   80 MEYVpggelfsylrnsgrfSNSTGLFYA-----------SEI--------VCALEYL-HSKEIVYRDLKPENILLDKEGH 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 254 IKLCDFGISGQLVDsiaKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05612  140 IKLTDFGFAKKLRD---RTWTlCGTPEYLAPEVI----QSKGHNKAVDWWALGILIYEMLVGYPPF 198
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
104-372 3.61e-17

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: 81.62  E-value: 3.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 104 QHWDFtaeDLKDlGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLlmdldVVMRSSDC-PYIVQFYGALFRE 182
Cdd:cd14179    4 QHYEL---DLKD-KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREI-----AALKLCEGhPNIVKLHEVYHDQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 183 GDCWICMELMSTS--FDKFYKyvysvlDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL-DRSGN--IKLC 257
Cdd:cd14179   75 LHTFLVMELLKGGelLERIKK------KQHFSETEASHIMRKLVSAVSHM-HDVGVVHRDLKPENLLFtDESDNseIKII 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 258 DFGIS------GQLVDSIAKTRDagcrpYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYP------KWNSVF 325
Cdd:cd14179  148 DFGFArlkppdNQPLKTPCFTLH-----YAAPELLN----YNGYDESCDLWSLGVILYTMLSGQVPFQchdkslTCTSAE 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 526479851 326 DQLTQVVKGDppqLSNSEE--REFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd14179  219 EIMKKIKQGD---FSFEGEawKNVSQEAKDLIQGLLTVDPNKRIKMSGL 264
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
106-383 3.73e-17

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: 82.01  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDfTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI----RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFY--GAL 179
Cdd:cd07877   13 WE-VPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLsrpfQSIIHAKRTYRELRLLKH-MKHENVIGLLDVFtpARS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 FRE-GDCWICMELMSTSFDKFYKyVYSVLDDvipeeilgKITLATVKALNHLK--ENLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd07877   91 LEEfNDVYLVTHLMGADLNNIVK-CQKLTDD--------HVQFLIYQILRGLKyiHSADIIHRDLKPSNLAVNEDCELKI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQLVDSIakTRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--G 334
Cdd:cd07877  162 LDFGLARHTDDEM--TGYVATRWYRAPEIM---LNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHI-DQLKLILRlvG 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 335 DPP-----QLSNSEEREFSPSF-----INFVNL--------------CLTKDESKRPKYKELLKHPFILMYEE 383
Cdd:cd07877  236 TPGaellkKISSESARNYIQSLtqmpkMNFANVfiganplavdllekMLVLDSDKRITAAQALAHAYFAQYHD 308
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
116-390 3.85e-17

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: 81.68  E-value: 3.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSV--NKMVHKPSGQIMAVKRIRSTVDEK--------EQKQL-----------LMDLDVVmrssdcpyivq 174
Cdd:cd07857    5 IKELGQGAYGIVcsARNAETSEEETVAIKKITNVFSKKilakralrELKLLrhfrghknitcLYDMDIV----------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 175 FYGAlFREGDCWicMELMSTSFDK------------FYKYVYSVLDDvipeeiLGKITLATVkalnhlkenlkiIHRDIK 242
Cdd:cd07857   74 FPGN-FNELYLY--EELMEADLHQiirsgqpltdahFQSFIYQILCG------LKYIHSANV------------LHRDLK 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 243 PSNILLDRSGNIKLCDFGIS-----GQLVDSIAKTRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELaTGRFP 317
Cdd:cd07857  133 PGNLLVNADCELKICDFGLArgfseNPGENAGFMTEYVATRWYRAPEIM---LSFQSYTKAIDVWSVGCILAEL-LGRKP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 318 YPKWNSVFDQLTQVVK--GDPP-----------------QLSNSEEREFSPSF-------INFVNLCLTKDESKRPKYKE 371
Cdd:cd07857  209 VFKGKDYVDQLNQILQvlGTPDeetlsrigspkaqnyirSLPNIPKKPFESIFpnanplaLDLLEKLLAFDPTKRISVEE 288
                        330
                 ....*....|....*....
gi 526479851 372 LLKHPFILMYEERAVEVAC 390
Cdd:cd07857  289 ALEHPYLAIWHDPDDEPVC 307
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
119-377 4.08e-17

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: 80.94  E-value: 4.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVK-----RIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGAlFREGD--CWIcMEL 191
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTGGDCPFIVCMTYA-FQTPDklCFI-LDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 M---------------STSFDKFYKyvysvlddviPEEILGkitlatvkaLNHLKENLkIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05606   80 MnggdlhyhlsqhgvfSEAEMRFYA----------AEVILG---------LEHMHNRF-IVYRDLKPANILLDEHGHVRI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQLVDSIAKTrDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPY----PKWNSVFDQLTQVV 332
Cdd:cd05606  140 SDLGLACDFSKKKPHA-SVGTHGYMAPEVL---QKGVAYDSSADWFSLGCMLYKLLKGHSPFrqhkTKDKHEIDRMTLTM 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 333 KGDPPQlsnseerEFSPSFINFVNLCLTKDESKR-----PKYKELLKHPF 377
Cdd:cd05606  216 NVELPD-------SFSPELKSLLEGLLQRDVSKRlgclgRGATEVKEHPF 258
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
134-379 4.42e-17

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: 80.79  E-value: 4.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 134 PSGQIMAVKRIrSTVDEKEQKQLLMDLDVVMRSSDCPYIVQF--YGALFREGDCWICMELMstsfdKFYKYVYSV----- 206
Cdd:cd14037   26 NGGNRAALKRV-YVNDEHDLNVCKREIEIMKRLSGHKNIVGYidSSANRSGNGVYEVLLLM-----EYCKGGGVIdlmnq 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 207 -LDDVIPE-EILgKI---TLATVKALNHLKEnlKIIHRDIKPSNILLDRSGNIKLCDFGiSGQLVDSIAKTRDaGCR--- 278
Cdd:cd14037  100 rLQTGLTEsEIL-KIfcdVCEAVAAMHYLKP--PLIHRDLKVENVLISDSGNYKLCDFG-SATTKILPPQTKQ-GVTyve 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 279 ---------PYMAPERIDPSaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQlsnseereFSP 349
Cdd:cd14037  175 edikkyttlQYRAPEMIDLY-RGKPITEKSDIWALGCLLYKLCFYTTPFEESGQLAILNGNFTFPDNSR--------YSK 245
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:cd14037  246 RLHKLIRYMLEEDPEKRPNIYQVSYEAFEL 275
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
108-313 4.69e-17

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: 80.89  E-value: 4.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKP----SGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREG 183
Cdd:cd05038    1 FEERHLKFIKQLGEGHFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQHMSDFKREIEI-LRTLDHEYIVKYKGVCESPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 184 DCWIC--ME-LMSTSFDKFYKYvysvLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd05038   80 RRSLRliMEyLPSGSLRDYLQR----HRDQIDLKRLLLFASQICKGMEYL-GSQRYIHRDLAARNILVESEDLVKISDFG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 261 ISGQLV--DSIAKTRDAGCRP--YMAPERIdpSASRqgYDVRSDVWSLGITLYELAT 313
Cdd:cd05038  155 LAKVLPedKEYYYVKEPGESPifWYAPECL--RESR--FSSASDVWSFGVTLYELFT 207
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
118-378 5.28e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 83.25  E-value: 5.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGD--CWICMEL--- 191
Cdd:PTZ00266   20 KIGNGRFGEVFLVKHKRTQEFFCWKAISyRGLKEREKSQLVIEVNV-MRELKHKNIVRYIDRFLNKANqkLYILMEFcda 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  192 --MSTSFDKFYKYVYSvlddvIPEEILGKITLATVKALNHLkENLK-------IIHRDIKPSNILLD-----------RS 251
Cdd:PTZ00266   99 gdLSRNIQKCYKMFGK-----IEEHAIVDITRQLLHALAYC-HNLKdgpngerVLHRDLKPQNIFLStgirhigkitaQA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  252 GNI------KLCDFGISGQL-VDSIAKTRdAGCRPYMAPERIdpSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSv 324
Cdd:PTZ00266  173 NNLngrpiaKIGDFGLSKNIgIESMAHSC-VGTPYYWSPELL--LHETKSYDDKSDMWALGCIIYELCSGKTPFHKANN- 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 526479851  325 FDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLcltkDESKRPKYKELLKHPFI 378
Cdd:PTZ00266  249 FSQLISELKRGPDLPIKGKSKELNILIKNLLNL----SAKERPSALQCLGYQII 298
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
119-366 5.42e-17

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: 80.84  E-value: 5.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQF-YGALFREGDCWIcMELMSTSF 196
Cdd:cd05630    8 LGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMALNEKQILEKVNSRFVVSLaYAYETKDALCLV-LTLMNGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYkyVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAG 276
Cdd:cd05630   87 LKFH--IYHMGQAGFPEARAVFYAAEICCGLEDLHRE-RIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 277 CRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVF--DQLTQVVKGDPPQLSNseerEFSPSFINF 354
Cdd:cd05630  164 TVGYMAPEVV----KNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIkrEEVERLVKEVPEEYSE----KFSPQARSL 235
                        250
                 ....*....|..
gi 526479851 355 VNLCLTKDESKR 366
Cdd:cd05630  236 CSMLLCKDPAER 247
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
119-377 5.49e-17

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: 81.17  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYgalfregdcwicmelmsTSF 196
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLqkKTILKKKEQNHIMAERNVLLKNLKHPFLVGLH-----------------YSF 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKyVYSVLDDVIPEEIL-------------GKITLATV-KALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd05603   66 QTSEK-LYFVLDYVNGGELFfhlqrercfleprARFYAAEVaSAIGYL-HSLNIIYRDLKPENILLDCQGHVVLTDFGLC 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGDPPQLSN 341
Cdd:cd05603  144 KEGMEPEETTSTfCGTPEYLAPEVL----RKEPYDRTVDWWCLGAVLYEMLYGLPPF--YSRDVSQMYDNILHKPLHLPG 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 342 SEerefSPSFINFVNLCLTKDESKR----PKYKELLKHPF 377
Cdd:cd05603  218 GK----TVAACDLLQGLLHKDQRRRlgakADFLEIKNHVF 253
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
119-318 5.50e-17

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: 80.63  E-value: 5.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTvDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALF--------REGDCWICME 190
Cdd:cd14036    8 IAEGGFAFVYEAQDVGTGKEYALKRLLSN-EEEKNKAIIQEINFMKKLSGHPNIVQFCSAASigkeesdqGQAEYLLLTE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKYVYSVlDDVIPEEILgKITLATVKALNHL-KENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd14036   87 LCKGQLVDFVKKVEAP-GPFSPDTVL-KIFYQTCRAVQHMhKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYP 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 270 AKTRDAGCRP-------------YMAPERID-----PSASRQgydvrsDVWSLGITLYELATGRFPY 318
Cdd:cd14036  165 DYSWSAQKRSlvedeitrnttpmYRTPEMIDlysnyPIGEKQ------DIWALGCILYLLCFRKHPF 225
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
117-369 5.88e-17

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: 80.01  E-value: 5.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVH--KPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALfrEGDCW-ICMELMS 193
Cdd:cd05116    1 GELGSGNFGTVKKGYYqmKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGIC--EAESWmLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TS-FDKFYKYVYSVLDDVIpEEILGKITLAtvkaLNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV--DSIA 270
Cdd:cd05116   79 LGpLNKFLQKNRHVTEKNI-TELVHQVSMG----MKYLEES-NFVHRDLAARNVLLVTQHYAKISDFGLSKALRadENYY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRP--YMAPERIDpsasRQGYDVRSDVWSLGITLYE-LATGRFPYP--KWNSVFDQLTQVVKGDPPQlsnseer 345
Cdd:cd05116  153 KAQTHGKWPvkWYAPECMN----YYKFSSKSDVWSFGVLMWEaFSYGQKPYKgmKGNEVTQMIEKGERMECPA------- 221
                        250       260
                 ....*....|....*....|....
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKY 369
Cdd:cd05116  222 GCPPEMYDLMKLCWTYDVDERPGF 245
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
112-377 6.10e-17

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: 80.54  E-value: 6.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEK-------EQKQLLMDLDvvmrssdCPYIVQFYGALFREGD 184
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvpstaiREISLLKELQ-------HPNIVCLEDVLMQENR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTSFDKFYKYVYS--VLDDVIPEEILGKITLATVKALNHlkenlKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd07861   74 LYLVFEFLSMDLKKYLDSLPKgkYMDAELVKSYLYQILQGILFCHSR-----RVLHRDLKPQNLLIDNKGVIKLADFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQL-VDSIAKTRDAGCRPYMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRfPYPKWNSVFDQLTQVVK--GDP--- 336
Cdd:cd07861  149 RAFgIPVRVYTHEVVTLWYRAPEVLLGS---PRYSTPVDIWSIGTIFAEMATKK-PLFHGDSEIDQLFRIFRilGTPted 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 337 ---------------PQLSNSEEREFSPSF----INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07861  225 iwpgvtslpdykntfPKWKKGSLRTAVKNLdedgLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
119-318 6.23e-17

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: 80.03  E-value: 6.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTSf 196
Cdd:cd14162    8 LGHGSYAVVKKAYSTKHKCKVAIKIVskKKAPEDYLQKFLPREIEV-IKGLKHPNLICFYEAIETTSRVYIIMELAENG- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 dkfykyvySVLDDV-----IPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS-GQLVDSIA 270
Cdd:cd14162   86 --------DLLDYIrkngaLPEPQARRWFRQLVAGVEYC-HSKGVVHRDLKCENLLLDKNNNLKITDFGFArGVMKTKDG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 271 KTRDA----GCRPYMAPE--RIDPsasrqgYD-VRSDVWSLGITLYELATGRFPY 318
Cdd:cd14162  157 KPKLSetycGSYAYASPEilRGIP------YDpFLSDIWSMGVVLYTMVYGRLPF 205
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
113-378 6.54e-17

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: 79.76  E-value: 6.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 113 LKDLGE-IGRGAYGSVNKMVHKPSGQIMAVKRIRST-VDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd14074    4 LYDLEEtLGRGHFAVVKLARHVFTGEKVAVKVIDKTkLDDVSKAHLFQEV-RCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdKFYKYVYSvLDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILL-DRSGNIKLCDFGISGQLVDSI 269
Cdd:cd14074   83 LGDGG--DMYDYIMK-HENGLNEDLARKYFRQIVSAISYCHK-LHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPYMAPERIDPSAsrqgYDVRS-DVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGD---PPQLsnseer 345
Cdd:cd14074  159 KLETSCGSLAYSAPEILLGDE----YDAPAvDIWSLGVILYMLVCGQPPFQEANDS-ETLTMIMDCKytvPAHV------ 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 346 efSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14074  228 --SPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
104-314 8.39e-17

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: 80.24  E-value: 8.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 104 QHWDftAEDLKDLG-EIGRGAYGSVNKMVHkpSGQIMAVKRIRSTVD---EKEQKQLLMDLDVvMRSSDCPYIVQFYGal 179
Cdd:cd14158    9 NNFD--ERPISVGGnKLGEGGFGVVFKGYI--NDKNVAVKKLAAMVDistEDLTKQFEQEIQV-MAKCQHENLVELLG-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 fregdcwicmelMSTSFDKF---YKYVY--SVLDDV--------IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNI 246
Cdd:cd14158   82 ------------YSCDGPQLclvYTYMPngSLLDRLaclndtppLSWHMRCKIAQGTANGINYLHEN-NHIHRDIKSANI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 247 LLDRSGNIKLCDFGI---SGQLVDSIAKTRDAGCRPYMAPEridpsASRQGYDVRSDVWSLGITLYELATG 314
Cdd:cd14158  149 LLDETFVPKISDFGLaraSEKFSQTIMTERIVGTTAYMAPE-----ALRGEITPKSDIFSFGVVLLEIITG 214
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
119-377 9.53e-17

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: 79.38  E-value: 9.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFdk 198
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDM-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 fYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCDFGISGQLVDSIAKTRDA 275
Cdd:cd14082   89 -LEMILSSEKGRLPERITKFLVTQILVALRYLHSK-NIVHCDLKPENVLLASAEPfpqVKLCDFGFARIIGEKSFRRSVV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQlsnsEEREFSPSFINFV 355
Cdd:cd14082  167 GTPAYLAPEVL----RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPN----PWKEISPDAIDLI 238
                        250       260
                 ....*....|....*....|..
gi 526479851 356 NLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14082  239 NNLLQVKMRKRYSVDKSLSHPW 260
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
118-377 1.02e-16

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: 79.76  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGA---LFREGDCWICM-ELMS 193
Cdd:cd14031   17 ELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSwesVLKGKKCIVLVtELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLK-IIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14031   97 SGTLKTYLKRFKVMK----PKVLRSWCRQILKGLQFLHTRTPpIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTSFAK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRdAGCRPYMAPERIDpsasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNseeREFSPSF 351
Cdd:cd14031  173 SV-IGTPEFMAPEMYE-----EHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFN---KVTDPEV 243
                        250       260
                 ....*....|....*....|....*.
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14031  244 KEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
119-373 1.05e-16

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: 79.36  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNK-MVHKPsgqiMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFd 197
Cdd:cd14062    1 IGSGSFGTVYKgRWHGD----VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSSL- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfYKYVYsVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIsgqlvdSIAKTRDAGC 277
Cdd:cd14062   76 --YKHLH-VLETKFEMLQLIDIARQTAQGMDYLHAK-NIIHRDLKSNNIFLHEDLTVKIGDFGL------ATVKTRWSGS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 RP---------YMAPERI---DPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQ-LTQVVKGD-PPQLSNSe 343
Cdd:cd14062  146 QQfeqptgsilWMAPEVIrmqDENP----YSFQSDVYAFGIVLYELLTGQLPYSHINNR-DQiLFMVGRGYlRPDLSKV- 219
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 344 eREFSPSFIN-FVNLCLTKDESKRPKYKELL 373
Cdd:cd14062  220 -RSDTPKALRrLMEDCIKFQRDERPLFPQIL 249
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
119-375 1.06e-16

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: 79.70  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRIRSTVDEK-----EQKQLLMDLDVVMRSsdcPYIVQFYGALFREGDCWICMEL-- 191
Cdd:cd14146    2 IGVGGFGKVYRATWK--GQEVAVKAARQDPDEDikataESVRQEAKLFSMLRH---PNIIKLEGVCLEEPNLCLVMEFar 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 ---MSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKEN--LKIIHRDIKPSNILL------DRSGN--IKLCD 258
Cdd:cd14146   77 ggtLNRALAAANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEavVPILHRDLKSSNILLlekiehDDICNktLKITD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLvDSIAKTRDAGCRPYMAPERIDPSASRQGydvrSDVWSLGITLYELATGRFPYP-------KWNSVFDQLTQV 331
Cdd:cd14146  157 FGLAREW-HRTTKMSAAGTYAWMAPEVIKSSLFSKG----SDIWSYGVLLWELLTGEVPYRgidglavAYGVAVNKLTLP 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 526479851 332 VKGDPPQlsnseerefspSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14146  232 IPSTCPE-----------PFAKLMKECWEQDPHIRPSFALILEQ 264
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
218-380 1.11e-16

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 79.52  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 218 KITLATVKALNHLKENlKIIHRDIKPSNILLDRS-GNIKLCDFGisgqLVDSI-AKTRDAGCRPYMAPERIdpsaSRQGY 295
Cdd:PHA03390 113 KIIRQLVEALNDLHKH-NIIHNDIKLENVLYDRAkDRIYLCDYG----LCKIIgTPSCYDGTLDYFSPEKI----KGHNY 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 296 DVRSDVWSLGITLYELATGRFPYPkwNSVFDQLTqvvkgdppqLSNSEEREFSP-SFINFVNL-------CLTK-DESKR 366
Cdd:PHA03390 184 DVSFDWWAVGVLTYELLTGKHPFK--EDEDEELD---------LESLLKRQQKKlPFIKNVSKnandfvqSMLKyNINYR 252
                        170
                 ....*....|....*
gi 526479851 367 -PKYKELLKHPFILM 380
Cdd:PHA03390 253 lTNYNEIIKHPFLKI 267
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
119-378 1.15e-16

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: 79.26  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIrstVDEKEQKQllmDLDVVMRSSDCPYIVQF---YGALFREGDCW-ICMELMST 194
Cdd:cd14172   12 LGLGVNGKVLECFHRRTGQKCALKLL---YDSPKARR---EVEHHWRASGGPHIVHIldvYENMHHGKRCLlIIMECMEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL---DRSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14172   86 G--ELFSRIQERGDQAFTEREASEIMRDIGTAIQYL-HSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIDPsasrQGYDVRSDVWSLGITLYELATGrfpYPKWNSVFDQ-----LTQVVKGDPPQLSNSEERE 346
Cdd:cd14172  163 QTPCYTPYYVAPEVLGP----EKYDKSCDMWSLGVIMYILLCG---FPPFYSNTGQaispgMKRRIRMGQYGFPNPEWAE 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14172  236 VSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
116-377 1.23e-16

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: 79.69  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVH-KPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMR---SSDCPYIVQFYGA-LFREGDCWICME 190
Cdd:cd07862    6 VAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRhleTFEHPNVVRLFDVcTVSRTDRETKLT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDK-FYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSI 269
Cdd:cd07862   86 LVFEHVDQdLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSH-RVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATgRFPYPKWNSVFDQLTQV--VKGDP-----PQLSNS 342
Cdd:cd07862  165 ALTSVVVTLWYRAPEVLLQSS----YATPVDLWSVGCIFAEMFR-RKPLFRGSSDVDQLGKIldVIGLPgeedwPRDVAL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 343 EEREFSPS----FINFVN-----------LCLTKDESKRPKYKELLKHPF 377
Cdd:cd07862  240 PRQAFHSKsaqpIEKFVTdidelgkdlllKCLTFNPAKRISAYSALSHPY 289
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
118-377 1.28e-16

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: 79.26  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR--STVDEKEQKQLLMDldvvmRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14665    7 DIGSGNFGVARLMRDKQTKELVAVKYIErgEKIDENVQREIINH-----RSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDKFYKYVYSVLDDV--IPEEILGKITLAtvkalnhlkENLKIIHRDIKPSNILLDRSG--NIKLCDFGISGQLVDSI 269
Cdd:cd14665   82 elFERICNAGRFSEDEArfFFQQLISGVSYC---------HSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRPYMAPERIdpsaSRQGYDVR-SDVWSLGITLYELATGRFPY--PKWNSVFDQLTQVVKGdpPQLSNSEERE 346
Cdd:cd14665  153 QPKSTVGTPAYIAPEVL----LKKEYDGKiADVWSCGVTLYVMLVGAYPFedPEEPRNFRKTIQRILS--VQYSIPDYVH 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14665  227 ISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
111-378 1.67e-16

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: 78.75  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrstvdekeQKQLLMDLDVVMRSSD-----C----PYIVQFYGALFR 181
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMI--------DKKAMQKAGMVQRVRNeveihCqlkhPSILELYNYFED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 182 EGDCWICMELMST-SFDKFYKYVYSVLDDVIPEEILGKItlatVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd14186   73 SNYVYLVLEMCHNgEMSRYLKNRKKPFTEDEARHFMHQI----VTGMLYLHSH-GILHRDLTLSNLLLTRNMNIKIADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQLVDSIAKTRD-AGCRPYMAPEridpSASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGD---P 336
Cdd:cd14186  148 LATQLKMPHEKHFTmCGTPNYISPE----IATRSAHGLESDVWSLGCMFYTLLVGRPPFDT-DTVKNTLNKVVLADyemP 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 337 PQLSNSEErefspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14186  223 AFLSREAQ--------DLIHQLLRKNPADRLSLSSVLDHPFM 256
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
108-313 1.78e-16

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: 79.29  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKP----SGQIMAVKRIRSTVDEKeqkqlLMDLD---VVMRSSDCPYIVQFYGALF 180
Cdd:cd14205    1 FEERHLKFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHSTEEH-----LRDFEreiEILKSLQHDNIVKYKGVCY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REG--DCWICMELMStsFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd14205   76 SAGrrNLRLIMEYLP--YGSLRDYLQKHKERIDHIKLL-QYTSQICKGMEYLGTK-RYIHRDLATRNILVENENRVKIGD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 259 FGISGQLVD--SIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT 313
Cdd:cd14205  152 FGLTKVLPQdkEYYKVKEPGESPifWYAPE----SLTESKFSVASDVWSFGVVLYELFT 206
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
111-378 1.86e-16

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: 78.71  E-value: 1.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGE--IGRGAYGSVNKMVHKPSGQIMAVKrIRSTVDekeqkQLLMDLDVvMRSSDCPYIVQFYGALFREG-DCWI 187
Cdd:cd14109    2 RELYEIGEedEKRAAQGAPFHVTERSTGRNFLAQ-LRYGDP-----FLMREVDI-HNSLDHPNIVQMHDAYDDEKlAVTV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFDkfykyvysVLD------DVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLdRSGNIKLCDFGI 261
Cdd:cd14109   75 IDNLASTIEL--------VRDnllpgkDYYTERQVAVFVRQLLLALKHMHD-LGIAHLDLRPEDILL-QDDKLKLADFGQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 SGQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDpPQLSN 341
Cdd:cd14109  145 SRRLLRGKLTTLIYGSPEFVSPEIV----NSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDR-ETLTNVRSGK-WSFDS 218
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14109  219 SPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
118-320 1.89e-16

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: 78.83  E-value: 1.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHK-PSGQI-MAVKRIRSTvDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGdCWICMELMSTS 195
Cdd:cd05115   11 ELGSGNFGCVKKGVYKmRKKQIdVAIKVLKQG-NEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMASGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 -FDKFYkyvySVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV--DSIAKT 272
Cdd:cd05115   89 pLNKFL----SGKKDEITVSNVVELMHQVSMGMKYLEEK-NFVHRDLAARNVLLVNQHYAKISDFGLSKALGadDSYYKA 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 273 RDAGCRP--YMAPERIDpsasRQGYDVRSDVWSLGITLYE-LATGRFPYPK 320
Cdd:cd05115  164 RSAGKWPlkWYAPECIN----FRKFSSRSDVWSYGVTMWEaFSYGQKPYKK 210
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
119-377 1.92e-16

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: 79.67  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYgalfregdcwicmelmsTSF 196
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVLqkKAILKRNEVKHIMAERNVLLKNVKHPFLVGLH-----------------YSF 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 ---DKfykyVYSVLDDV--------------IPE--------EIlgkitlatVKALNHLKEnLKIIHRDIKPSNILLDRS 251
Cdd:cd05575   66 qtkDK----LYFVLDYVnggelffhlqrerhFPEprarfyaaEI--------ASALGYLHS-LNIIYRDLKPENILLDSQ 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 252 GNIKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQ 330
Cdd:cd05575  133 GHVVLTDFGLCKEGIEPSDTTSTfCGTPEYLAPEVL----RKQPYDRTVDWWCLGAVLYEMLYGLPPF--YSRDTAEMYD 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 331 VVKGDPPQLSNSeereFSPSFINFVNLCLTKDESKR----PKYKELLKHPF 377
Cdd:cd05575  207 NILHKPLRLRTN----VSPSARDLLEGLLQKDRTKRlgsgNDFLEIKNHSF 253
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
119-378 1.92e-16

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: 78.42  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRsTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIK-CRKAKDREDVRNEIEI-MNQLRHPRLLQLYDAFETPREMVLVMEYVAGGelF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKfykyvysVLDD--VIPEEILGKITLATVKALNHLKENLkIIHRDIKPSNIL-LDRSGN-IKLCDFGISgQLVDSIAKT 272
Cdd:cd14103   79 ER-------VVDDdfELTERDCILFMRQICEGVQYMHKQG-ILHLDLKPENILcVSRTGNqIKIIDFGLA-RKYDPDKKL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 R-DAGCRPYMAPERIDpsasrqgYDVRS---DVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDppqlSNSEEREF- 347
Cdd:cd14103  150 KvLFGTPEFVAPEVVN-------YEPISyatDMWSVGVICYVLLSGLSPFMGDNDA-ETLANVTRAK----WDFDDEAFd 217
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 348 --SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14103  218 diSDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
235-378 2.56e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 80.45  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA---KTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYEL 311
Cdd:PTZ00267 189 KMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSldvASSFCGTPYYLAPELWE----RKRYSKKADMWSLGVILYEL 264
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 312 ATGRFPYpKWNSVFDQLTQVVKGD----PPQLSNSEEREFSPsfinfvnlCLTKDESKRPKYKELLKHPFI 378
Cdd:PTZ00267 265 LTLHRPF-KGPSQREIMQQVLYGKydpfPCPVSSGMKALLDP--------LLSKNPALRPTTQQLLHTEFL 326
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
105-373 2.80e-16

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: 78.53  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 105 HWDFTAEDLKDLGEIGRGAYGSVNKmvHKPSGQImAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGD 184
Cdd:cd14149    6 YWEIEASEVMLSTRIGSGSFGTVYK--GKWHGDV-AVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTSFdkfYKYVYsVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgq 264
Cdd:cd14149   83 AIVTQWCEGSSL---YKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLA-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 lvdsIAKTRDAGCRP---------YMAPERIDpSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVV--K 333
Cdd:cd14149  156 ----TVKSRWSGSQQveqptgsilWMAPEVIR-MQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNR-DQIIFMVgrG 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 334 GDPPQLSNSEEReFSPSFINFVNLCLTKDESKRPKYKELL 373
Cdd:cd14149  230 YASPDLSKLYKN-CPKAMKRLVADCIKKVKEERPLFPQIL 268
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
116-373 2.93e-16

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: 78.13  E-value: 2.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKmvHKPSGQImAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14150    5 LKRIGTGSFGTVFR--GKWHGDV-AVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FdkfYKYVYsVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgqlvdsIAKTRDA 275
Cdd:cd14150   82 L---YRHLH-VTETRFDTMQLIDVARQTAQGMDYLHAK-NIIHRDLKSNNIFLHEGLTVKIGDFGLA------TVKTRWS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRP---------YMAPERI---DPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKG----DPPQL 339
Cdd:cd14150  151 GSQQveqpsgsilWMAPEVIrmqDTNP----YSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGylspDLSKL 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 340 SNSEEREFSPSFINfvnlCLTKDESKRPKYKELL 373
Cdd:cd14150  227 SSNCPKAMKRLLID----CLKFKREERPLFPQIL 256
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
119-397 3.27e-16

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 80.08  E-value: 3.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLM-DLDVVmrssDCPYIVQFY-GALFREGDCWI----CMELM 192
Cdd:PTZ00036  74 IGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMkNLNHI----NIIFLKDYYyTECFKKNEKNIflnvVMEFI 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSFDKFYKYvYSVLDDVIPEEILGKITLATVKALNHLKENLkIIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAK 271
Cdd:PTZ00036 150 PQTVHKYMKH-YARNNHALPLFLVKLYSYQLCRALAYIHSKF-ICHRDLKPQNLLIDpNTHTLKLCDFGSAKNLLAGQRS 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGrFPYPKWNSVFDQLTQVVK--GDP------------- 336
Cdd:PTZ00036 228 VSYICSRFYRAPELMLGATN---YTTHIDLWSLGCIIAEMILG-YPIFSGQSSVDQLVRIIQvlGTPtedqlkemnpnya 303
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 337 ----PQLSNSEEREFSP-----SFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKILD 397
Cdd:PTZ00036 304 dikfPDVKPKDLKKVFPkgtpdDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDPCIKLPKYIDKLPD 373
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
235-378 3.38e-16

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: 78.47  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA-KTRDAGCRPYMAPERIdpSASRQGYDVRS-DVWSLGITLYELA 312
Cdd:cd14199  146 KIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDAlLTNTVGTPAFMAPETL--SETRKIFSGKAlDVWAMGVTLYCFV 223
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 313 TGRFPYpkWNSVFDQLTQVVKGDPpqLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14199  224 FGQCPF--MDERILSLHSKIKTQP--LEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
117-342 3.91e-16

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: 77.76  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHKPSGQIMAVKRIRST-VDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14075    8 GELGSGNFSQVKLGIHQLTKEKVAIKILDKTkLDQKTQRLLSREISS-MEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdKFYKYVYSvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDA 275
Cdd:cd14075   87 --ELYTKIST--EGKLSESEAKPLFAQIVSAVKHMHEN-NIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTFC 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRPYMAPERIDpSASRQGYDVrsDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKGD---PPQLSNS 342
Cdd:cd14075  162 GSPPYAAPELFK-DEHYIGIYV--DIWALGVLLYFMVTGVMPF-RAETVAKLKKCILEGTytiPSYVSEP 227
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
97-377 4.47e-16

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: 78.97  E-value: 4.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  97 KLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVD-EKEQKQLLMDLDVVMRSSDCPYIVQF 175
Cdd:cd05593    1 EMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 176 -YGALFREGDCWIcMELMSTSfDKFYkyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNI 254
Cdd:cd05593   81 kYSFQTKDRLCFV-MEYVNGG-ELFF---HLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISGQ-LVDSIAKTRDAGCRPYMAPERIDPSasrqGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVK 333
Cdd:cd05593  155 KITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDN----DYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELIL 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 526479851 334 GDPPQLSnseeREFSPSFINFVNLCLTKDESKR-----PKYKELLKHPF 377
Cdd:cd05593  229 MEDIKFP----RTLSADAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 273
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
236-378 4.58e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; 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). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 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: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 77.30  E-value: 4.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 236 IIHRDIKPSNILLD-RSGNIKLCDFGiSGQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRS-DVWSLGITLYELAT 313
Cdd:cd14102  126 VVHRDIKDENLLVDlRTGELKLIDFG-SGALLKDTVYTDFDGTRVYSPPEWI----RYHRYHGRSaTVWSLGVLLYDMVC 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 314 GRFPypkwnsvFDQLTQVVKGdppqlSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14102  201 GDIP-------FEQDEEILRG-----RLYFRRRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
119-318 4.70e-16

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: 78.51  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRStvdekeqkqllmdLDVVMRS--------------SDCPYIVQFYGAlFREGD 184
Cdd:cd05598    9 IGVGAFGEVSLVRKKDTNALYAMKTLRK-------------KDVLKRNqvahvkaerdilaeADNEWVVKLYYS-FQDKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 C-WICME------LMSTSFDKFykyvysvlddvIPEEILGKITLAT-VKALNHLkENLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05598   75 NlYFVMDyipggdLMSLLIKKG-----------IFEEDLARFYIAElVCAIESV-HKMGFIHRDIKPDNILIDRDGHIKL 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 257 CDFGisgqLVDSIAKTRDA---------GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05598  143 TDFG----LCTGFRWTHDSkyylahslvGTPNYIAPEVL----LRTGYTQLCDWWSVGVILYEMLVGQPPF 205
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
226-319 5.41e-16

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 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: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 78.03  E-value: 5.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 226 ALNHLKENlKIIHRDIKPSNILLDRSGN-IKLCDFGisgqlvdSIAKTRDAGCRPYM------APERIDPSAsrqgYDVR 298
Cdd:cd14135  117 ALKHLKKC-NILHADIKPDNILVNEKKNtLKLCDFG-------SASDIGENEITPYLvsrfyrAPEIILGLP----YDYP 184
                         90       100
                 ....*....|....*....|.
gi 526479851 299 SDVWSLGITLYELATGRFPYP 319
Cdd:cd14135  185 IDMWSVGCTLYELYTGKILFP 205
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
105-372 5.76e-16

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk 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: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 77.09  E-value: 5.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 105 HWDFTAEDlkdlgEIGRGAYGSVNKMVHKPSGQImAVKRIRSTvDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGD 184
Cdd:cd05148    5 REEFTLER-----KLGSGYFGEVWEGLWKNRVRV-AIKILKSD-DLLKQQDFQKEVQA-LKRLRHKHLISLFAVCSVGEP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd05148   77 VYIITELMEKG--SLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQ-NSIHRDLAARNILVGEDLVCKVADFGLARL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCrPY--MAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNS--VFDQLTQVVKGDPPQl 339
Cdd:cd05148  154 IKEDVYLSSDKKI-PYkwTAPE----AASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNheVYDQITAGYRMPCPA- 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 340 snseerEFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05148  228 ------KCPQEIYKIMLECWAAEPEDRPSFKAL 254
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
106-372 5.80e-16

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn 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: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 77.39  E-value: 5.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQImAVKRIRSTVdekEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd05072    2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGT---MSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfdkfykyvySVLDDVIPEEiLGKITL-------ATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd05072   78 YIITEYMAKG---------SLLDFLKSDE-GGKVLLpklidfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIAD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWNSVfDQLTQVVKG- 334
Cdd:cd05072  148 FGLARVIEDNEYTAREGAKFPikWTAPEAINFGS----FTIKSDVWSFGILLYEIVTyGKIPYPGMSNS-DVMSALQRGy 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 526479851 335 DPPQLSNSEEREFspsfiNFVNLCLTKDESKRPKYKEL 372
Cdd:cd05072  223 RMPRMENCPDELY-----DIMKTCWKEKAEERPTFDYL 255
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
119-366 6.01e-16

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: 77.73  E-value: 6.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQF-YGALFREGDCWIcMELMSTSF 196
Cdd:cd05631    8 LGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMALNEKRILEKVNSRFVVSLaYAYETKDALCLV-LTIMNGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYkyVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAG 276
Cdd:cd05631   87 LKFH--IYNMGNPGFDEQRAIFYAAELCCGLEDLQRE-RIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 277 CRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVF--DQLTQVVKGDPPQLSNseerEFSPSFINF 354
Cdd:cd05631  164 TVGYMAPEVIN----NEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVkrEEVDRRVKEDQEEYSE----KFSEDAKSI 235
                        250
                 ....*....|..
gi 526479851 355 VNLCLTKDESKR 366
Cdd:cd05631  236 CRMLLTKNPKER 247
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
107-318 6.38e-16

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: 77.39  E-value: 6.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 107 DFTAEDLKDLgeIGRGAYGSVNKMVHkpSGQIMAVKRIRSTVDE---------KEQKQLLMDLDvvmrssdCPYIVQFYG 177
Cdd:cd14145    4 DFSELVLEEI--IGIGGFGKVYRAIW--IGDEVAVKAARHDPDEdisqtienvRQEAKLFAMLK-------HPNIIALRG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 178 ALFREGDCWICMElmstsFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKEN--LKIIHRDIKPSNILL------- 248
Cdd:cd14145   73 VCLKEPNLCLVME-----FARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEaiVPVIHRDLKSSNILIlekveng 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 249 DRSGNI-KLCDFGISGQLvDSIAKTRDAGCRPYMAPERIDPSASRQGydvrSDVWSLGITLYELATGRFPY 318
Cdd:cd14145  148 DLSNKIlKITDFGLAREW-HRTTKMSAAGTYAWMAPEVIRSSMFSKG----SDVWSYGVLLWELLTGEVPF 213
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
119-391 6.60e-16

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: 78.18  E-value: 6.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDE-KEQKQLLMDLDVvMRSSDCPYIVQfygalfregdcwICMELMSTSFD 197
Cdd:cd07855   13 IGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVvTTAKRTLRELKI-LRHFKHDNIIA------------IRDILRPKVPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYVYSVLDdvIPEEILGKI-------TLATVKA-LNHLKENLK------IIHRDIKPSNILLDRSGNIKLCDFGISG 263
Cdd:cd07855   80 ADFKDVYVVLD--LMESDLHHIihsdqplTLEHIRYfLYQLLRGLKyihsanVIHRDLKPSNLLVNENCELKIGDFGMAR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QLVDSIAK-----TRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELaTGRFPYPKWNSVFDQLTQV--VKGDP 336
Cdd:cd07855  158 GLCTSPEEhkyfmTEYVATRWYRAPELM---LSLPEYTQAIDMWSVGCIFAEM-LGRRQLFPGKNYVHQLQLIltVLGTP 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 337 PQ-----------------LSNSEEREF-------SPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACY 391
Cdd:cd07855  234 SQavinaigadrvrryiqnLPNKQPVPWetlypkaDQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPDCA 312
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
119-377 6.70e-16

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: 77.61  E-value: 6.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRstVDEKEQKQLLMDLDV-----VMRSSDCPYIVQFYgALFREGDCwIC--MEL 191
Cdd:cd07841    8 LGEGTYAVVYKARDKETGRIVAIKKIK--LGERKEAKDGINFTAlreikLLQELKHPNIIGLL-DVFGHKSN-INlvFEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSFDKfykyvysVLDDVI----PEEIlgK-ITLATVKALNHLKENLkIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd07841   84 METDLEK-------VIKDKSivltPADI--KsYMLMTLRGLEYLHSNW-ILHRDLKPNNLLIASDGVLKLADFGLARSFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAK-TRDAGCRPYMAPERIdpSASRQgYDVRSDVWSLGITLYELATgRFPYPKWNSVFDQLTQVVK--GDP-----PQ 338
Cdd:cd07841  154 SPNRKmTHQVVTRWYRAPELL--FGARH-YGVGVDMWSVGCIFAELLL-RVPFLPGDSDIDQLGKIFEalGTPteenwPG 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 339 LSN----SEEREFSP-SF-----------INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07841  230 VTSlpdyVEFKPFPPtPLkqifpaasddaLDLLQRLLTLNPNKRITARQALEHPY 284
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
110-375 7.14e-16

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: 77.22  E-value: 7.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSsDCPYIVQ-FYGALFREGDCWic 188
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVLREVRALAKL-DHPGIVRyFNAWLERPPEGW-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMstsfDKFYKYVY------SVLDDVI---------PEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGN 253
Cdd:cd14048   82 QEKM----DEVYLYIQmqlcrkENLKDWMnrrctmesrELFVCLNIFKQIASAVEYL-HSKGLIHRDLKPSNVFFSLDDV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 254 IKLCDFGIS------------GQLVDSIAK-TRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELAtgrFPYPK 320
Cdd:cd14048  157 VKVGDFGLVtamdqgepeqtvLTPMPAYAKhTGQVGTRLYMSPEQI----HGNQYSEKVDIFALGLILFELI---YSFST 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 321 WNSVFDQLTQVVKGD-PPQLSNSEEREFspsfiNFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14048  230 QMERIRTLTDVRKLKfPALFTNKYPEER-----DMVQQMLSPSPSERPEAHEVIEH 280
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
112-378 8.46e-16

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: 76.99  E-value: 8.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEI-GRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd14167    3 DIYDFREVlGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEI-AVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTS--FDKFY-KYVYSvlddvipEEILGKITLATVKALNHLkENLKIIHRDIKPSNIL---LDRSGNIKLCDFGISGQ 264
Cdd:cd14167   82 LVSGGelFDRIVeKGFYT-------ERDASKLIFQILDAVKYL-HDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN--SVFDQLTQV-VKGDPPQLSn 341
Cdd:cd14167  154 EGSGSVMSTACGTPGYVAPEVL----AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdaKLFEQILKAeYEFDSPYWD- 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 seerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14167  229 ----DISDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
112-374 8.78e-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: 77.00  E-value: 8.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKmvHKPSGQImAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGAlfregdcwiCMEL 191
Cdd:cd14063    1 ELEIKEVIGKGRFGRVHR--GRWHGDV-AIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGA---------CMDP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 ----MSTSFDK---FYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDrSGNIKLCDFGISGq 264
Cdd:cd14063   69 phlaIVTSLCKgrtLYSLIHERKEKFDFNKTV-QIAQQICQGMGYLHAK-GIIHKDLKSKNIFLE-NGRVVITDFGLFS- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGC-------RPYMAPERI---DPSASRQG---YDVRSDVWSLGITLYELATGRFPYPK--WNSVfdqLT 329
Cdd:cd14063  145 LSGLLQPGRREDTlvipngwLCYLAPEIIralSPDLDFEEslpFTKASDVYAFGTVWYELLAGRWPFKEqpAESI---IW 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 526479851 330 QVVKGDPPQLSN-SEEREFSpsfiNFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14063  222 QVGCGKKQSLSQlDIGREVK----DILMQCWAYDPEKRPTFSDLLR 263
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
106-377 1.13e-15

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: 77.72  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEdLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR----STVDEK----EQKQL-LMD-------LDVVMRSSDC 169
Cdd:cd07851   11 WEVPDR-YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSrpfqSAIHAKrtyrELRLLkHMKhenviglLDVFTPASSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 170 PYIVQFYgalfregdcwICMELMSTSFDKFYKYvySVL-DDVIpEEILGKItlatVKALNHLkENLKIIHRDIKPSNILL 248
Cdd:cd07851   90 EDFQDVY----------LVTHLMGADLNNIVKC--QKLsDDHI-QFLVYQI----LRGLKYI-HSAGIIHRDLKPSNLAV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 249 DRSGNIKLCDFGISGQLVDSIakTRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQL 328
Cdd:cd07851  152 NEDCELKILDFGLARHTDDEM--TGYVATRWYRAPEIM---LNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHI-DQL 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 329 TQVVK--GDPP-----QLSNSEEREF-------------------SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07851  226 KRIMNlvGTPDeellkKISSESARNYiqslpqmpkkdfkevfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPY 300
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
115-376 1.14e-15

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: 76.21  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGE-IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQkqlLMDLDV-VMRSSDCPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14095    3 DIGRvIGDGNFAVVKECRDKATDKEYALKIIdKAKCKGKEH---MIENEVaILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MS--------TSFDKFykyvysvlddviPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL----DRSGNIKLCDF 259
Cdd:cd14095   80 VKggdlfdaiTSSTKF------------TERDASRMVTDLAQALKYL-HSLSIVHRDIKPENLLVveheDGSKSLKLADF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQLVDSIAKTrdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGrFPyPKWNSVFDQ---LTQVVKGD- 335
Cdd:cd14095  147 GLATEVKEPLFTV--CGTPTYVAPEIL----AETGYGLKVDIWAAGVITYILLCG-FP-PFRSPDRDQeelFDLILAGEf 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 526479851 336 ---PPQLSNseereFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14095  219 eflSPYWDN-----ISDSAKDLISRMLVVDPEKRYSAGQVLDHP 257
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
105-372 1.26e-15

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like 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: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 76.29  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 105 HWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQImAVKRIRS-TVDEKE---QKQllmdldvVMRSSDCPYIVQFYGALF 180
Cdd:cd05068    2 QWEIDRKSLKLLRKLGSGQFGEVWEGLWNNTTPV-AVKTLKPgTMDPEDflrEAQ-------IMKKLRHPKLIQLYAVCT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REGDCWICMELMST-SFDKFYKYVYSVLDdvIPEEIlgkITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDF 259
Cdd:cd05068   74 LEEPIYIITELMKHgSLLEYLQGKGRSLQ--LPQLI---DMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQL-VDSIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNSVfDQLTQVVKG- 334
Cdd:cd05068  149 GLARVIkVEDEYEAREGAKFPikWTAPE----AANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNA-EVLQQVERGy 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 526479851 335 DPPQLSNSEerefsPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05068  224 RMPCPPNCP-----PQLYDIMLECWKADPMERPTFETL 256
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
111-318 1.29e-15

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: 77.79  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05627    2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRkADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 EL-----MSTSFDKfykyvysvlDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGI--- 261
Cdd:cd05627   82 EFlpggdMMTLLMK---------KDTLSEEATQFYIAETVLAIDAIHQ-LGFIHRDIKPDNLLLDAKGHVKLSDFGLctg 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 ---------------------------SGQLVDSIAKTR------DAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITL 308
Cdd:cd05627  152 lkkahrtefyrnlthnppsdfsfqnmnSKRKAETWKKNRrqlaysTVGTPDYIAPEVF----MQTGYNKLCDWWSLGVIM 227
                        250
                 ....*....|
gi 526479851 309 YELATGRFPY 318
Cdd:cd05627  228 YEMLIGYPPF 237
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
111-378 1.30e-15

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: 76.88  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRStvdEKEQKQL----LMDLDVVMRSSDcPYIVQFygalfREgdcw 186
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKM---EKEKEGFpitsLREINILLKLQH-PNIVTV-----KE---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 icmELMSTSFDKFY---KYVYSVLDDVIpEEILGKITLATVKAL--------NHLKENlKIIHRDIKPSNILLDRSGNIK 255
Cdd:cd07843   72 ---VVVGSNLDKIYmvmEYVEHDLKSLM-ETMKQPFLQSEVKCLmlqllsgvAHLHDN-WILHRDLKTSNLLLNNRGILK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 256 LCDFGISGQLVDSIAK-TRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRfPYPKWNSVFDQLTQVVK- 333
Cdd:cd07843  147 ICDFGLAREYGSPLKPyTQLVVTLWYRAPELL---LGAKEYSTAIDMWSVGCIFAELLTKK-PLFPGKSEIDQLNKIFKl 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 334 -GDP-----PQLS---------------NSEEREFSPSFI-----NFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd07843  223 lGTPtekiwPGFSelpgakkktftkypyNQLRKKFPALSLsdngfDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
114-378 1.31e-15

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: 76.59  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLgeIGRGAYGSVNKMVH-KPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd14201   11 KDL--VGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLGKEIKI-LKELQHENIVALYDVQEMPNSVFLVMEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 ST-SFDKFYKYVYSVLDDVIpeeilgKITLATVKALNHLKENLKIIHRDIKPSNILLDRSG---------NIKLCDFGIS 262
Cdd:cd14201   88 NGgDLADYLQAKGTLSEDTI------RVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpKWNSvfDQLTQVVKGDPPQLSNS 342
Cdd:cd14201  162 RYLQSNMMAATLCGSPMYMAPEVI----MSQHYDAKADLWSIGTVIYQCLVGKPPF-QANS--PQDLRMFYEKNKNLQPS 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 343 EEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14201  235 IPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
119-318 1.31e-15

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: 76.28  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRIRSTVDEKEQKQLlmdlDVVMRSSDC------PYIVQFYGALFREGDCWICMEL- 191
Cdd:cd14061    2 IGVGGFGKVYRGIWR--GEEVAVKAARQDPDEDISVTL----ENVRQEARLfwmlrhPNIIALRGVCLQPPNLCLVMEYa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 ----MSTSFDKfykyvysvldDVIPEEILGKITLATVKALNHLKEN--LKIIHRDIKPSNILLDRSGN--------IKLC 257
Cdd:cd14061   76 rggaLNRVLAG----------RKIPPHVLVDWAIQIARGMNYLHNEapVPIIHRDLKSSNILILEAIEnedlenktLKIT 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 258 DFGISGQLVDSiAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd14061  146 DFGLAREWHKT-TRMSAAGTYAWMAPEVIKSST----FSKASDVWSYGVLLWELLTGEVPY 201
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
119-378 1.33e-15

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: 76.93  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd05632   10 LGKGGFGEVCACQVRATGKMYACKRLeKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYkyVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGC 277
Cdd:cd05632   90 KFH--IYNMGNPGFEEERALFYAAEILCGLEDLHRE-NTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 RPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPypkwnsvFDQLTQVVKGDPPQLSNSEERE-----FSPSFI 352
Cdd:cd05632  167 VGYMAPEVLN----NQRYTLSPDYWGLGCLIYEMIEGQSP-------FRGRKEKVKREEVDRRVLETEEvysakFSEEAK 235
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 353 NFVNLCLTKDESKRPKYK-----ELLKHPFI 378
Cdd:cd05632  236 SICKMLLTKDPKQRLGCQeegagEVKRHPFF 266
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
116-351 1.47e-15

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: 76.32  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd07839    5 LEKIGEGTYGTVFKAKNRETHEIVALKRVRlDDDDEGVPSSALREI-CLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgqlvdsiaktrd 274
Cdd:cd07839   84 DLKKYFDSCNGDID----PEIVKSFMFQLLKGLAFCHSH-NVLHRDLKPQNLLINKNGELKLADFGLA------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 agcRPYMAPERI-------------DPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVK--GDP--- 336
Cdd:cd07839  147 ---RAFGIPVRCysaevvtlwyrppDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRllGTPtee 223
                        250
                 ....*....|....*..
gi 526479851 337 --PQLSNSEEREFSPSF 351
Cdd:cd07839  224 swPGVSKLPDYKPYPMY 240
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
119-378 1.74e-15

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: 76.61  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMdldvvmRSSDCPYIVQF---YGALFREGDCW-ICMELMST 194
Cdd:cd14170   10 LGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHW------RASQCPHIVRIvdvYENLYAGRKCLlIVMECLDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDR---SGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14170   84 G--ELFSRIQDRGDQAFTEREASEIMKSIGEAIQYL-HSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIDPsasrQGYDVRSDVWSLGITLYELATGrfpYPKWNS-----VFDQLTQVVKGDPPQLSNSEERE 346
Cdd:cd14170  161 TTPCYTPYYVAPEVLGP----EKYDKSCDMWSLGVIMYILLCG---YPPFYSnhglaISPGMKTRIRMGQYEFPNPEWSE 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14170  234 VSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 265
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
119-378 1.76e-15

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: 75.97  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVMRSSDCPyIVQFYGAL-FREGDCWICMELMSTS 195
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKIIdkKKAPDDFVEKFLPRELEILARLNHKS-IIKTYEIFeTSDGKVYIVMELGVQG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdKFYKYVYSVLddVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV-DS-----I 269
Cdd:cd14165   88 --DLLEFIKLRG--ALPEDVARKMFHQLSSAIKYCHE-LDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLrDEngrivL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRdAGCRPYMAPERIdpsasrQG--YDVR-SDVWSLGITLYELATGRFPYPKWN---SVFDQLTQVVKGDPPQLSNSE 343
Cdd:cd14165  163 SKTF-CGSAAYAAPEVL------QGipYDPRiYDIWSLGVILYIMVCGSMPYDDSNvkkMLKIQKEHRVRFPRSKNLTSE 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 526479851 344 ERefspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14165  236 CK-------DLIYRLLQPDVSQRLCIDEVLSHPWL 263
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
117-374 1.78e-15

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: 76.15  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMS-TS 195
Cdd:cd05045   11 GEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNH-PHVIKLYGACSQDGPLLLIVEYAKyGS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYK--------YVYSVL---------DDVIPEEILGKITLA--TVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05045   90 LRSFLResrkvgpsYLGSDGnrnssyldnPDERALTMGDLISFAwqISRGMQYLAE-MKLVHRDLAARNVLVAEGRKMKI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQLV--DSIAKtRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKW--NSVFDQLT 329
Cdd:cd05045  169 SDFGLSRDVYeeDSYVK-RSKGRIPvkWMAIE----SLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIapERLFNLLK 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 330 QVVKGDPPQlsNSEEREFspsfiNFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05045  244 TGYRMERPE--NCSEEMY-----NLMLTCWKQEPDKRPTFADISK 281
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
220-377 1.85e-15

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: 75.47  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 220 TLATVKALNHLKENlKIIHRDIKPSNILLDRS---GNIKLCDFGISGQLVDSIAKTRDAGCRP--YMAPERIDPSASrqg 294
Cdd:cd14012  110 TLQLLEALEYLHRN-GVVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLLDMCSRGSLDEFKQtyWLPPELAQGSKS--- 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 295 YDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLtqvvkgDPPQLSnseerefsPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14012  186 PTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVL------VSLDLS--------ASLQDFLSKCLSLDPKKRPTALELLP 251

                 ...
gi 526479851 375 HPF 377
Cdd:cd14012  252 HEF 254
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
106-375 2.19e-15

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: 75.99  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNK-----MVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALF 180
Cdd:cd05054    2 WEFPRDRLKLGKPLGRGAFGKVIQasafgIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGACT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 R-EGDCWICMELmsTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHL-KENL----------------------KI 236
Cdd:cd05054   82 KpGGPLMVIVEF--CKFGNLSNYLRSKREEFVPYRDKGARDVEEEEDDDELyKEPLtledlicysfqvargmeflasrKC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 237 IHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCR---PYMAPERIDPSAsrqgYDVRSDVWSLGITLYEL-A 312
Cdd:cd05054  160 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARlplKWMAPESIFDKV----YTTQSDVWSFGVLLWEIfS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 313 TGRFPYP--KWNSVF-DQLTQVVKGDPPQLSnseerefSPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd05054  236 LGASPYPgvQMDEEFcRRLKEGTRMRAPEYT-------TPEIYQIMLDCWHGEPKERPTFSELVEK 294
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
211-377 2.19e-15

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: 75.82  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 211 IPEEILGKITLATVKALNHLKE-NLKIIHRDIKPSNILLDR---SGNIKLCDFGISGQL------VDSIAKTRD-AGCRP 279
Cdd:cd13990  102 IPEREARSIIMQVVSALKYLNEiKPPIIHYDLKPGNILLHSgnvSGEIKITDFGLSKIMddesynSDGMELTSQgAGTYW 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 280 YMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQL--------TQVVKGDPPQLSNSEErefspsf 351
Cdd:cd13990  182 YLPPECFVVGKTPPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILeentilkaTEVEFPSKPVVSSEAK------- 254
                        170       180
                 ....*....|....*....|....*.
gi 526479851 352 iNFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd13990  255 -DFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
119-372 2.21e-15

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: 75.76  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKR-IRstVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTSFd 197
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKElIR--FDEETQRTFLKEVKV-MRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 kfYKYVYSVLDDVIP--EEILGKITLATVKALNHlkeNLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSiaKTRDA 275
Cdd:cd14221   77 --LRGIIKSMDSHYPwsQRVSFAKDIASGMAYLH---SMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDE--KTQPE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCR----------------PY-MAPERIDPsasrQGYDVRSDVWSLGITLYELaTGRfpypkwnsvfdqltqvVKGDPPQ 338
Cdd:cd14221  150 GLRslkkpdrkkrytvvgnPYwMAPEMING----RSYDEKVDVFSFGIVLCEI-IGR----------------VNADPDY 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 339 LSNSEE-----REF---------SPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd14221  209 LPRTMDfglnvRGFldrycppncPPSFFPIAVLCCDLDPEKRPSFSKL 256
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
109-377 2.30e-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: 76.99  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 109 TAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVD-EKEQKQLLMDLDVVMRSSDCPYIVQFYGAlFREGDcWI 187
Cdd:cd05594   23 TMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYS-FQTHD-RL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFDKFYKYVYSvlDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD 267
Cdd:cd05594  101 CFVMEYANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRD-AGCRPYMAPERIDPSasrqGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGDPPQLSnseeRE 346
Cdd:cd05594  179 DGATMKTfCGTPEYLAPEVLEDN----DYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEEIRFP----RT 248
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 347 FSPSFINFVNLCLTKDESKR-----PKYKELLKHPF 377
Cdd:cd05594  249 LSPEAKSLLSGLLKKDPKQRlgggpDDAKEIMQHKF 284
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
119-318 2.52e-15

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: 76.27  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVdekeqkqLLMDLDV----VMR-----SSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNQYFAIKALKKDV-------VLEDDDVectmIERrvlalASQHPFLTHLFCTFQTESHLFFVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 E------LM-----STSFD----KFYKyvysvlddvipEEIlgkitlatVKALNHLKENLkIIHRDIKPSNILLDRSGNI 254
Cdd:cd05592   76 EylnggdLMfhiqqSGRFDedraRFYG-----------AEI--------ICGLQFLHSRG-IIYRDLKLDNVLLDREGHI 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 255 KLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIDPsasrQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05592  136 KIADFGMCKENIYGENKASTfCGTPDYIAPEILKG----QKYNQSVDWWSFGVLLYEMLIGQSPF 196
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
119-378 2.57e-15

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: 75.56  E-value: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGdcWIC----MELMST 194
Cdd:cd14077    9 IGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISRDIRTIREAALSSLLNHP--HICrlrdFLRTPN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVY--SVLDDVIP-----EEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS----- 262
Cdd:cd14077   87 HYYMLFEYVDggQLLDYIIShgklkEKQARKFARQIASALDYLHRN-SIVHRDLKIENILISKSGNIKIIDFGLSnlydp 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 --------GQLVDSIAKTRDAgcRPYMAPEridpsasrqgydvrSDVWSLGITLYELATGRFPYPKWN-SVFDQLTQVVK 333
Cdd:cd14077  166 rrllrtfcGSLYFAAPELLQA--QPYTGPE--------------VDVWSFGVVLYVLVCGKVPFDDENmPALHAKIKKGK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 334 GDPPQLSNSEerefspsFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14077  230 VEYPSYLSSE-------CKSLISRMLVVDPKKRATLEQVLNHPWM 267
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
111-373 2.92e-15

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: 74.99  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGsvnkMVHKPSGQI---MAVKRIR----STVDEKEQKQLLMDLDvvmrssdCPYIVQFYGALFREG 183
Cdd:cd05112    4 SELTFVQEIGSGQFG----LVHLGYWLNkdkVAIKTIRegamSEEDFIEEAEVMMKLS-------HPKLVQLYGVCLEQA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 184 DCWICMELMS----TSFDKFYKYVYSvlddvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDF 259
Cdd:cd05112   73 PICLVFEFMEhgclSDYLRTQRGLFS-------AETLLGMCLDVCEGMAYLEEA-SVIHRDLAARNCLVGENQVVKVSDF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQLVDSiAKTRDAGCR---PYMAPERIdpSASRqgYDVRSDVWSLGITLYEL-ATGRFPYP-KWNS-VFDQLTQVVK 333
Cdd:cd05112  145 GMTRFVLDD-QYTSSTGTKfpvKWSSPEVF--SFSR--YSSKSDVWSFGVLMWEVfSEGKIPYEnRSNSeVVEDINAGFR 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 334 GDPPQLSnseerefSPSFINFVNLCLTKDESKRPKYKELL 373
Cdd:cd05112  220 LYKPRLA-------STHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
119-377 3.40e-15

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: 74.96  E-value: 3.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS-TSF 196
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIpHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSrKSL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDdviPE-EILGKITLATVKALnHLKenlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL--VDSIAKTR 273
Cdd:cd14189   89 AHIWKARHTLLE---PEvRYYLKQIISGLKYL-HLK---GILHRDLKLGNFFINENMELKVGDFGLAARLepPEQRKKTI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 dAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN--SVFDQLTQVVKGDPPQLsnseerefSPSF 351
Cdd:cd14189  162 -CGTPNYLAPEVL----LRQGHGPESDVWSLGCVMYTLLCGNPPFETLDlkETYRCIKQVKYTLPASL--------SLPA 228
                        250       260
                 ....*....|....*....|....*.
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14189  229 RHLLAGILKRNPGDRLTLDQILEHEF 254
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
118-377 3.46e-15

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: 74.93  E-value: 3.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRI--RStvdeKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14107    9 EIGRGTFGFVKRVTHKGNGECCAAKFIplRS----STRARAFQERDILARLSH-RRLTCLLDQFETRKTLILILELCSSE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDKFYKyvysvlDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL--DRSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14107   84 elLDRLFL------KGVVTEAEVKLYIQQVLEGIGYLHGM-NILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIDPSASRQGydvrSDVWSLGITLYELATGRFPYPKWN---SVFDQLTQVVKGDPPQLSN-SEEREf 347
Cdd:cd14107  157 FSKYGSPEFVAPEIVHQEPVSAA----TDIWALGVIAYLSLTCHSPFAGENdraTLLNVAEGVVSWDTPEITHlSEDAK- 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 348 spsfiNFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14107  232 -----DFIKRVLQPDPEKRPSASECLSHEW 256
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
111-318 3.49e-15

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: 76.62  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRkADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 EL-----MSTSFDKfykyvysvlDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd05628   81 EFlpggdMMTLLMK---------KDTLTEEETQFYIAETVLAIDSIHQ-LGFIHRDIKPDNLLLDSKGHVKLSDFGLCTG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 L---------------------VDSIAKTRDA---------------GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITL 308
Cdd:cd05628  151 LkkahrtefyrnlnhslpsdftFQNMNSKRKAetwkrnrrqlafstvGTPDYIAPEVF----MQTGYNKLCDWWSLGVIM 226
                        250
                 ....*....|
gi 526479851 309 YELATGRFPY 318
Cdd:cd05628  227 YEMLIGYPPF 236
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
119-378 3.76e-15

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: 75.41  E-value: 3.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRStVDEKEQKQLLMDLDVVMR--SSDCPYIVQFYGAlfrEGDCWICMELMSTS- 195
Cdd:cd14166   11 LGSGAFSEVYLVKQRSTGKLYALKCIKK-SPLSRDSSLENEIAVLKRikHENIVTLEDIYES---TTHYYLVMQLVSGGe 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 -FDKfykyvysVLD-DVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL---DRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd14166   87 lFDR-------ILErGVYTEKDASRVINQVLSAVKYLHEN-GIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQNGIM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDPPQLSNSEEREFSPS 350
Cdd:cd14166  159 STA-CGTPGYVAPEVL----AQKPYSKAVDCWSIGVITYILLCGYPPFYEETE--SRLFEKIKEGYYEFESPFWDDISES 231
                        250       260
                 ....*....|....*....|....*...
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14166  232 AKDFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
227-377 3.95e-15

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: 75.08  E-value: 3.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 227 LNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS-IAKTRdAGCRPYMAPERIDpsasRQGYDVRSDVWSLG 305
Cdd:cd05605  115 LEHL-HSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGeTIRGR-VGTVGYMAPEVVK----NERYTFSPDWWGLG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 306 ITLYELATGRFPY------PKWNSVfdqlTQVVKGDPPQLSNSeereFSPSFINFVNLCLTKDESKR-----PKYKELLK 374
Cdd:cd05605  189 CLIYEMIEGQAPFrarkekVKREEV----DRRVKEDQEEYSEK----FSEEAKSICSQLLQKDPKTRlgcrgEGAEDVKS 260

                 ...
gi 526479851 375 HPF 377
Cdd:cd05605  261 HPF 263
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
211-378 3.99e-15

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK 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: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 75.69  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 211 IPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDrSGNI--KLCDFG----ISGQLVDSIaKTrdagcRPYMAPE 284
Cdd:cd14136  116 IPLPLVKKIARQVLQGLDYLHTKCGIIHTDIKPENVLLC-ISKIevKIADLGnacwTDKHFTEDI-QT-----RQYRSPE 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 285 RIDPSasrqGYDVRSDVWSLGITLYELATGRF-----PYPKWNSVFDQLTQVVK--GD-PPQ--LSNSEEREF------- 347
Cdd:cd14136  189 VILGA----GYGTPADIWSTACMAFELATGDYlfdphSGEDYSRDEDHLALIIEllGRiPRSiiLSGKYSREFfnrkgel 264
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 348 -------------------------SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14136  265 rhisklkpwpledvlvekykwskeeAKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
112-372 4.08e-15

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 75.49  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIM----AVKRIRSTVDEKEQKQLlMDLDVVMRSSDCPYIVQFYGALFREgDCWI 187
Cdd:cd05110    8 ELKRVKVLGSGAFGTVYKGIWVPEGETVkipvAIKILNETTGPKANVEF-MDEALIMASMDHPHLVRLLGVCLSP-TIQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFdkFYKYVYSVLDDvIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV- 266
Cdd:cd05110   86 VTQLMPHGC--LLDYVHEHKDN-IGSQLLLNWCVQIAKGMMYLEER-RLVHRDLAARNVLVKSPNHVKITDFGLARLLEg 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYpkwnsvfdqlTQVVKGDPPQLSNSE 343
Cdd:cd05110  162 DEKEYNADGGKMPikWMALECI----HYRKFTHQSDVWSYGVTIWELMTfGGKPY----------DGIPTREIPDLLEKG 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 344 EREFSPSFINF-----VNLCLTKDESKRPKYKEL 372
Cdd:cd05110  228 ERLPQPPICTIdvymvMVKCWMIDADSRPKFKEL 261
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
119-375 4.14e-15

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: 74.45  E-value: 4.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVdekEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS----- 193
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFD---EQRSFLKEVKL-MRRLSHPNILRFIGVCVKDNKLNFITEYVNggtle 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 ---TSFDKFYKYvysvlddviPEEILGKITLATVKALNHLKenlKIIHRDIKPSNILL---DRSGNIKLCDFGISGQLVD 267
Cdd:cd14065   77 ellKSMDEQLPW---------SQRVSLAKDIASGMAYLHSK---NIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRDAGCR------PY-MAPERIdpsaSRQGYDVRSDVWSLGITLYELaTGRFPypkwnsvfdqltqvvkGDPPQLS 340
Cdd:cd14065  145 EKTKKPDRKKRltvvgsPYwMAPEML----RGESYDEKVDVFSFGIVLCEI-IGRVP----------------ADPDYLP 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 341 NSEE-----REFS--------PSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14065  204 RTMDfgldvRAFRtlyvpdcpPSFLPLAIRCCQLDPEKRPSFVELEHH 251
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
116-377 4.58e-15

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: 75.26  E-value: 4.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE-QKQLLMDLDVVMRSSDCPYIVQFYGALFREGD----CWICME 190
Cdd:cd07837    6 LEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGvPSTALREVSLLQMLSQSIYIVRLLDVEHVEENgkplLYLVFE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRS-GNIKLCDFGISGQLVDSI 269
Cdd:cd07837   86 YLDTDLKKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSH-GVMHRDLKPQNLLVDKQkGLLKIADLGLGRAFTIPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AK-TRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK--GDP---------- 336
Cdd:cd07837  165 KSyTHEIVTLWYRAPEVLLGSTH---YSTPVDMWSVGCIFAEMSRKQPLFPG-DSELQQLLHIFRllGTPneevwpgvsk 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526479851 337 -----------PQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07837  241 lrdwheypqwkPQDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
140-313 4.76e-15

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: 75.13  E-value: 4.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 140 AVKRIRSTVDEKEQKQL---LMDLDVVMRSSDCPYIVQFYG-ALFREGDCWICMELMSTS-FDKFYKYVYSVLDDVIPEE 214
Cdd:cd14001   32 AVKKINSKCDKGQRSLYqerLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLAMEYGGKSlNDLIEERYEAGLGPFPAAT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 215 ILgKITLATVKALNHLKENLKIIHRDIKPSNILLdrSGN---IKLCDFGISGQL-----VDSIAKTRDAGCRPYMAPERI 286
Cdd:cd14001  112 IL-KVALSIARALEYLHNEKKILHGDIKSGNVLI--KGDfesVKLCDFGVSLPLtenleVDSDPKAQYVGTEPWKAKEAL 188
                        170       180
                 ....*....|....*....|....*....
gi 526479851 287 DpsasrQGYDV--RSDVWSLGITLYELAT 313
Cdd:cd14001  189 E-----EGGVItdKADIFAYGLVLWEMMT 212
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
236-377 4.78e-15

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: 74.33  E-value: 4.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 236 IIHRDIKPSNILLDRSGN---------IKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIdpsASRQgYDVRSDVWSLGI 306
Cdd:cd14120  113 IVHRDLKPQNILLSHNSGrkpspndirLKIADFGFARFLQDGMMAATLCGSPMYMAPEVI---MSLQ-YDAKADLWSIGT 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 307 TLYELATGRFPYpKWNSvfdqltqvvkgdPPQLSNSEER----------EFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14120  189 IVYQCLTGKAPF-QAQT------------PQELKAFYEKnanlrpnipsGTSPALKDLLLGLLKRNPKDRIDFEDFFSHP 255

                 .
gi 526479851 377 F 377
Cdd:cd14120  256 F 256
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
116-377 5.44e-15

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: 75.10  E-value: 5.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRStvdEKEQK----------QLLMDLD----------VVMRSSDCPYIVQF 175
Cdd:cd07845   12 LNRIGEGTYGIVYRARDTTSGEIVALKKVRM---DNERDgipisslreiTLLLNLRhpnivelkevVVGKHLDSIFLVME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 176 YGalfrEGDCWICMELMSTSFdkfykyvysvlddviPEEILGKITLATVKALNHLKENLkIIHRDIKPSNILLDRSGNIK 255
Cdd:cd07845   89 YC----EQDLASLLDNMPTPF---------------SESQVKCLMLQLLRGLQYLHENF-IIHRDLKVSNLLLTDKGCLK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 256 LCDFGisgqlvdsIAKTRDAGCRP---------YMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRfPYPKWNSVFD 326
Cdd:cd07845  149 IADFG--------LARTYGLPAKPmtpkvvtlwYRAPELLLGCTT---YTTAIDMWAVGCILAELLAHK-PLLPGKSEIE 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 327 QLTQVVK--GDP-----PQLS---------------NSEEREF---SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07845  217 QLDLIIQllGTPnesiwPGFSdlplvgkftlpkqpyNNLKHKFpwlSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
119-324 5.89e-15

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: 74.79  E-value: 5.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVK--RIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGA-----LFREGDC-WICME 190
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkcRQELSPSDKNRERWCLEVQI-MKKLNHPNVVSARDVppeleKLSPNDLpLLAME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdKFYKYV-----YSVLDDVIPEEILGKITlatvKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCDFGIS 262
Cdd:cd13989   80 YCSGG--DLRKVLnqpenCCGLKESEVRTLLSDIS----SAISYLHEN-RIIHRDLKPENIVLQQGGGrviYKLIDLGYA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 263 GQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY-PKWNSV 324
Cdd:cd13989  153 KELDQGSLCTSFVGTLQYLAPELF----ESKKYTCTVDYWSFGTLAFECITGYRPFlPNWQPV 211
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
119-366 7.00e-15

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: 75.10  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMR---SSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd05633   13 IGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTrD 274
Cdd:cd05633   93 GDLHYHLSQHGVFS----EKEMRFYATEIILGLEHM-HNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHA-S 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKWNSV----FDQLTQVVKGDPPQlsnseerEFSPS 350
Cdd:cd05633  167 VGTHGYMAPEVLQKGTA---YDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkheIDRMTLTVNVELPD-------SFSPE 236
                        250
                 ....*....|....*.
gi 526479851 351 FINFVNLCLTKDESKR 366
Cdd:cd05633  237 LKSLLEGLLQRDVSKR 252
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
119-377 7.20e-15

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: 73.89  E-value: 7.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVM-RSSDCPYIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd14188    9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELhRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYVYSVLDDVIPEEILGKItlatVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD-AG 276
Cdd:cd14188   89 AHILKARKVLTEPEVRYYLRQI----VSGLKYLHEQ-EILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTiCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 277 CRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKWN--SVFDQLTQVVKGDPPQLSNSEErefspsfiNF 354
Cdd:cd14188  164 TPNYLSPEVLN----KQGHGCESDIWALGCVMYTMLLGRPPFETTNlkETYRCIREARYSLPSSLLAPAK--------HL 231
                        250       260
                 ....*....|....*....|...
gi 526479851 355 VNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14188  232 IASMLSKNPEDRPSLDEIIRHDF 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
119-318 7.34e-15

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: 74.36  E-value: 7.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMRSSDCPYIVQfygalfregdcwicmelMSTSFd 197
Cdd:cd14209    9 LGTGSFGRVMLVRHKETGNYYAMKILdKQKVVKLKQVEHTLNEKRILQAINFPFLVK-----------------LEYSF- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYVYSVLDDVIPEEIL------GKIT--------LATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISg 263
Cdd:cd14209   71 KDNSNLYMVMEYVPGGEMFshlrriGRFSepharfyaAQIVLAFEYL-HSLDLIYRDLKPENLLIDQQGYIKVTDFGFA- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 264 QLVDSIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd14209  149 KRVKGRTWTL-CGTPEYLAPEII----LSKGYNKAVDWWALGVLIYEMAAGYPPF 198
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
119-374 9.88e-15

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: 73.48  E-value: 9.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRIRSTVDEK-----EQKQLLMDLDVVMRSsdcPYIVQFYGALFREGDCWICMElms 193
Cdd:cd14148    2 IGVGGFGKVYKGLWR--GEEVAVKAARQDPDEDiavtaENVRQEARLFWMLQH---PNIIALRGVCLNPPHLCLVME--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 tsFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKEN--LKIIHRDIKPSNIL-LDRSGN-------IKLCDFGISG 263
Cdd:cd14148   74 --YARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEaiVPIIHRDLKSSNILiLEPIENddlsgktLKITDFGLAR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QLvDSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSV-------FDQLTQVVKGDP 336
Cdd:cd14148  152 EW-HKTTKMSAAGTYAWMAPEVIRLSL----FSKSSDVWSFGVLLWELLTGEVPYREIDALavaygvaMNKLTLPIPSTC 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 526479851 337 PQlsnseerefspSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14148  227 PE-----------PFARLLEECWDPDPHGRPDFGSILK 253
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
111-378 1.12e-14

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: 73.50  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGE-IGRGAYGSVNKMVHKPSGQIMAVKRIRS-TVDEKEQkqlLMDLDVVMRSSDCPYIVQFYGALfrEGDCWIC 188
Cdd:cd14191    1 SDFYDIEErLGSGKFGQVFRLVEKKTKKVWAGKFFKAySAKEKEN---IRQEISIMNCLHHPKLVQCVDAF--EEKANIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNIL-LDRSGN-IKLCDFGISGQLV 266
Cdd:cd14191   76 MVLEMVSGGELFERIIDEDFELTERECI-KYMRQISEGVEYIHKQ-GIVHLDLKPENIMcVNKTGTkIKLIDFGLARRLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPERIDPSASrqGYDvrSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDPPQLSNSEERE 346
Cdd:cd14191  154 NAGSLKVLFGTPEFVAPEVINYEPI--GYA--TDMWSIGVICYILVSGLSPFMGDND--NETLANVTSATWDFDDEAFDE 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14191  228 ISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
111-378 1.18e-14

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: 73.45  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLG-EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLL---MDLDV-VMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd14196    4 EDFYDIGeELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSreeIEREVsILRQVLHPNIITLHDVYENRTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTS--FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNI-LLDRSG---NIKLCDF 259
Cdd:cd14196   84 VLILELVSGGelFD------FLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENImLLDKNIpipHIKLIDF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISGQLVDSIAKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYpkwnsvFDQLTQVVKGDPPQL 339
Cdd:cd14196  157 GLAHEIEDGVEFKNIFGTPEFVAPEIVN----YEPLGLEADMWSIGVITYILLSGASPF------LGDTKQETLANITAV 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 526479851 340 SNSEEREF----SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14196  227 SYDFDEEFfshtSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
108-390 1.25e-14

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: 73.36  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE--QKQLLMDLDVVMRSSDcPYIVQFYGALFREGDC 185
Cdd:cd14117    3 FTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgvEHQLRREIEIQSHLRH-PNILRLYNYFHDRKRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfdKFYKYV--YSVLDDVIPEEILGKITlatvKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISG 263
Cdd:cd14117   82 YLILEYAPRG--ELYKELqkHGRFDEQRTATFMEELA----DALHYCHEK-KVIHRDIKPENLLMGYKGELKIADFGWSV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 QlVDSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPY--PKWNSVFDQLTQVVKGDPPQLSN 341
Cdd:cd14117  155 H-APSLRRRTMCGTLDYLPPEMIEGRT----HDEKVDLWCIGVLCYELLVGMPPFesASHTETYRRIVKVDLKFPPFLSD 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 526479851 342 SEErefspsfiNFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVAC 390
Cdd:cd14117  230 GSR--------DLISKLLRYHPSERLPLKGVMEHPWVKANSRRVLPPVY 270
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
118-377 1.34e-14

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: 73.57  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM----ELMS 193
Cdd:cd14032    8 ELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKGKRCIvlvtELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLK-IIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14032   88 SGTLKTYLKRFKVMK----PKVLRSWCRQILKGLLFLHTRTPpIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRdAGCRPYMAPERIDpsasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQlsnSEEREFSPSF 351
Cdd:cd14032  164 SV-IGTPEFMAPEMYE-----EHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPA---SFEKVTDPEI 234
                        250       260
                 ....*....|....*....|....*.
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14032  235 KEIIGECICKNKEERYEIKDLLSHAF 260
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
118-377 1.35e-14

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: 73.11  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGA---LFREGDCWICM-ELMS 193
Cdd:cd14033    8 EIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSwksTVRGHKCIILVtELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLK-IIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14033   88 SGTLKTYLKRFREMK----LKLLQRWSRQILKGLHFLHSRCPpILHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRdAGCRPYMAPERIDpsasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPqlsNSEEREFSPSF 351
Cdd:cd14033  164 SV-IGTPEFMAPEMYE-----EKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKP---DSFYKVKVPEL 234
                        250       260
                 ....*....|....*....|....*.
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14033  235 KEIIEGCIRTDKDERFTIQDLLEHRF 260
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
117-372 1.49e-14

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: 73.31  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQkqllMDLDVVMRSsdcPYIVQFYGALfREGDcW--ICMELMST 194
Cdd:cd13991   12 LRIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEE----LMACAGLTS---PRVVPLYGAV-REGP-WvnIFMDLKEG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 -SFDKFYKyvysvLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSG-NIKLCDFGIS------GQLV 266
Cdd:cd13991   83 gSLGQLIK-----EQGCLPEDRALHYLGQALEGLEYL-HSRKILHGDVKADNVLLSSDGsDAFLCDFGHAecldpdGLGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPE--RIDPSasrqgyDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDPPQLsnsee 344
Cdd:cd13991  157 SLFTGDYIPGTETHMAPEvvLGKPC------DAKVDVWSSCCMMLHMLNGCHPWTQYYS--GPLCLKIANEPPPL----- 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 345 REFSPSFINF----VNLCLTKDESKRPKYKEL 372
Cdd:cd13991  224 REIPPSCAPLtaqaIQAGLRKEPVHRASAAEL 255
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
112-378 1.76e-14

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: 72.95  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLgeIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQllMDLDVVMRSSDcPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14087    4 DIKAL--IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCE--SELNVLRRVRH-TNIIQLIEVFETKERVYMVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTS--FDKFY-KYVYSVLDdviPEEILgKITLATVKALNhlkeNLKIIHRDIKPSNILLDRSGN---IKLCDFGISGQL 265
Cdd:cd14087   79 ATGGelFDRIIaKGSFTERD---ATRVL-QMVLDGVKYLH----GLGITHRDLKPENLLYYHPGPdskIMITDFGLASTR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 --VDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGdppQLSNSE 343
Cdd:cd14087  151 kkGPNCLMKTTCGTPEYIAPEIL----LRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRT-RLYRQILRA---KYSYSG 222
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 344 E--REFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14087  223 EpwPSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
117-374 1.80e-14

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: 72.73  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEI-GRGAYGSVNKMVHKPSGQImAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd05085    1 GELlGKGNFGEVYKGTLKDKTPV-AVKTCKEDLPQELKIKFLSEARI-LKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fdKFYKYVYSVLDDVIPEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDA 275
Cdd:cd05085   79 --DFLSFLRKKKDELKTKQLV-KFSLDAAAGMAYL-ESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYE-LATGRFPYPKWNS--VFDQLTQVVKGDPPQLSNSEerefsps 350
Cdd:cd05085  155 KQIPikWTAPEALNYGR----YSSESDVWSFGILLWEtFSLGVCPYPGMTNqqAREQVEKGYRMSAPQRCPED------- 223
                        250       260
                 ....*....|....*....|....
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05085  224 IYKIMQRCWDYNPENRPKFSELQK 247
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
116-318 1.92e-14

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: 72.58  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGE-IGRGAYGSVNKMV---HKPSGQIMAVKRIRSTVDEKeQKQLLMDLDVvMRSSDCPYIVQFYGAL-FREGDCWICME 190
Cdd:cd14164    4 LGTtIGEGSFSKVKLATsqkYCCKVAIKIVDRRRASPDFV-QKFLPRELSI-LRRVNHPNIVQMFECIeVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKYVYsvlddVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSG-NIKLCDFGISGQLVD-S 268
Cdd:cd14164   82 AAATDLLQKIQEVH-----HIPKDLARDMFAQMVGAVNYLHD-MNIVHRDLKCENILLSADDrKIKIADFGFARFVEDyP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 269 IAKTRDAGCRPYMAPERIdpsaSRQGYDVRS-DVWSLGITLYELATGRFPY 318
Cdd:cd14164  156 ELSTTFCGSRAYTPPEVI----LGTPYDPKKyDVWSLGVVLYVMVTGTMPF 202
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
114-377 1.95e-14

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: 73.28  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd07836    3 KQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIREISL-MKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKfYKYVYSVLddvipeeilGKITLATVKALNH--LK------ENlKIIHRDIKPSNILLDRSGNIKLCDFGIS--- 262
Cdd:cd07836   82 KDLKK-YMDTHGVR---------GALDPNTVKSFTYqlLKgiafchEN-RVLHRDLKPQNLLINKRGELKLADFGLAraf 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLVDSIAKtrDAGCRPYMAPERIdpSASRQgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--GDP---- 336
Cdd:cd07836  151 GIPVNTFSN--EVVTLWYRAPDVL--LGSRT-YSTSIDIWSVGCIMAEMITGRPLFPGTNNE-DQLLKIFRimGTPtest 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 337 -PQLSNSEERE-----------------FSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07836  225 wPGISQLPEYKptfpryppqdlqqlfphADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
119-377 2.05e-14

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: 72.66  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDV-VMRSSDCPYIVQFYGaLFREGD-CWICMEL-MSTS 195
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIaIHRSLAHQHVVGFHG-FFEDNDfVYVVLELcRRRS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYKYVYSVLDdviPEeilGKITL-ATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL-VDSIAKTR 273
Cdd:cd14187   94 LLELHKRRKALTE---PE---ARYYLrQIILGCQYLHRN-RVIHRDLKLGNLFLNDDMEVKIGDFGLATKVeYDGERKKT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPkwnsvfdqlTQVVKGDPPQLSNSE---EREFSPS 350
Cdd:cd14187  167 LCGTPNYIAPEVL----SKKGHSFEVDIWSIGCIMYTLLVGKPPFE---------TSCLKETYLRIKKNEysiPKHINPV 233
                        250       260
                 ....*....|....*....|....*..
gi 526479851 351 FINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14187  234 AASLIQKMLQTDPTARPTINELLNDEF 260
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
119-379 2.41e-14

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: 73.50  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVD-EKEQKQLLMDLDVVMRSSDCPYIVQFYGAlFREGD--CWIcMELMSTS 195
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIiAKDEVAHTVTESRVLQNTRHPFLTALKYA-FQTHDrlCFV-MEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 fDKFYkyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD- 274
Cdd:cd05595   81 -ELFF---HLSRERVFTEDRARFYGAEIVSALEYLHSR-DVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTf 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIDPSasrqGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQLTQVVKGDPPQLSnseeREFSPSFINF 354
Cdd:cd05595  156 CGTPEYLAPEVLEDN----DYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHERLFELILMEEIRFP----RTLSPEAKSL 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 526479851 355 VNLCLTKDESKR-----PKYKELLKHPFIL 379
Cdd:cd05595  226 LAGLLKKDPKQRlgggpSDAKEVMEHRFFL 255
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
224-377 2.42e-14

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: 73.54  E-value: 2.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 224 VKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIDPSasrqGYDVRSDVW 302
Cdd:cd05571  105 VLALGYLHSQ-GIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTfCGTPEYLAPEVLEDN----DYGRAVDWW 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 303 SLGITLYELATGRFPYpkWNSVFDQLTQVVKGDPPQLSnseeREFSPSFINFVNLCLTKDESKR-----PKYKELLKHPF 377
Cdd:cd05571  180 GLGVVMYEMMCGRLPF--YNRDHEVLFELILMEEVRFP----STLSPEAKSLLAGLLKKDPKKRlgggpRDAKEIMEHPF 253
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
116-377 2.62e-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: 73.37  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRS----TVDEK-EQKQL--LMDLDVVMRSsdcpYIVQFYGALFREGDcwIC 188
Cdd:cd14134   17 LRLLGEGTFGKVLECWDRKRKRYVAVKIIRNvekyREAAKiEIDVLetLAEKDPNGKS----HCVQLRDWFDYRGH--MC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MelmstSFDKFYKYVYSVLDD----VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLD--------------- 249
Cdd:cd14134   91 I-----VFELLGPSLYDFLKKnnygPFPLEHVQHIAKQLLEAVAFLHDL-KLTHTDLKPENILLVdsdyvkvynpkkkrq 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 250 ----RSGNIKLCDFGiSGQLVD----SIAKTRdagcrPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGR--F--- 316
Cdd:cd14134  165 irvpKSTDIKLIDFG-SATFDDeyhsSIVSTR-----HYRAPEVI----LGLGWSYPCDVWSIGCILVELYTGEllFqth 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 317 --------------PYPKW--------NSVFDQ------------LTQVVKGDPPQLSNSEEREFS--PSFINFVNLCLT 360
Cdd:cd14134  235 dnlehlammerilgPLPKRmirrakkgAKYFYFyhgrldwpegssSGRSIKRVCKPLKRLMLLVDPehRLLFDLIRKMLE 314
                        330
                 ....*....|....*..
gi 526479851 361 KDESKRPKYKELLKHPF 377
Cdd:cd14134  315 YDPSKRITAKEALKHPF 331
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
119-318 3.00e-14

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: 72.18  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRIRS-TVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGAlfregdcwiCMELMStSFD 197
Cdd:cd14064    1 IGSGSFGKVYKGRCR--NKIVAIKRYRAnTYCSKSDVDMFCREVSILCRLNHPCVIQFVGA---------CLDDPS-QFA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYV-----YSVLDD---VIPEEILGKITLATVKALNHLKENLK-IIHRDIKPSNILLDRSGNIKLCDFGISG--QLV 266
Cdd:cd14064   69 IVTQYVsggslFSLLHEqkrVIDLQSKLIIAVDVAKGMEYLHNLTQpIIHRDLNSHNILLYEDGHAVVADFGESRflQSL 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526479851 267 DSIAKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd14064  149 DEDNMTKQPGNLRWMAPEVFTQCTR---YSIKADVFSYALCLWELLTGEIPF 197
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
119-366 3.01e-14

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: 73.16  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVVMR---SSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14223    8 IGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVYSVLDDVIPEEILGKITLAtvkaLNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTrD 274
Cdd:cd14223   88 GDLHYHLSQHGVFSEAEMRFYAAEIILG----LEHM-HSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHA-S 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKWNSV----FDQLTQVVKGDPPQlsnseerEFSPS 350
Cdd:cd14223  162 VGTHGYMAPEVLQKGVA---YDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkheIDRMTLTMAVELPD-------SFSPE 231
                        250
                 ....*....|....*.
gi 526479851 351 FINFVNLCLTKDESKR 366
Cdd:cd14223  232 LRSLLEGLLQRDVNRR 247
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
111-373 3.10e-14

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members 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, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx 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: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 72.22  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNkmVHKPSGQI-MAVKRIR----STVDEKEQKQLLMDLDvvmrssdCPYIVQFYGALFREGDC 185
Cdd:cd05113    4 KDLTFLKELGTGQFGVVK--YGKWRGQYdVAIKMIKegsmSEDEFIEEAKVMMNLS-------HEKLVQLYGVCTKQRPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSFdkFYKYVYSVLDDVIPEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd05113   75 FIITEYMANGC--LLNYLREMRKRFQTQQLL-EMCKDVCEAMEYL-ESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSiAKTRDAGCR---PYMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWNS--VFDQLTQVVKGDPPQL 339
Cdd:cd05113  151 LDD-EYTSSVGSKfpvRWSPPEVLMYSK----FSSKSDVWAFGVLMWEVYSlGKMPYERFTNseTVEHVSQGLRLYRPHL 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 340 SnseerefSPSFINFVNLCLTKDESKRPKYKELL 373
Cdd:cd05113  226 A-------SEKVYTIMYSCWHEKADERPTFKILL 252
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
217-381 3.37e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 74.14  E-value: 3.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 217 GKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS----GQLVDSIAKTRdAGCRPYMAPEridpSASR 292
Cdd:PTZ00283 146 GLLFIQVLLAVHHVHSK-HMIHRDIKSANILLCSNGLVKLGDFGFSkmyaATVSDDVGRTF-CGTPYYVAPE----IWRR 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 293 QGYDVRSDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKG--DP-PQlsnseerEFSPSFINFVNLCLTKDESKRPKY 369
Cdd:PTZ00283 220 KPYSKKADMFSLGVLLYELLTLKRPFDGEN-MEEVMHKTLAGryDPlPP-------SISPEMQEIVTALLSSDPKRRPSS 291
                        170
                 ....*....|..
gi 526479851 370 KELLKHPFILMY 381
Cdd:PTZ00283 292 SKLLNMPICKLF 303
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
119-378 4.15e-14

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: 71.87  E-value: 4.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRsTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKIIK-ARSQKEKEEVKNEIEV-MNQLNHANLIQLYDAFESRNDIVLVMEYVDGGelF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFY--KYVYSVLDDVIpeeILGKITlatvKALNHLKEnLKIIHRDIKPSNIL-LDRSGN-IKLCDFGISGQLVDSIAKT 272
Cdd:cd14193   90 DRIIdeNYNLTELDTIL---FIKQIC----EGIQYMHQ-MYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRPYMAPERIDpsasrqgYDVRS---DVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDpPQLSNSEEREFSP 349
Cdd:cd14193  162 VNFGTPEFLAPEVVN-------YEFVSfptDMWSLGVIAYMLLSGLSPFLGEDDN-ETLNNILACQ-WDFEDEEFADISE 232
                        250       260
                 ....*....|....*....|....*....
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14193  233 EAKDFISKLLIKEKSWRMSASEALKHPWL 261
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
119-372 4.45e-14

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl 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: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 71.68  E-value: 4.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRStvDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfdK 198
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVKTLKE--DTMEVEEFLKEA-AVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYG--N 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 FYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgQLVDSIAKTRDAGCR 278
Cdd:cd05052   89 LLDYLRECNREELNAVVLLYMATQIASAMEYLEKK-NFIHRDLAARNCLVGENHLVKVADFGLS-RLMTGDTYTAHAGAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 279 ---PYMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP--KWNSVFDQLTQVVKGDPPQlsnseerEFSPSFI 352
Cdd:cd05052  167 fpiKWTAPE----SLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPgiDLSQVYELLEKGYRMERPE-------GCPPKVY 235
                        250       260
                 ....*....|....*....|
gi 526479851 353 NFVNLCLTKDESKRPKYKEL 372
Cdd:cd05052  236 ELMRACWQWNPSDRPSFAEI 255
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
116-378 4.45e-14

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: 72.30  E-value: 4.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIR----------STVDEKeqkQLLMDLDvvmrSSDCPYIVQFYG--ALFREg 183
Cdd:cd07863    5 VAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtnedglplSTVREV---ALLKRLE----AFDHPNIVRLMDvcATSRT- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 184 DCWICMELMSTSFDKFYK-YVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd07863   77 DRETKVTLVFEHVDQDLRtYLDKVPPPGLPAETIKDLMRQFLRGLDFLHAN-CIVHRDLKPENILVTSGGQVKLADFGLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLVDSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATgRFPYPKWNSVFDQLTQV--VKGDPPQ-- 338
Cdd:cd07863  156 RIYSCQMALTPVVVTLWYRAPEVLLQST----YATPVDMWSVGCIFAEMFR-RKPLFCGNSEADQLGKIfdLIGLPPEdd 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 339 ------LSNSeerEFSPSFINFVNLC---------------LTKDESKRPKYKELLKHPFI 378
Cdd:cd07863  231 wprdvtLPRG---AFSPRGPRPVQSVvpeieesgaqlllemLTFNPHKRISAFRALQHPFF 288
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
117-372 4.57e-14

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: 71.61  E-value: 4.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHK-PSGQIMAVK-RIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALfrEGDCWI-CMELMS 193
Cdd:cd05060    1 KELGHGNFGSVRKGVYLmKSGKEVEVAvKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVC--KGEPLMlVMELAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 T-SFDKFYKYvysvlDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV--DSIA 270
Cdd:cd05060   79 LgPLLKYLKK-----RREIPVSDLKELAHQVAMGMAYL-ESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGagSDYY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYP--KWNSVFDQLTQVVKGDPPQlsnseer 345
Cdd:cd05060  153 RATTAGRWPlkWYAPECINYGK----FSSKSDVWSYGVTLWEAFSyGAKPYGemKGPEVIAMLESGERLPRPE------- 221
                        250       260
                 ....*....|....*....|....*..
gi 526479851 346 EFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05060  222 ECPQEIYSIMLSCWKYRPEDRPTFSEL 248
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
119-378 5.09e-14

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: 71.56  E-value: 5.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI--RSTVDEKEQKQLLMDLDVVmRSSDCPYIVQFYGAL-FREGDCWICMELMSTS 195
Cdd:cd14163    8 IGEGTYSKVKEAFSKKHQRKVAIKIIdkSGGPEEFIQRFLPRELQIV-ERLDHKNIIHVYEMLeSADGKIYLVMELAEDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLdRSGNIKLCDFGISGQLVDS---IA 270
Cdd:cd14163   87 dvFD------CVLHGGPLPEHRAKALFRQLVEAIRYC-HGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGgreLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRdAGCRPYMAPERID--PSASRQGydvrsDVWSLGITLYELATGRFPYPKWNsVFDQLTQVVKGD--PPQLSNSEERE 346
Cdd:cd14163  159 QTF-CGSTAYAAPEVLQgvPHDSRKG-----DIWSMGVVLYVMLCAQLPFDDTD-IPKMLCQQQKGVslPGHLGVSRTCQ 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 347 fspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14163  232 ------DLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-378 5.48e-14

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: 72.17  E-value: 5.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLG-EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDekeQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICM 189
Cdd:cd14085    2 EDFFEIEsELGRGATSVVYRCRQKGTQKPYAVKKLKKTVD---KKIVRTEIGVLLRLSH-PNIIKLKEIFETPTEISLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTS--FDKFY-KYVYSVLD--DVIpEEILgkitlatvKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCDFGI 261
Cdd:cd14085   78 ELVTGGelFDRIVeKGYYSERDaaDAV-KQIL--------EAVAYLHEN-GIVHRDLKPENLLYATPAPdapLKIADFGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 SGQLVDSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQ--LTQVVKGDPPQL 339
Cdd:cd14085  148 SKIVDQQVTMKTVCGTPGYCAPEILRGCA----YGPEVDMWSVGVITYILLCGFEPF--YDERGDQymFKRILNCDYDFV 221
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 340 SNSEErEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14085  222 SPWWD-DVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWV 259
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
119-377 5.98e-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: 72.51  E-value: 5.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALF----RE-GDCWICMELMS 193
Cdd:cd07859    8 IGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLppsrREfKDIYVVFELME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKfykyVYSVLDDVIPEEIlgKITL-ATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD----S 268
Cdd:cd07859   88 SDLHQ----VIKANDDLTPEHH--QFFLyQLLRALKYIHTA-NVFHRDLKPKNILANADCKLKICDFGLARVAFNdtptA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERIDPSASRqgYDVRSDVWSLGITLYELATGRFPYPKWNSV--FDQLTQVVkGDPPQLS-----N 341
Cdd:cd07859  161 IFWTDYVATRWYRAPELCGSFFSK--YTPAIDIWSIGCIFAEVLTGKPLFPGKNVVhqLDLITDLL-GTPSPETisrvrN 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 342 SEEREF-------------------SPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07859  238 EKARRYlssmrkkqpvpfsqkfpnaDPLALRLLERLLAFDPKDRPTAEEALADPY 292
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
119-374 6.25e-14

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: 71.37  E-value: 6.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVhKPSGQIMAVKRI--RSTVDEKEQKQLLMDL--DVVMRSsdcpyIVQFYGALFREGDCWICMELMST 194
Cdd:cd14664    1 IGRGGAGTVYKGV-MPNGTLVAVKRLkgEGTQGGDHGFQAEIQTlgMIRHRN-----IVRLRGYCSNPTTNLLVYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdkfykYVYSVLDDVIPE------EILGKITLATVKALNHLKENL--KIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd14664   75 G------SLGELLHSRPESqppldwETRQRIALGSARGLAYLHHDCspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 D--SIAKTRDAGCRPYMAPERIDPSASrqgyDVRSDVWSLGITLYELATGRFPY-----PKWNSVFDQLTQVVKG----- 334
Cdd:cd14664  149 DkdSHVMSSVAGSYGYIAPEYAYTGKV----SEKSDVYSYGVVLLELITGKRPFdeaflDDGVDIVDWVRGLLEEkkvea 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 335 --DPPQLSNSEEREFSPSFInFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14664  225 lvDPDLQGVYKLEEVEQVFQ-VALLCTQSSPMERPTMREVVR 265
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
119-377 7.10e-14

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: 70.76  E-value: 7.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdvvMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAAL---LQHLQHPQYITLHDTYESPTSYILVLELMDDGrlL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DkfykyvYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRS---GNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd14115   78 D------YLMNHDELMEEKVAFYIRDIMEALQYL-HNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHRHVHH 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAGCRPYMAPERIdpsasrQGYDVR--SDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGD---PPQLSNseerEFS 348
Cdd:cd14115  151 LLGNPEFAAPEVI------QGTPVSlaTDIWSIGVLTYVMLSGVSPFLD-ESKEETCINVCRVDfsfPDEYFG----DVS 219
                        250       260
                 ....*....|....*....|....*....
gi 526479851 349 PSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14115  220 QAARDFINVILQEDPRRRPTAATCLQHPW 248
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
115-318 7.23e-14

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: 71.83  E-value: 7.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGE--IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLlmdldVVMRSSDC-PYIVQFYGALFREGDCWICMEL 191
Cdd:cd14180    8 DLEEpaLGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREV-----AALRLCQShPNIVALHEVLHDQYHTYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTS--FDKFYKyvysvlDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGN---IKLCDFGIsgqlv 266
Cdd:cd14180   83 LRGGelLDRIKK------KARFSESEASQLMRSLVSAVSFMHE-AGVVHRDLKPENILYADESDgavLKVIDFGF----- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 267 dsiAKTRDAGCRP---------YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd14180  151 ---ARLRPQGSRPlqtpcftlqYAAPELF----SNQGYDESCDLWSLGVILYTMLSGQVPF 204
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
108-372 1.05e-13

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 70.75  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQL---LMDLDVVMRSSDCPYIVQFYGalfregd 184
Cdd:cd05111    4 FKETELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQSfqaVTDHMLAIGSLDHAYIVRLLG------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 cwIC----MELMS--TSFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd05111   77 --ICpgasLQLVTqlLPLGSLLDHVRQHRGSLGPQLLL-NWCVQIAKGMYYLEEH-RMVHRNLAARNVLLKSPSQVQVAD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISG-------QLVDSIAKTRDAgcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYpkwnsvfdqlTQ 330
Cdd:cd05111  153 FGVADllypddkKYFYSEAKTPIK----WMALESI----HFGKYTHQSDVWSYGVTVWEMMTfGAEPY----------AG 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 331 VVKGDPPQLSNSEEREFSPSFINF-VNLCLTK----DESKRPKYKEL 372
Cdd:cd05111  215 MRLAEVPDLLEKGERLAQPQICTIdVYMVMVKcwmiDENIRPTFKEL 261
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
111-318 1.06e-13

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: 71.99  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd05618   20 QDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELvnDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSFDKFYKYVYSVLDDVIPEEILGKITLAtvkaLNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVD 267
Cdd:cd05618  100 IEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLA----LNYLHER-GIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRP 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526479851 268 SIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05618  175 GDTTSTFCGTPNYIAPEIL----RGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
112-376 1.37e-13

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: 70.09  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLgeIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14083    6 EFKEV--LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAV-LRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTS--FDKFY-KYVYSVLDdviPEEILGKItlatVKALNHLKEnLKIIHRDIKPSNIL---LDRSGNIKLCDFGISGQL 265
Cdd:cd14083   83 VTGGelFDRIVeKGSYTEKD---ASHLIRQV----LEAVDYLHS-LGIVHRDLKPENLLyysPDEDSKIMISDFGLSKME 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGrfpYPKWNSVFDQ--LTQVVKGdppqlsnse 343
Cdd:cd14083  155 DSGVMSTA-CGTPGYVAPEVL----AQKPYGKAVDCWSIGVISYILLCG---YPPFYDENDSklFAQILKA--------- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 526479851 344 EREF-SP-------SFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14083  218 EYEFdSPywddisdSAKDFIRHLMEKDPNKRYTCEQALEHP 258
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
112-378 1.43e-13

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: 70.52  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDL-GEI-GRGAYGSVNKMVHKPSGQIMAVKRIrstvdEK----EQKQLLMDLDVVMRSSDCPYIVQfygalfregdc 185
Cdd:cd14090    1 DLYKLtGELlGEGAYASVQTCINLYTGKEYAVKII-----EKhpghSRSRVFREVETLHQCQGHPNILQ----------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 wiCMELMSTSfDKFYkyvysvlddVIPEEILGKITLATVKALNHLKE------------------NLKIIHRDIKPSNIL 247
Cdd:cd14090   65 --LIEYFEDD-ERFY---------LVFEKMRGGPLLSHIEKRVHFTEqeaslvvrdiasaldflhDKGIAHRDLKPENIL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 248 LDRSGNI---KLCDFGISGQLVDSIAKTRDA---------GCRPYMAPERIDP-SASRQGYDVRSDVWSLGITLYELATG 314
Cdd:cd14090  133 CESMDKVspvKICDFDLGSGIKLSSTSMTPVttpelltpvGSAEYMAPEVVDAfVGEALSYDKRCDLWSLGVILYIMLCG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 315 rfpYPK----------WN------SVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14090  213 ---YPPfygrcgedcgWDrgeacqDCQELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
119-378 1.65e-13

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: 70.44  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKqllmdldvVMRSSDCPYIVQfygalfreGDCWIcMELMSTSFD- 197
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSR--------VFREVETLYQCQ--------GNKNI-LELIEFFEDd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 -KFYkyvysvlddVIPEEILGKITLATVKALNHLKE------------------NLKIIHRDIKPSNILL---DRSGNIK 255
Cdd:cd14174   73 tRFY---------LVFEKLRGGSILAHIQKRKHFNEreasrvvrdiasaldflhTKGIAHRDLKPENILCespDKVSPVK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 256 LCDFGI-SGQLVDSIAK-------TRDAGCRPYMAPERIDPSASRQG-YDVRSDVWSLGITLYELATGRFPYP------- 319
Cdd:cd14174  144 ICDFDLgSGVKLNSACTpittpelTTPCGSAEYMAPEVVEVFTDEATfYDKRCDLWSLGVILYIMLSGYPPFVghcgtdc 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 320 KWN------SVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14174  224 GWDrgevcrVCQNKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
226-378 1.77e-13

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: 69.88  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 226 ALNHLKENlKIIHRDIKPSNILLDRSG-------NIKLCDFGIS----GQLVDSIAKTrdAGCRPYMAPERIdpsaSRQG 294
Cdd:cd14097  112 AVAYLHKN-DIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvqkyGLGEDMLQET--CGTPIYMAPEVI----SAHG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 295 YDVRSDVWSLGITLYELATGRFPYPkwNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14097  185 YSQQCDIWSIGVIMYMLLCGEPPFV--AKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLD 262

                 ....
gi 526479851 375 HPFI 378
Cdd:cd14097  263 NPWI 266
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
107-375 1.83e-13

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: 70.06  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 107 DFTAEDLKDLgeIGRGAYGSVNKMVHKpsGQIMAVKRIRSTVDE---------KEQKQLLMDLDvvmrssdCPYIVQFYG 177
Cdd:cd14147    1 SFQELRLEEV--IGIGGFGKVYRGSWR--GELVAVKAARQDPDEdisvtaesvRQEARLFAMLA-------HPNIIALKA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 178 ALFREGDCWICMELMSTSfdkfyKYVYSVLDDVIPEEILGKITLATVKALNHLKEN--LKIIHRDIKPSNILLDRSG--- 252
Cdd:cd14147   70 VCLEEPNLCLVMEYAAGG-----PLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEalVPVIHRDLKSNNILLLQPIend 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 253 -----NIKLCDFGISGQLvDSIAKTRDAGCRPYMAPERIDPSASRQGydvrSDVWSLGITLYELATGRFPYP-------K 320
Cdd:cd14147  145 dmehkTLKITDFGLAREW-HKTTQMSAAGTYAWMAPEVIKASTFSKG----SDVWSFGVLLWELLTGEVPYRgidclavA 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 321 WNSVFDQLTQVVKGDPPQlsnseerefspSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14147  220 YGVAVNKLTLPIPSTCPE-----------PFAQLMADCWAQDPHRRPDFASILQQ 263
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
119-366 1.85e-13

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: 71.21  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd05617   23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKELvhDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLddviPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD-A 275
Cdd:cd05617  103 LMFHMQRQRKL----PEEHARFYAAEICIALNFLHER-GIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTfC 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY------PKWNSVfDQLTQVVKGDPPQLSNSEEREFSP 349
Cdd:cd05617  178 GTPNYIAPEIL----RGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTE-DYLFQVILEKPIRIPRFLSVKASH 252
                        250
                 ....*....|....*..
gi 526479851 350 SFINFVNlcltKDESKR 366
Cdd:cd05617  253 VLKGFLN----KDPKER 265
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
116-377 2.01e-13

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: 70.70  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRI----RSTVDEKEQKQLL-----MDLDVVMRSSDcpyiVQFYGALFRE-GDC 185
Cdd:cd07879   20 LKQVGSGAYGSVCSAIDKRTGEKVAIKKLsrpfQSEIFAKRAYRELtllkhMQHENVIGLLD----VFTSAVSGDEfQDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSFDKFYKYVYSvlddvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGisgql 265
Cdd:cd07879   96 YLVMPYMQTDLQKIMGHPLS-------EDKVQYLVYQMLCGLKYIHSA-GIIHRDLKPGNLAVNEDCELKILDFG----- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 vdsIAKTRDAG------CRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVK--GDP- 336
Cdd:cd07879  163 ---LARHADAEmtgyvvTRWYRAPEVI---LNWMHYNQTVDIWSVGCIMAEMLTGKTLF-KGKDYLDQLTQILKvtGVPg 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 337 ----------------PQLSNSEEREFS-------PSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07879  236 pefvqkledkaaksyiKSLPKYPRKDFStlfpkasPQAVDLLEKMLELDVDKRLTATEALEHPY 299
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
119-311 2.04e-13

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: 69.97  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKR-IRstVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKElIR--CDEETQKTFLTEVKV-MRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KfyKYVYSvlDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD---------S 268
Cdd:cd14222   78 K--DFLRA--DDPFPWQQKVSFAKGIASGMAYL-HSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEekkkpppdkP 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 269 IAKTRDAG-----------CRPY-MAPERIDPsasrQGYDVRSDVWSLGITLYEL 311
Cdd:cd14222  153 TTKKRTLRkndrkkrytvvGNPYwMAPEMLNG----KSYDEKVDIFSFGIVLCEI 203
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
119-373 2.44e-13

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: 69.70  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKmvHKPSGQImAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFdk 198
Cdd:cd14151   16 IGSGSFGTVYK--GKWHGDV-AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSL-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 fYKYVYsVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISgqlvdsIAKTRDAGCR 278
Cdd:cd14151   91 -YHHLH-IIETKFEMIKLIDIARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLA------TVKSRWSGSH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 279 PY---------MAPERIDPSASRQgYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDPPQLSNSEEREFSP 349
Cdd:cd14151  162 QFeqlsgsilwMAPEVIRMQDKNP-YSFQSDVYAFGIVLYELMTGQLPYSNINNR-DQIIFMVGRGYLSPDLSKVRSNCP 239
                        250       260
                 ....*....|....*....|....*
gi 526479851 350 SFIN-FVNLCLTKDESKRPKYKELL 373
Cdd:cd14151  240 KAMKrLMAECLKKKRDERPLFPQIL 264
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
111-378 2.51e-13

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: 69.66  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLG-EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDlDV-----VMRSSDCPYIVQFYGALFREGD 184
Cdd:cd14194    4 DDYYDTGeELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSRE-DIerevsILKEIQHPNVITLHEVYENKTD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTS--FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNI-LLDRSG---NIKLCD 258
Cdd:cd14194   83 VILILELVAGGelFD------FLAEKESLTEEEATEFLKQILNGVYYL-HSLQIAHFDLKPENImLLDRNVpkpRIKIID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQlVDSIAKTRDA-GCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYpkwnsvFDQLTQVVKGDPP 337
Cdd:cd14194  156 FGLAHK-IDFGNEFKNIfGTPEFVAPEIVN----YEPLGLEADMWSIGVITYILLSGASPF------LGDTKQETLANVS 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 338 QLSNSEEREF----SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14194  225 AVNYEFEDEYfsntSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
218-367 2.72e-13

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: 69.57  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 218 KITLATVKALNHLKENlKIIHRDIKPSNILL-----DRSGNIKLCDFGISGQLVDSIAKTRDaGCRPYMAPERIdpsASR 292
Cdd:cd14000  116 RIALQVADGLRYLHSA-MIIYRDLKSHNVLVwtlypNSAIIIKIADYGISRQCCRMGAKGSE-GTPGFRAPEIA---RGN 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 293 QGYDVRSDVWSLGITLYELATGRFPYPKWNSvFDQLTQVVKGDPPQLSNSEEREFsPSFINFVNLCLTKDESKRP 367
Cdd:cd14000  191 VIYNEKVDVFSFGMLLYEILSGGAPMVGHLK-FPNEFDIHGGLRPPLKQYECAPW-PEVEVLMKKCWKENPQQRP 263
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
232-372 2.83e-13

Catalytic domain of a subset of 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 includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like 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: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 69.17  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 232 ENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLY 309
Cdd:cd14203  108 ERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPikWTAPE----AALYGRFTIKSDVWSFGILLT 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 310 ELAT-GRFPYPKWNS--VFDQLTQVVKGDPPQlsnseerEFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd14203  184 ELVTkGRVPYPGMNNreVLEQVERGYRMPCPP-------GCPESLHELMCQCWRKDPEERPTFEYL 242
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
119-377 3.13e-13

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: 69.94  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVilQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDDVIPEEILGKITlatvKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVDSIAKTRDA 275
Cdd:cd05590   83 LMFHIQKSRRFDEARARFYAAEIT----SALMFLHDK-GIIYRDLKLDNVLLDHEGHCKLADFGMCKEgIFNGKTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDP---PQLSNSEEREFSPSFi 352
Cdd:cd05590  158 GTPDYIAPEIL----QEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENE--DDLFEAILNDEvvyPTWLSQDAVDILKAF- 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 353 nfvnlcLTKDESKR------PKYKELLKHPF 377
Cdd:cd05590  231 ------MTKNPTMRlgsltlGGEEAILRHPF 255
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
115-373 3.30e-13

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: 69.46  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIrsTVDEKEQKQLLMDL-DV-VMRSSDCPYIVQFYGALFR--EGDCWICME 190
Cdd:cd14049   10 EIARLGKGGYGKVYKVRNKLDGQYYAIKKI--LIKKVTKRDCMKVLrEVkVLAGLQHPNIVGYHTAWMEhvQLMLYIQMQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTS-------------FDKFYKYVYSVLDDVIPEEILGKItlatVKALNHLkENLKIIHRDIKPSNILLDRSG-NIKL 256
Cdd:cd14049   88 LCELSlwdwivernkrpcEEEFKSAPYTPVDVDVTTKILQQL----LEGVTYI-HSMGIVHRDLKPRNIFLHGSDiHVRI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFG-----ISGQLVDSIAKTRDAGCRP--------YMAPERIDPSAsrqgYDVRSDVWSLGITLYELATgrfPYPKWNS 323
Cdd:cd14049  163 GDFGlacpdILQDGNDSTTMSRLNGLTHtsgvgtclYAAPEQLEGSH----YDFKSDMYSIGVILLELFQ---PFGTEME 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 324 VFDQLTQVVKGdppQLSNSEEREFsPSFINFVNLCLTKDESKRPKYKELL 373
Cdd:cd14049  236 RAEVLTQLRNG---QIPKSLCKRW-PVQAKYIKLLTSTEPSERPSASQLL 281
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
116-384 3.40e-13

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: 69.65  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEK------EQKQLLMDLDVVmrssdcpYIVQFYGALFREGDCWICM 189
Cdd:cd07873    7 LDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGapctaiREVSLLKDLKHA-------NIVTLHDIIHTEKSLTLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSFDKFykyvysvLDD---VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS-GQL 265
Cdd:cd07873   80 EYLDKDLKQY-------LDDcgnSINMHNVKLFLFQLLRGLAYCHRR-KVLHRDLKPQNLLINERGELKLADFGLArAKS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK--GDPPQ----- 338
Cdd:cd07873  152 IPTKTYSNEVVTLWYRPPDILLGSTD---YSTQIDMWGVGCIFYEMSTGRPLFPG-STVEEQLHFIFRilGTPTEetwpg 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 339 -LSNSEEREFS-PSF----------------INFVNLCLTKDESKRPKYKELLKHPFILMYEER 384
Cdd:cd07873  228 iLSNEEFKSYNyPKYradalhnhaprldsdgADLLSKLLQFEGRKRISAEEAMKHPYFHSLGER 291
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
139-374 3.71e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 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 FGFR1 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: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 69.66  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 139 MAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYV-------YSVLDDVI 211
Cdd:cd05098   48 VAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQArrppgmeYCYNPSHN 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 212 PEEILGKITLAT-----VKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL--VDSIAKTRDaGCRP--YMA 282
Cdd:cd05098  128 PEEQLSSKDLVScayqvARGMEYLASK-KCIHRDLAARNVLVTEDNVMKIADFGLARDIhhIDYYKKTTN-GRLPvkWMA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 283 PERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYP--KWNSVFDQLTQVVKGDPPQLSNSEerefspsFINFVNLCL 359
Cdd:cd05098  206 PEAL----FDRIYTHQSDVWSFGVLLWEIFTlGGSPYPgvPVEELFKLLKEGHRMDKPSNCTNE-------LYMMMRDCW 274
                        250
                 ....*....|....*
gi 526479851 360 TKDESKRPKYKELLK 374
Cdd:cd05098  275 HAVPSQRPTFKQLVE 289
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
115-378 4.38e-13

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: 68.85  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQkqLLMDLDVvMRSSDCPYIVQFYGAlFREGDCWICMELMST 194
Cdd:cd14113   11 EVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQ--VTHELGV-LQSLQHPQLVGLLDT-FETPTSYILVLEMAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfDKFYKYVYSvLDDVIPEEI---LGKItlatVKALNHLkENLKIIHRDIKPSNILLDRSGN---IKLCDFGISGQLVDS 268
Cdd:cd14113   87 Q-GRLLDYVVR-WGNLTEEKIrfyLREI----LEALQYL-HNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERI--DPSAsrqgydVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDpPQLSNSEERE 346
Cdd:cd14113  160 YYIHQLLGSPEFAAPEIIlgNPVS------LTSDLWSIGVLTYVLLSGVSPFLD-ESVEETCLNICRLD-FSFPDDYFKG 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 347 FSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14113  232 VSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
106-372 4.57e-13

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: 69.44  E-value: 4.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNK-----MVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALF 180
Cdd:cd05055   30 WEFPRNNLSFGKTLGAGAFGKVVEataygLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLGNHENIVNLLGACT 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REGDCWICMELmsTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd05055  110 IGGPILVITEY--CCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFL-ASKNCIHRDLAARNVLLTHGKIVKICDFG 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQLV-DSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKW--NSVFDQLTQvvkg 334
Cdd:cd05055  187 LARDIMnDSNYVVKGNARLPvkWMAPESIFNCV----YTFESDVWSYGILLWEIFSlGSNPYPGMpvDSKFYKLIK---- 258
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 335 DPPQLSNSeerEFSPSFI-NFVNLCLTKDESKRPKYKEL 372
Cdd:cd05055  259 EGYRMAQP---EHAPAEIyDIMKTCWDADPLKRPTFKQI 294
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
235-375 4.59e-13

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 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: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 69.62  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCR---PYMAPERIDPSAsrqgYDVRSDVWSLGITLYEL 311
Cdd:cd05103  199 KCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARlplKWMAPETIFDRV----YTIQSDVWSFGVLLWEI 274
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526479851 312 -ATGRFPYP--KWNSVF-DQLTQVVKGDPPQLSNSEEREfspSFINfvnlCLTKDESKRPKYKELLKH 375
Cdd:cd05103  275 fSLGASPYPgvKIDEEFcRRLKEGTRMRAPDYTTPEMYQ---TMLD----CWHGEPSQRPTFSELVEH 335
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
106-374 5.01e-13

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: 69.27  E-value: 5.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSV--------NKmvHKPSGQI-MAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFY 176
Cdd:cd05101   19 WEFPRDKLTLGKPLGEGCFGQVvmaeavgiDK--DKPKEAVtVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 177 GALFREGDCWICMELMSTSFDKFY---------KYVYSVldDVIPEEILG-----KITLATVKALNHLKENlKIIHRDIK 242
Cdd:cd05101   97 GACTQDGPLYVIVEYASKGNLREYlrarrppgmEYSYDI--NRVPEEQMTfkdlvSCTYQLARGMEYLASQ-KCIHRDLA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 243 PSNILLDRSGNIKLCDFGISGQL--VDSIAKTRDaGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFP 317
Cdd:cd05101  174 ARNVLVTENNVMKIADFGLARDInnIDYYKKTTN-GRLPvkWMAPEALFDRV----YTHQSDVWSFGVLMWEIFTlGGSP 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 318 YP--KWNSVFDQLTQVVKGDPPQLSNSEerefspsFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05101  249 YPgiPVEELFKLLKEGHRMDKPANCTNE-------LYMMMRDCWHAVPSQRPTFKQLVE 300
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
232-377 5.58e-13

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like 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: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 68.08  E-value: 5.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 232 ENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLY 309
Cdd:cd05034  109 ESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAKFPikWTAPE----AALYGRFTIKSDVWSFGILLY 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 310 ELAT-GRFPYPKWNSVfDQLTQVVKG-DPPQLSNSEErefspSFINFVNLCLTKDESKRPKYkELLKHPF 377
Cdd:cd05034  185 EIVTyGRVPYPGMTNR-EVLEQVERGyRMPKPPGCPD-----ELYDIMLQCWKKEPEERPTF-EYLQSFL 247
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
108-337 5.89e-13

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: 69.18  E-value: 5.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVdekeqkqLLMDLDV---------VMRSSDCPYIVQFYGA 178
Cdd:cd05619    2 LTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDV-------VLMDDDVectmvekrvLSLAWEHPFLTHLFCT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 179 LFREGDCWICMELMSTSFDKFYKYVYSVLDdvipeeiLGKITLATVKALNHLK--ENLKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05619   75 FQTKENLFFVMEYLNGGDLMFHIQSCHKFD-------LPRATFYAAEIICGLQflHSKGIVYRDLKLDNILLDKDGHIKI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGD 335
Cdd:cd05619  148 ADFGMCKENMLGDAKTSTfCGTPDYIAPEIL----LGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDE--EELFQSIRMD 221

                 ..
gi 526479851 336 PP 337
Cdd:cd05619  222 NP 223
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
116-378 5.94e-13

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: 69.06  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRsTVDEKEQKQLLMDLDV-VMRSSDCPYIVQFYGALFREGDcwicmelmST 194
Cdd:cd07864   12 IGIIGEGTYGQVYKAKDKDTGELVALKKVR-LDNEKEGFPITAIREIkILRQLNHRSVVNLKEIVTDKQD--------AL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDK----FYkYVYSVLD-DVI----------PEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDF 259
Cdd:cd07864   83 DFKKdkgaFY-LVFEYMDhDLMgllesglvhfSEDHIKSFMKQLLEGLNYC-HKKNFLHRDIKCSNILLNNKGQIKLADF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 260 GISgQLVDSIAKtrdagcRPY---------------MAPERIDPSAsrqgydvrsDVWSLGITLYELATGRfPYPKWNSV 324
Cdd:cd07864  161 GLA-RLYNSEES------RPYtnkvitlwyrppellLGEERYGPAI---------DVWSCGCILGELFTKK-PIFQANQE 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 325 FDQLTQVVK--GDP-----PQLSN-----------------SEEREFSPS-FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd07864  224 LAQLELISRlcGSPcpavwPDVIKlpyfntmkpkkqyrrrlREEFSFIPTpALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
119-318 6.02e-13

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: 68.19  E-value: 6.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS-- 195
Cdd:cd14071    8 IGKGNFAVVKLARHRITKTEVAIKIIdKSQLDEENLKKIYREVQI-MKMLNHPHIIKLYQVMETKDMLYLVTEYASNGei 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDkfykyvYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS-----GQLVDSIa 270
Cdd:cd14071   87 FD------YLAQHGRMSEKEARKKFWQILSAVEYCHKR-HIVHRDLKAENLLLDANMNIKIADFGFSnffkpGELLKTW- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 271 ktrdAGCRPYMAPERIDpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd14071  159 ----CGSPPYAAPEVFE---GKEYEGPQLDIWSLGVVLYVLVCGALPF 199
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
119-324 7.12e-13

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: 68.45  E-value: 7.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMR--------SSDCPYIVQfygALFREGDCWICME 190
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRlnhpnvvaARDVPEGLQ---KLAPNDLPLLAME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSfdKFYKYVYSVLDDVIPEEILGKITLATV-KALNHLKENlKIIHRDIKPSNILLDRSGNI---KLCDFGISGQLV 266
Cdd:cd14038   79 YCQGG--DLRKYLNQFENCCGLREGAILTLLSDIsSALRYLHEN-RIIHRDLKPENIVLQQGEQRlihKIIDLGYAKELD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 267 DSIAKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPY-PKWNSV 324
Cdd:cd14038  156 QGSLCTSFVGTLQYLAPELLE----QQKYTVTVDYWSFGTLAFECITGFRPFlPNWQPV 210
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
119-377 7.95e-13

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: 68.13  E-value: 7.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKrirsTVDEKE--QKQLLMDLDV-VMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14184    9 IGDGNFAVVKECVERSTGKEFALK----IIDKAKccGKEHLIENEVsILRRVKHPNIIMLIEEMDTPAELYLVMELVKGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDKFY---KYVysvlddvipEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL----DRSGNIKLCDFGISgQLV 266
Cdd:cd14184   85 dlFDAITsstKYT---------ERDASAMVYNLASALKYL-HGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLA-TVV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNS----VFDQ-LTQVVKGDPPQLSN 341
Cdd:cd14184  154 EGPLYTV-CGTPTYVAPEII----AETGYGLKVDIWAAGVITYILLCGFPPFRSENNlqedLFDQiLLGKLEFPSPYWDN 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 342 seereFSPSFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14184  229 -----ITDSAKELISHMLQVNVEARYTAEQILSHPW 259
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
106-372 8.84e-13

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src 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: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 68.18  E-value: 8.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQImAVKRIRSTVDEKEQkqlLMDLDVVMRSSDCPYIVQFYgALFREGDC 185
Cdd:cd05071    4 WEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRV-AIKTLKPGTMSPEA---FLQEAQVMKKLRHEKLVQLY-AVVSEEPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMST-SFDKFYKYVYSVLDDvIPEEILGKITLATVKALnhlKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd05071   79 YIVTEYMSKgSLLDFLKGEMGKYLR-LPQLVDMAAQIASGMAY---VERMNYVHRDLRAANILVGENLVCKVADFGLARL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKW--NSVFDQLTQVVKGDPPQl 339
Cdd:cd05071  155 IEDNEYTARQGAKFPikWTAPE----AALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMvnREVLDQVERGYRMPCPP- 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 340 snseerEFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05071  230 ------ECPESLHDLMCQCWRKEPEERPTFEYL 256
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
112-318 9.04e-13

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: 68.87  E-value: 9.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVviQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSfDKFYkYVYSVLDDVIPEEILGKITLATVKALNHLKenlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVDS 268
Cdd:cd05616   81 EYVNGG-DLMY-HIQQVGRFKEPHAVFYAAEIAIGLFFLQSK---GIIYRDLKLDNVMLDSEGHIKIADFGMCKEnIWDG 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05616  156 VTTKTFCGTPDYIAPEII----AYQPYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
106-383 9.44e-13

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: 68.92  E-value: 9.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDfTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI----------RSTVDE------KEQKQLLMDLDVVMRSSDc 169
Cdd:cd07878   11 WE-VPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLsrpfqslihaRRTYRElrllkhMKHENVIGLLDVFTPATS- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 170 pyivqfyGALFREgdCWICMELMSTSFDKFYKYvYSVLDDvipeeilgKITLATVKALNHLK--ENLKIIHRDIKPSNIL 247
Cdd:cd07878   89 -------IENFNE--VYLVTNLMGADLNNIVKC-QKLSDE--------HVQFLIYQLLRGLKyiHSAGIIHRDLKPSNVA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 248 LDRSGNIKLCDFGISGQLVDSIakTRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQ 327
Cdd:cd07878  151 VNEDCELRILDFGLARQADDEM--TGYVATRWYRAPEIM---LNWMHYNQTVDIWSVGCIMAELLKGKALFPG-NDYIDQ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 328 LTQV--VKGDPP-----QLSNSEEREF-------------------SPSFINFVNLCLTKDESKRPKYKELLKHPFILMY 381
Cdd:cd07878  225 LKRImeVVGTPSpevlkKISSEHARKYiqslphmpqqdlkkifrgaNPLAIDLLEKMLVLDSDKRISASEALAHPYFSQY 304

                 ..
gi 526479851 382 EE 383
Cdd:cd07878  305 HD 306
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
115-383 9.57e-13

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: 68.75  E-value: 9.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIR---STVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFRegDCWICMEL 191
Cdd:cd07856   14 DLQPVGMGAFGLVCSARDQLTGQNVAVKKIMkpfSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLE--DIYFVTEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MSTSFDKFYKYvySVLDDVIPEEILGKItlatVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISgqLVDSIAK 271
Cdd:cd07856   92 LGTDLHRLLTS--RPLEKQFIQYFLYQI----LRGLKYV-HSAGVIHRDLKPSNILVNENCDLKICDFGLA--RIQDPQM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSV--FDQLTQVVkGDPPQ----------- 338
Cdd:cd07856  163 TGYVSTRYYRAPEIM---LTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVnqFSIITELL-GTPPDdvinticsent 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 526479851 339 ------LSNSEEREFS-------PSFINFVNLCLTKDESKRPKYKELLKHPFILMYEE 383
Cdd:cd07856  239 lrfvqsLPKRERVPFSekfknadPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHD 296
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
119-312 1.08e-12

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: 68.23  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMvhKPSGQIMAVKRI-----RSTVDEKEQKQllmdlDVVMRSSDcpyIVQFYGALFREGDCWICMELMS 193
Cdd:cd13998    3 IGKGRFGEVWKA--SLKNEPVAVKIFssrdkQSWFREKEIYR-----TPMLKHEN---ILQFIAADERDTALRTELWLVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDK--FYKYVYSVLDDVipeEILGKITLATVKALNHLKENL--------KIIHRDIKPSNILLDRSGNIKLCDFGIS- 262
Cdd:cd13998   73 AFHPNgsL*DYLSLHTIDW---VSLCRLALSVARGLAHLHSEIpgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLAv 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 263 ----GQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYD--VRSDVWSLGITLYELA 312
Cdd:cd13998  150 rlspSTGEEDNANNGQVGTKRYMAPEVLEGAINLRDFEsfKRVDIYAMGLVLWEMA 205
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
119-390 1.10e-12

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: 68.55  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRI----RSTVDEK----EQKQL-LMDLDVVMRSSDC---PYIVQFygalfreGDCW 186
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIanafDNRIDAKrtlrEIKLLrHLDHENVIAIKDImppPHREAF-------NDVY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSFDKFYKYVYSVLDDVIpEEILGKItlatVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGisgqlv 266
Cdd:cd07858   86 IVYELMDTDLHQIIRSSQTLSDDHC-QYFLYQL----LRGLKYI-HSANVLHRDLKPSNLLLNANCDLKICDFG------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 dsIAKTRDAGC---------RPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--GD 335
Cdd:cd07858  154 --LARTTSEKGdfmteyvvtRWYRAPELL---LNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYV-HQLKLITEllGS 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 336 PP-----------------QLSNSEEREF-------SPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVAC 390
Cdd:cd07858  228 PSeedlgfirnekarryirSLPYTPRQSFarlfphaNPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVC 306
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
106-319 1.12e-12

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk 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: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 67.60  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVnKMVHKPSGQIMAVKRIRSTVDEKEQkqLLMDLDVvMRSSDCPYIVQFYGALFREgDC 185
Cdd:cd05067    2 WEVPRETLKLVERLGAGQFGEV-WMGYYNGHTKVAIKSLKQGSMSPDA--FLAEANL-MKQLQHQRLVRLYAVVTQE-PI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMST-SFDKFYKY-------VYSVLDdvipeeILGKIT--LATVKALNHlkenlkiIHRDIKPSNILLDRSGNIK 255
Cdd:cd05067   77 YIITEYMENgSLVDFLKTpsgikltINKLLD------MAAQIAegMAFIEERNY-------IHRDLRAANILVSDTLSCK 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 256 LCDFGISGQLVDSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYP 319
Cdd:cd05067  144 IADFGLARLIEDNEYTAREGAKFPikWTAPEAINYGT----FTIKSDVWSFGILLTEIVThGRIPYP 206
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
116-348 1.13e-12

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: 68.11  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGdcwiCMELMSTS 195
Cdd:cd07871   10 LDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSL-LKNLKHANIVTLHDIIHTER----CLTLVFEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGIS-GQLVDSIAKTRD 274
Cdd:cd07871   85 LDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKR-KILHRDLKPQNLLINEKGELKLADFGLArAKSVPTKTYSNE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK--GDPPQ------LSNSEERE 346
Cdd:cd07871  164 VVTLWYRPPDVLLGSTE---YSTPIDMWGVGCILYEMATGRPMFPG-STVKEELHLIFRllGTPTEetwpgvTSNEEFRS 239

                 ..
gi 526479851 347 FS 348
Cdd:cd07871  240 YL 241
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
118-369 1.17e-12

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: 67.26  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd05084    3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFLQEARI-LKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 KFYKYVYSVLDDVIPEEILgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTrDAGC 277
Cdd:cd05084   80 DFLTFLRTEGPRLKVKELI-RMVENAAAGMEYL-ESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAA-TGGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 278 R----PYMAPERIDPSAsrqgYDVRSDVWSLGITLYE-LATGRFPYPKWNS--VFDQLTQVVKGDPPQLSNSEerefsps 350
Cdd:cd05084  157 KqipvKWTAPEALNYGR----YSSESDVWSFGILLWEtFSLGAVPYANLSNqqTREAVEQGVRLPCPENCPDE------- 225
                        250
                 ....*....|....*....
gi 526479851 351 FINFVNLCLTKDESKRPKY 369
Cdd:cd05084  226 VYRLMEQCWEYDPRKRPSF 244
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
106-378 1.25e-12

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: 68.15  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGE----IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFR 181
Cdd:cd14168    1 WKKQVEDIKKIFEfkevLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEI-AVLRKIKHENIVALEDIYES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 182 EGDCWICMELMSTS--FDKFYKYVYSVLDDVipeeilGKITLATVKALNHLkENLKIIHRDIKPSNILL---DRSGNIKL 256
Cdd:cd14168   80 PNHLYLVMQLVSGGelFDRIVEKGFYTEKDA------STLIRQVLDAVYYL-HRMGIVHRDLKPENLLYfsqDEESKIMI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQLVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWN--SVFDQLTQV-VK 333
Cdd:cd14168  153 SDFGLSKMEGKGDVMSTACGTPGYVAPEVL----AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdsKLFEQILKAdYE 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 334 GDPPQLSnseerEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14168  229 FDSPYWD-----DISDSAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
111-347 1.38e-12

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; 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. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 67.72  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSVNKMVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWIC 188
Cdd:cd05089    2 EDIKFEDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTS--FDKFYKYVYSVLDDVIPEEILGKITLAT----------VKALNHLKENlKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05089   82 IEYAPYGnlLDFLRKSRVLETDPAFAKEHGTASTLTSqqllqfasdvAKGMQYLSEK-QFIHRDLAARNVLVGENLVSKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWN--SVFDQLTQVVK 333
Cdd:cd05089  161 ADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSV----YTTKSDVWSFGVLLWEIVSlGGTPYCGMTcaELYEKLPQGYR 236
                        250
                 ....*....|....
gi 526479851 334 GDPPQLSNSEEREF 347
Cdd:cd05089  237 MEKPRNCDDEVYEL 250
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
115-376 1.42e-12

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: 67.43  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKR----IRSTVDEKeqkqllMDLDVVMRSS---DCPYIVQFYGALFREGDCWI 187
Cdd:cd14051    4 EVEKIGSGEFGSVYKCINRLDGCVYAIKKskkpVAGSVDEQ------NALNEVYAHAvlgKHPHVVRYYSAWAEDDHMII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSfdkfykyvysVLDDVIPE-----EILGKITLATVkaLNHLKENLKIIHR------DIKPSNILLDRSGNI-- 254
Cdd:cd14051   78 QNEYCNGG----------SLADAISEnekagERFSEAELKDL--LLQVAQGLKYIHSqnlvhmDIKPGNIFISRTPNPvs 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 -----------------KLCDFGIsGQL--VDSIA--KTRDAGCRpYMAPERIdpsasRQGYD--VRSDVWSLGITLYEL 311
Cdd:cd14051  146 seeeeedfegeednpesNEVTYKI-GDLghVTSISnpQVEEGDCR-FLANEIL-----QENYShlPKADIFALALTVYEA 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 312 ATGRfPYPKwNSvfDQLTQVVKGDPPQLSNseereFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14051  219 AGGG-PLPK-NG--DEWHEIRQGNLPPLPQ-----CSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
119-330 1.47e-12

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 67.34  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALF----REGDCWICMELM 192
Cdd:cd05075    8 LGEGEFGSVMEGQLNQDDSVLkvAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLqnteSEGYPSPVVILP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSFDKFYKYV-YSVLDDV---IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS 268
Cdd:cd05075   88 FMKHGDLHSFLlYSRLGDCpvyLPTQMLVKFMTDIASGMEYLSSK-NFIHRDLAARNCMLNENMNVCVADFGLSKKIYNG 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 269 -------IAKTrdagcrP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP--KWNSVFDQLTQ 330
Cdd:cd05075  167 dyyrqgrISKM------PvkWIAIE----SLADRVYTTKSDVWSFGVTMWEIATrGQTPYPgvENSEIYDYLRQ 230
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
111-375 2.33e-12

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: 67.03  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGEIGRGAYGSV-----NKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDC 185
Cdd:cd05036    6 KNLTLIRALGQGAFGEVyegtvSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEA-LIMSKFNHPNIVRCIGVCFQRLPR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMS----TSFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCD 258
Cdd:cd05036   85 FILLELMAggdlKSFLRENRPRPEQPSSLTMLDLL-QLAQDVAKGCRYLEEN-HFIHRDIAARNCLLTCKGPgrvAKIGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSiAKTRDAGCRpyMAPER-IDPSASRQG-YDVRSDVWSLGITLYEL-ATGRFPYP-KWNSVFDQLtqVVKG 334
Cdd:cd05036  163 FGMARDIYRA-DYYRKGGKA--MLPVKwMPPEAFLDGiFTSKTDVWSFGVLLWEIfSLGYMPYPgKSNQEVMEF--VTSG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 526479851 335 ---DPPqlsnseeREFSPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd05036  238 grmDPP-------KNCPGPVYRIMTQCWQHIPEDRPNFSTILER 274
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
118-377 2.60e-12

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: 67.00  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGAL---FREGDCWICM-ELMS 193
Cdd:cd14030   32 EIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWestVKGKKCIVLVtELMT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENLK-IIHRDIKPSNILLD-RSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14030  112 SGTLKTYLKRFKVMK----IKVLRSWCRQILKGLQFLHTRTPpIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAK 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRdAGCRPYMAPERIDpsasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPqlsNSEEREFSPSF 351
Cdd:cd14030  188 SV-IGTPEFMAPEMYE-----EKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKP---ASFDKVAIPEV 258
                        250       260
                 ....*....|....*....|....*.
gi 526479851 352 INFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14030  259 KEIIEGCIRQNKDERYAIKDLLNHAF 284
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
235-374 2.76e-12

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (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. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 67.31  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCR---PYMAPERIDPSAsrqgYDVRSDVWSLGITLYEL 311
Cdd:cd05102  192 KCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARlplKWMAPESIFDKV----YTTQSDVWSFGVLLWEI 267
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 312 -ATGRFPYP--KWNSVFDQ-LTQVVKGDPPQLSNSEEREFSPSfinfvnlCLTKDESKRPKYKELLK 374
Cdd:cd05102  268 fSLGASPYPgvQINEEFCQrLKDGTRMRAPEYATPEIYRIMLS-------CWHGDPKERPTFSDLVE 327
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
111-378 2.79e-12

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: 66.74  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGE-IGRGAYGSVNKMVHKPSGQIMAVKRI--------RSTVDEKEqkqllMDLDV-VMRSSDCPYIVQFYGALF 180
Cdd:cd14105    4 EDFYDIGEeLGSGQFAVVKKCREKSTGLEYAAKFIkkrrskasRRGVSRED-----IEREVsILRQVLHPNIITLHDVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REGDCWICMELMSTS--FDKFYKYVYSVLDDVIpeEILGKItlatVKALNHLkENLKIIHRDIKPSNI-LLDRS---GNI 254
Cdd:cd14105   79 NKTDVVLILELVAGGelFDFLAEKESLSEEEAT--EFLKQI----LDGVNYL-HTKNIAHFDLKPENImLLDKNvpiPRI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 255 KLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKG 334
Cdd:cd14105  152 KLIDFGLAHKIEDGNEFKNIFGTPEFVAPEIVN----YEPLGLEADMWSIGVITYILLSGASPF-LGDTKQETLANITAV 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 335 DppqlSNSEEREFSPS---FINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14105  227 N----YDFDDEYFSNTselAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
119-312 2.85e-12

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: 66.73  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMvhKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcpyIVQFYGALFREGDCWICMELMSTSFD- 197
Cdd:cd14144    3 VGKGRYGEVWKG--KWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHEN---ILGFIAADIKGTGSWTQLYLITDYHEn 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 -KFYKYVYSvldDVIPEEILGKITLATVKALNHLKENL-------KIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDS- 268
Cdd:cd14144   78 gSLYDFLRG---NTLDTQSMLKLAYSAACGLAHLHTEIfgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISEt 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 ----IAKTRDAGCRPYMAPERIDPSASRQGYD--VRSDVWSLGITLYELA 312
Cdd:cd14144  155 nevdLPPNTRVGTKRYMAPEVLDESLNRNHFDayKMADMYSFGLVLWEIA 204
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
225-378 2.87e-12

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: 66.97  E-value: 2.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 225 KALNHLkENLKIIHRDIKPSNILL---DRSGNIKLCDFGI-SGQLVDSIAKT-------RDAGCRPYMAPERIDP-SASR 292
Cdd:cd14173  111 SALDFL-HNKGIAHRDLKPENILCehpNQVSPVKICDFDLgSGIKLNSDCSPistpellTPCGSAEYMAPEVVEAfNEEA 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 293 QGYDVRSDVWSLGITLYELATGRFPYP-------KWN------SVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCL 359
Cdd:cd14173  190 SIYDKRCDLWSLGVILYIMLSGYPPFVgrcgsdcGWDrgeacpACQNMLFESIQEGKYEFPEKDWAHISCAAKDLISKLL 269
                        170
                 ....*....|....*....
gi 526479851 360 TKDESKRPKYKELLKHPFI 378
Cdd:cd14173  270 VRDAKQRLSAAQVLQHPWV 288
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
119-338 3.25e-12

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: 66.96  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCP---YIVQFYGAL-FREGDCwICMELMSt 194
Cdd:cd14226   21 IGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEnkyYIVRLKRHFmFRNHLC-LVFELLS- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 sfdkfykyvYSvLDDVIPEEILGKITLATVK--------ALNHLKE-NLKIIHRDIKPSNILL---DRSGnIKLCDFGIS 262
Cdd:cd14226   99 ---------YN-LYDLLRNTNFRGVSLNLTRkfaqqlctALLFLSTpELSIIHCDLKPENILLcnpKRSA-IKIIDFGSS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 GQLVDSIAKTRDAgcRPYMAPERIdpsasrQG--YDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVK--GDPPQ 338
Cdd:cd14226  168 CQLGQRIYQYIQS--RFYRSPEVL------LGlpYDLAIDMWSLGCILVEMHTGEPLFSGANEV-DQMNKIVEvlGMPPV 238
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
119-374 3.33e-12

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 66.29  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKP-----SGQI-MAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICMELM 192
Cdd:cd05044    3 LGSGAFGEVFEGTAKDilgdgSGETkVAVKTLRKGATDQEKAEFLKEA-HLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 S----TSF------DKFYKYVYSVLDdvipeeiLGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGN----IKLCD 258
Cdd:cd05044   82 EggdlLSYlraarpTAFTPPLLTLKD-------LLSICVDVAKGCVYL-EDMHFVHRDLAARNCLVSSKDYrervVKIGD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDS-IAKTRDAGCRP--YMAPERIdpsasRQGY-DVRSDVWSLGITLYELAT-GRFPYPKWNSvFDQLTQVVK 333
Cdd:cd05044  154 FGLARDIYKNdYYRKEGEGLLPvrWMAPESL-----VDGVfTTQSDVWAFGVLMWEILTlGQQPYPARNN-LEVLHFVRA 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 526479851 334 G---DPPQlsNSEEREFspsfiNFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05044  228 GgrlDQPD--NCPDDLY-----ELMLRCWSTDPEERPSFARILE 264
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
119-378 3.52e-12

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: 66.10  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRsTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTGLKLAAKVIN-KQNSKDKEMVLLEIQV-MNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGelF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKfykyvysVLDDVIPeeilgkitLATVKALNHLKE---------NLKIIHRDIKPSNILL-DRSGN-IKLCDFGISGQL 265
Cdd:cd14190   90 ER-------IVDEDYH--------LTEVDAMVFVRQicegiqfmhQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKTRDAGCRPYMAPERIDpsasrqgYDVRS---DVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKGDppqlSNS 342
Cdd:cd14190  155 NPREKLKVNFGTPEFLSPEVVN-------YDQVSfptDMWSMGVITYMLLSGLSPFLGDDDT-ETLNNVLMGN----WYF 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 343 EEREF---SPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14190  223 DEETFehvSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
120-370 3.52e-12

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: 66.26  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 120 GRGAYGsvnKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDldvvMRSSDCPYIVQFYGALFREGDCWICMELMS----- 193
Cdd:cd13992   12 GEPKYV---KKVGVYGGRTVAIKHItFSRTEKRTILQELNQ----LKELVHDNLNKFIGICINPPNIAVVTEYCTrgslq 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 -------TSFDKFYKYvySVLDDVipeeilgkitlatVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd13992   85 dvllnreIKMDWMFKS--SFIKDI-------------VKGMNYLHSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRP----YMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPkwNSVFDQLTQVVK--GDPPQLS 340
Cdd:cd13992  150 EQTNHQLDEDAQHkkllWTAPELLRGSLLEVRGTQKGDVYSFAIILYEILFRSDPFA--LEREVAIVEKVIsgGNKPFRP 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 341 N--SEEREFSPSFINFVNLCLTKDESKRPKYK 370
Cdd:cd13992  228 ElaVLLDEFPPRLVLLVKQCWAENPEKRPSFK 259
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
102-377 4.15e-12

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: 66.41  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 102 PEQHWDFtaEDLK-DLGE---------IGRGAYGSVNKMVHKPSGQIMAVKRIRStvdEKEQK-----QLLMDLdvvmrs 166
Cdd:cd14132    1 PPEYWDY--ENLNvEWGSqddyeiirkIGRGKYSEVFEGINIGNNEKVVIKVLKP---VKKKKikreiKILQNL------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 167 SDCPYIVQFYGAlFREGD----CWICMELMSTSFdkfyKYVYSVLDD----VIPEEILgkitlatvKALN--HLKenlKI 236
Cdd:cd14132   70 RGGPNIVKLLDV-VKDPQsktpSLIFEYVNNTDF----KTLYPTLTDydirYYMYELL--------KALDycHSK---GI 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 237 IHRDIKPSNILLDRSGN-IKLCDFGIS-----GQ----LVDSiaktrdagcRPYMAPERIdpsASRQGYDVRSDVWSLGI 306
Cdd:cd14132  134 MHRDVKPHNIMIDHEKRkLRLIDWGLAefyhpGQeynvRVAS---------RYYKGPELL---VDYQYYDYSLDMWSLGC 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 307 TLYELATGRFPYPKWNSVFDQLTQVVK---GD-------------PPQLS---------------NSEEREF-SPSFINF 354
Cdd:cd14132  202 MLASMIFRKEPFFHGHDNYDQLVKIAKvlgTDdlyayldkygielPPRLNdilgrhskkpwerfvNSENQHLvTPEALDL 281
                        330       340
                 ....*....|....*....|...
gi 526479851 355 VNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14132  282 LDKLLRYDHQERITAKEAMQHPY 304
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
119-373 4.44e-12

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 65.83  E-value: 4.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICME------ 190
Cdd:cd05047    3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEyaphgn 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 ---------LMSTsfDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGI 261
Cdd:cd05047   83 lldflrksrVLET--DPAFAIANSTASTLSSQQLL-HFAADVARGMDYLSQK-QFIHRDLAARNILVGENYVAKIADFGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 S-GQLVdSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWN--SVFDQLTQVVKGDPP 337
Cdd:cd05047  159 SrGQEV-YVKKTMGRLPVRWMAIESLNYSV----YTTNSDVWSYGVLLWEIVSlGGTPYCGMTcaELYEKLPQGYRLEKP 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 338 QLSNSEEREfspsfinFVNLCLTKDESKRPKYKELL 373
Cdd:cd05047  234 LNCDDEVYD-------LMRQCWREKPYERPSFAQIL 262
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
119-378 4.62e-12

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: 66.07  E-value: 4.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVdEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS--F 196
Cdd:cd14169   11 LGEGAFSEVVLAQERGSQRLVALKCIPKKA-LRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGelF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDDVipEEILGKItlatVKALNHLkENLKIIHRDIKPSNILLD---RSGNIKLCDFGISGQLVDSIAKTR 273
Cdd:cd14169   90 DRIIERGSYTEKDA--SQLIGQV----LQAVKYL-HQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIEAQGMLSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 dAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKG----DPPQLSnseerEFSP 349
Cdd:cd14169  163 -CGTPGYVAPELLE----QKPYGKAVDVWAIGVISYILLCGYPPFYDENDS-ELFNQILKAeyefDSPYWD-----DISE 231
                        250       260
                 ....*....|....*....|....*....
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14169  232 SAKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
118-318 5.17e-12

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: 65.56  E-value: 5.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRS--TVDEKEQKQLlmdldVVMRSSDCPYIVQFYGALFREGDCWICMELMSTS 195
Cdd:cd14662    7 DIGSGNFGVARLMRNKETKELVAVKYIERglKIDENVQREI-----INHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 --FDKF----------YKYVYSVLddvipeeilgkitLATVKALNHLKenlkIIHRDIKPSNILLDRS--GNIKLCDFGI 261
Cdd:cd14662   82 elFERIcnagrfsedeARYFFQQL-------------ISGVSYCHSMQ----ICHRDLKLENTLLDGSpaPRLKICDFGY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 262 S-GQLVDSIAKTrDAGCRPYMAPERIdpsaSRQGYDVR-SDVWSLGITLYELATGRFPY 318
Cdd:cd14662  145 SkSSVLHSQPKS-TVGTPAYIAPEVL----SRKEYDGKvADVWSCGVTLYVMLVGAYPF 198
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
119-378 5.46e-12

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: 65.75  E-value: 5.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVK--RIRSTVDEKEQKQLLMdldvVMRSSDCPYIVQFYGALFREGDCWICMELMSTS- 195
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAAKiiKVKGAKEREEVKNEIN----IMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGe 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 -FDKFY--KYVYSVLDDVIpeeilgkITLATVKALNHLKENLkIIHRDIKPSNIL-LDRSGN-IKLCDFGISGQLVDSIA 270
Cdd:cd14192   88 lFDRITdeSYQLTELDAIL-------FTRQICEGVHYLHQHY-ILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPYMAPERIDpsasrqgYDVRS---DVWSLGITLYELATGRFPYPKWNSVfDQLTQVVKG----DPPQLSN-S 342
Cdd:cd14192  160 LKVNFGTPEFLAPEVVN-------YDFVSfptDMWSVGVITYMLLSGLSPFLGETDA-ETMNNIVNCkwdfDAEAFENlS 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 343 EEREfspsfiNFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14192  232 EEAK------DFISRLLVKEKSCRMSATQCLKHEWL 261
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
119-373 5.85e-12

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They 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. The EphB 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: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 65.66  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSG---QIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST- 194
Cdd:cd05065   12 IGAGEFGEVCRGRLKLPGkreIFVAIKTLKSGYTEKQRRDFLSEASI-MGQFDHPNIIHLEGVVTKSRPVMIITEFMENg 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKyvysvLDD--VIPEEILGKITlATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK- 271
Cdd:cd05065   91 ALDSFLR-----QNDgqFTVIQLVGMLR-GIAAGMKYLSE-MNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDp 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 --TRDAGCR---PYMAPERIdpsASRQgYDVRSDVWSLGITLYE-LATGRFPYpkWNSVFDQLTQVVKGD---PPQLSns 342
Cdd:cd05065  164 tyTSSLGGKipiRWTAPEAI---AYRK-FTSASDVWSYGIVMWEvMSYGERPY--WDMSNQDVINAIEQDyrlPPPMD-- 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 343 eerefSPSFINFVNL-CLTKDESKRPKYKELL 373
Cdd:cd05065  236 -----CPTALHQLMLdCWQKDRNLRPKFGQIV 262
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
226-317 6.00e-12

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 67.67  E-value: 6.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  226 ALNHLKENlKIIHRDIKPSNILLDRSGN----IKLCDFGISGQLVDSIaktrDAGCRPYMAPERIDPSASRqgYDVRSDV 301
Cdd:NF033442  619 AVVHLEGQ-GVWHRDIKPDNIGIRPRPSrtlhLVLFDFSLAGAPADNI----EAGTPGYLDPFLGTGTRPR--YDDAAER 691
                          90
                  ....*....|....*.
gi 526479851  302 WSLGITLYELATGRFP 317
Cdd:NF033442  692 YAAAVTLYEMATGTLP 707
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
119-373 6.08e-12

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: 65.38  E-value: 6.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQ---IMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMST- 194
Cdd:cd05063   13 IGAGEFGEVFRGILKMPGRkevAVAIKTLKPGYTEKQRQDFLSEASIMGQFSH-HNIIRLEGVVTKFKPAMIITEYMENg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKyvySVLDDVIPEEILGKI--TLATVKALNhlkeNLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD--SIA 270
Cdd:cd05063   92 ALDKYLR---DHDGEFSSYQLVGMLrgIAAGMKYLS----DMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDdpEGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYpkWNSVFDQLTQVVKgDPPQLSNSEEref 347
Cdd:cd05063  165 YTTSGGKIPirWTAPEAI----AYRKFTSASDVWSFGIVMWEVMSfGERPY--WDMSNHEVMKAIN-DGFRLPAPMD--- 234
                        250       260
                 ....*....|....*....|....*..
gi 526479851 348 SPSFINFVNL-CLTKDESKRPKYKELL 373
Cdd:cd05063  235 CPSAVYQLMLqCWQQDRARRPRFVDIV 261
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
119-318 6.29e-12

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: 66.29  E-value: 6.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELvnDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLddviPEE----ILGKITLAtvkaLNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVDSIAK 271
Cdd:cd05588   83 LMFHMQRQRRL----PEEharfYSAEISLA----LNFLHEK-GIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGDTT 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 526479851 272 TRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:cd05588  154 STFCGTPNYIAPEIL----RGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
118-377 6.51e-12

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: 65.31  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKE----QKQLLMDLDvvmrsSDCpyIVQFYGALFREGDCWICMELMS 193
Cdd:cd14108    9 EIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTsarrELALLAELD-----HKS--IVRFHDAFEKRRVVIIVTELCH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSFDKFYKYVYSVLDDVIpEEILGKItlatVKALNHLKENlKIIHRDIKPSNILLDRSGN--IKLCDFGISGQLVDSIAK 271
Cdd:cd14108   82 EELLERITKRPTVCESEV-RSYMRQL----LEGIEYLHQN-DVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNEPQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 272 TRDAGCRPYMAPERIDPSASRQgydvRSDVWSLGITLYELATGRFPYpkwnsvfdqltqVVKGDPPQLSNS-------EE 344
Cdd:cd14108  156 YCKYGTPEFVAPEIVNQSPVSK----VTDIWPVGVIAYLCLTGISPF------------VGENDRTTLMNIrnynvafEE 219
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 345 REF---SPSFINFVNLCLTKDEsKRPKYKELLKHPF 377
Cdd:cd14108  220 SMFkdlCREAKGFIIKVLVSDR-LRPDAEETLEHPW 254
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
118-373 6.83e-12

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: 65.47  E-value: 6.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNK-MVHKPSGQ--IMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd05033   11 VIGGGEFGEVCSgSLKLPGKKeiDVAIKTLKSGYSDKQRLDFLTEASI-MGQFDHPNVIRLEGVVTKSRPVMIVTEYMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 -SFDKFYKyvysVLDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAK-T 272
Cdd:cd05033   90 gSLDKFLR----ENDGKFTVTQLVGMLRGIASGMKYLSE-MNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATyT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDAGCRP--YMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNS--VFDQLTQVVKGDPPqlsnseerEF 347
Cdd:cd05033  165 TKGGKIPirWTAPEAI----AYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNqdVIKAVEDGYRLPPP--------MD 232
                        250       260
                 ....*....|....*....|....*..
gi 526479851 348 SPSFINFVNL-CLTKDESKRPKYKELL 373
Cdd:cd05033  233 CPSALYQLMLdCWQKDRNERPTFSQIV 259
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
106-374 7.07e-12

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand 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 signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 65.76  E-value: 7.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHK------PSGQImAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGAL 179
Cdd:cd05061    1 WEVSREKITLLRELGQGSFGMVYEGNARdiikgeAETRV-AVKTVNESASLRERIEFLNEASV-MKGFTCHHVVRLLGVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 FREGDCWICMELMSTSfdKFYKYVYSVLDDV------IPEEILGKITLAT--VKALNHLKENlKIIHRDIKPSNILLDRS 251
Cdd:cd05061   79 SKGQPTLVVMELMAHG--DLKSYLRSLRPEAennpgrPPPTLQEMIQMAAeiADGMAYLNAK-KFVHRDLAARNCMVAHD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 252 GNIKLCDFGISGQLVDS-IAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWNSvfdq 327
Cdd:cd05061  156 FTVKIGDFGMTRDIYETdYYRKGGKGLLPvrWMAPESLKDGV----FTTSSDMWSFGVVLWEITSlAEQPYQGLSN---- 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526479851 328 lTQVVK-----GDPPQLSNSEERefspsFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05061  228 -EQVLKfvmdgGYLDQPDNCPER-----VTDLMRMCWQFNPKMRPTFLEIVN 273
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
119-338 7.64e-12

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: 65.74  E-value: 7.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVdekeqkqLLMDLDV---------VMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05620    3 LGKGSFGKVLLAELKGKGEYFAVKALKKDV-------VLIDDDVectmvekrvLALAWENPFLTHLYCTFQTKEHLFFVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTS-----------FDKFYKYVYSVlddvipeEILGKITLATVKAlnhlkenlkIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd05620   76 EFLNGGdlmfhiqdkgrFDLYRATFYAA-------EIVCGLQFLHSKG---------IIYRDLKLDNVMLDRDGHIKIAD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLV--DSIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDP 336
Cdd:cd05620  140 FGMCKENVfgDNRASTF-CGTPDYIAPEIL----QGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDE--DELFESIRVDT 212

                 ..
gi 526479851 337 PQ 338
Cdd:cd05620  213 PH 214
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
106-372 7.87e-12

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 65.47  E-value: 7.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQImAVKRIRSTVDEKEQkqlLMDLDVVMRSSDCPYIVQFYGALFREgDC 185
Cdd:cd05070    4 WEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSPES---FLEEAQIMKKLKHDKLVQLYAVVSEE-PI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfdkfykyvySVLDDVIPEEilGKI--------TLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLC 257
Cdd:cd05070   79 YIVTEYMSKG---------SLLDFLKDGE--GRAlklpnlvdMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 258 DFGISGQLVDSIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNS--VFDQLTQVV 332
Cdd:cd05070  148 DFGLARLIEDNEYTARQGAKFPikWTAPE----AALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNreVLEQVERGY 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 526479851 333 KGDPPQlsnseerEFSPSFINFVNLCLTKDESKRPKYKEL 372
Cdd:cd05070  224 RMPCPQ-------DCPISLHELMIHCWKKDPEERPTFEYL 256
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
224-377 8.54e-12

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like 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: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 65.42  E-value: 8.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 224 VKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD-----SIAKTRDAGCRP-------YMAPERIdPSAS 291
Cdd:cd14011  124 SEALSFLHNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQatdqfPYFREYDPNLPPlaqpnlnYLAPEYI-LSKT 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 292 rqgYDVRSDVWSLGITLYEL-ATGRFPYPKWNSV--FDQLTQVVKgdppQLSNSeEREFSPSFIN-FVNLCLTKDESKRP 367
Cdd:cd14011  203 ---CDPASDMFSLGVLIYAIyNKGKPLFDCVNNLlsYKKNSNQLR----QLSLS-LLEKVPEELRdHVKTLLNVTPEVRP 274
                        170
                 ....*....|
gi 526479851 368 KYKELLKHPF 377
Cdd:cd14011  275 DAEQLSKIPF 284
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
119-313 8.60e-12

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: 65.48  E-value: 8.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV--NKMVHKPSGQ--IMAVKRIRstVDE----KEQKQLLMDLDVVMrssdcPYIVQFYGALFREGDC----W 186
Cdd:cd14055    3 VGKGRFAEVwkAKLKQNASGQyeTVAVKIFP--YEEyaswKNEKDIFTDASLKH-----ENILQFLTAEERGVGLdrqyW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICmelmsTSFdkfykYVYSVLDD-----VIPEEILGKITLATVKALNHL--------KENLKIIHRDIKPSNILLDRSGN 253
Cdd:cd14055   76 LI-----TAY-----HENGSLQDyltrhILSWEDLCKMAGSLARGLAHLhsdrtpcgRPKIPIAHRDLKSSNILVKNDGT 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 254 IKLCDFGISGQL-----VDSIAKTRDAGCRPYMAPERIDPSASRQgyDVRS----DVWSLGITLYELAT 313
Cdd:cd14055  146 CVLADFGLALRLdpslsVDELANSGQVGTARYMAPEALESRVNLE--DLESfkqiDVYSMALVLWEMAS 212
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
112-366 8.71e-12

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: 65.79  E-value: 8.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05615   11 DFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVviQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSfDKFYkYVYSVLDDVIPEEILGKITLATVKALNHLKenlKIIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVDS 268
Cdd:cd05615   91 EYVNGG-DLMY-HIQQVGKFKEPQAVFYAAEISVGLFFLHKK---GIIYRDLKLDNVMLDSEGHIKIADFGMCKEhMVEG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKWNSvfDQLTQVVKGDPPQLSNSEEREfs 348
Cdd:cd05615  166 VTTRTFCGTPDYIAPEII----AYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDE--DELFQSIMEHNVSYPKSLSKE-- 237
                        250       260
                 ....*....|....*....|.
gi 526479851 349 psfinFVNLC---LTKDESKR 366
Cdd:cd05615  238 -----AVSICkglMTKHPAKR 253
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
119-385 9.41e-12

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: 64.81  E-value: 9.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPS-----GQIMAVKRIRS-TVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALfrEGDCWICMELM 192
Cdd:cd14076    9 LGEGEFGKVKLGWPLPKanhrsGVQVAIKLIRRdTQQENCQTSKIMREINILKGLTHPNIVRLLDVL--KTKKYIGIVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSFDKFYKYVYS--VLDDVIPEEILGKItlatVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIA 270
Cdd:cd14076   87 FVSGGELFDYILArrRLKDSVACRLFAQL----ISGVAYLHKK-GVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGC-RP-YMAPERIDPSASRQGYDVrsDVWSLGITLYELATGRFPYpkwnsvfdqltqvvkGDPPQLSNSEEREFS 348
Cdd:cd14076  162 DLMSTSCgSPcYAAPELVVSDSMYAGRKA--DIWSCGVILYAMLAGYLPF---------------DDDPHNPNGDNVPRL 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 349 PSFInfVNLCLTKDESKRPKYKELLKHPFILMYEERA 385
Cdd:cd14076  225 YRYI--CNTPLIFPEYVTPKARDLLRRILVPNPRKRI 259
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
84-318 9.86e-12

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 65.77  E-value: 9.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851  84 IERLRTHSIESSGKLKiSPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSG-QIMAVKRI-RSTVDEKEQKQLLMDLD 161
Cdd:PTZ00426   4 LKNLQLHKKKDSDSTK-EPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFeKSKIIKQKQVDHVFSER 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 162 VVMRSSDCPYIVQFYGALFREGDCWICME-LMSTSFDKFYKYVYSVLDDVipeeilGKITLATVKALNHLKENLKIIHRD 240
Cdd:PTZ00426  83 KILNYINHPFCVNLYGSFKDESYLYLVLEfVIGGEFFTFLRRNKRFPNDV------GCFYAAQIVLIFEYLQSLNIVYRD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526479851 241 IKPSNILLDRSGNIKLCDFGISgQLVDSIAKTRdAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:PTZ00426 157 LKPENLLLDKDGFIKMTDFGFA-KVVDTRTYTL-CGTPEYIAPEIL----LNVGHGKAADWWTLGIFIYEILVGCPPF 228
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
232-370 1.04e-11

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes 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 (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 65.09  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 232 ENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRP--YMAPEridpSASRQGYDVRSDVWSLGITLY 309
Cdd:cd05069  125 ERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPikWTAPE----AALYGRFTIKSDVWSFGILLT 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 310 ELAT-GRFPYPKW--NSVFDQLTQVVKGDPPQLSNSEEREfspsfinFVNLCLTKDESKRPKYK 370
Cdd:cd05069  201 ELVTkGRVPYPGMvnREVLEQVERGYRMPCPQGCPESLHE-------LMKLCWKKDPDERPTFE 257
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
116-378 1.05e-11

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: 64.84  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQiMAVKRIRSTvdEKEQKQLLMDLDVVMRSSDC--------PYIVQFYGALFREgdcwI 187
Cdd:cd14111    8 LDEKARGRFGVIRRCRENATGK-NFPAKIVPY--QAEEKQGVLQEYEILKSLHHerimalheAYITPRYLVLIAE----F 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 C--MELMSTSFDKFYkyvYSVlDDVIpeeilgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGiSGQL 265
Cdd:cd14111   81 CsgKELLHSLIDRFR---YSE-DDVV------GYLVQILQGLEYL-HGRRVLHLDIKPDNIMVTNLNAIKIVDFG-SAQS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIA---KTRDAGCRPYMAPERI--DPSASrqgydvRSDVWSLGITLYELATGRFPYPKWNSvfdQLTQ----VVKGDP 336
Cdd:cd14111  149 FNPLSlrqLGRRTGTLEYMAPEMVkgEPVGP------PADIWSIGVLTYIMLSGRSPFEDQDP---QETEakilVAKFDA 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 337 PQLSNSeereFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14111  220 FKLYPN----VSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
236-377 1.28e-11

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: 65.11  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 236 IIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATG 314
Cdd:cd05587  118 IIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTfCGTPDYIAPEII----AYQPYGKSVDWWAYGVLLYEMLAG 193
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 315 RFPYPKWNSvfDQLTQVVKGDPPQLSNSEEREfspsfinFVNLC---LTKDESKR-----PKYKELLKHPF 377
Cdd:cd05587  194 QPPFDGEDE--DELFQSIMEHNVSYPKSLSKE-------AVSICkglLTKHPAKRlgcgpTGERDIKEHPF 255
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
114-372 1.32e-11

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: 65.49  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREG------DCW 186
Cdd:cd07874   20 QNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLsRPFQNQTHAKRAYREL-VLMKCVNHKNIISLLNVFTPQKsleefqDVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSfdkfykyVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd07874   99 LVMELMDAN-------LCQVIQMELDHERMSYLLYQMLCGIKHL-HSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYP------KWNSVFDQLtqvvkGDP-PQL 339
Cdd:cd07874  171 TSFMMTPYVVTRYYRAPEVI----LGMGYKENVDIWSVGCIMGEMVRHKILFPgrdyidQWNKVIEQL-----GTPcPEF 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 340 SnseeREFSPSFINFVnlcltkdeSKRPKYKEL 372
Cdd:cd07874  242 M----KKLQPTVRNYV--------ENRPKYAGL 262
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
114-329 1.33e-11

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: 65.08  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTvDEKEQKQLLMDLDV-VMRSSDCPYIVQFYGalfregdcwICMELm 192
Cdd:cd07865   15 EKLAKIGQGTFGEVFKARHRKTGQIVALKKVLME-NEKEGFPITALREIkILQLLKHENVVNLIE---------ICRTK- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 STSFDKFYKYVYSVLD----DV--IPEEILGKITLATVKA--------LNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd07865   84 ATPYNRYKGSIYLVFEfcehDLagLLSNKNVKFTLSEIKKvmkmllngLYYIHRN-KILHRDMKAANILITKDGVLKLAD 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526479851 259 FGISGQLvdSIAKTRDAGCRP-------YMAPERIdpSASRQgYDVRSDVWSLGITLYELATgRFPYPKWNSVFDQLT 329
Cdd:cd07865  163 FGLARAF--SLAKNSQPNRYTnrvvtlwYRPPELL--LGERD-YGPPIDMWGAGCIMAEMWT-RSPIMQGNTEQHQLT 234
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
114-377 1.36e-11

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: 65.13  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGAL--------FRegD 184
Cdd:cd07850    3 QNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLsRPFQNVTHAKRAYREL-VLMKLVNHKNIIGLLNVFtpqksleeFQ--D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTSFdkfYKYVYSVLDdvipEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd07850   80 VYLVMELMDANL---CQVIQMDLD----HERMSYLLYQMLCGIKHL-HSAGIIHRDLKPSNIVVKSDCTLKILDFGLART 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYP------KWNSVFDQLtqvvkGDPPQ 338
Cdd:cd07850  152 AGTSFMMTPYVVTRYYRAPEVI----LGMGYKENVDIWSVGCIMGEMIRGTVLFPgtdhidQWNKIIEQL-----GTPSD 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 339 lsnSEEREFSPSFINFVnlcltkdeSKRPKYKellKHPF 377
Cdd:cd07850  223 ---EFMSRLQPTVRNYV--------ENRPKYA---GYSF 247
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
114-378 1.60e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 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 that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 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: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 65.07  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYG------ALFREGDCW 186
Cdd:cd07875   27 QNLKPIGSGAQGIVCAAYDAILERNVAIKKLsRPFQNQTHAKRAYREL-VLMKCVNHKNIIGLLNvftpqkSLEEFQDVY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSfdkfykyVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd07875  106 IVMELMDAN-------LCQVIQMELDHERMSYLLYQMLCGIKHL-HSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYP------KWNSVFDQL----TQVVKGDP 336
Cdd:cd07875  178 TSFMMTPYVVTRYYRAPEVI----LGMGYKENVDIWSVGCIMGEMIKGGVLFPgtdhidQWNKVIEQLgtpcPEFMKKLQ 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526479851 337 PQL-------------------------SNSEEREFSPSFI-NFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd07875  254 PTVrtyvenrpkyagysfeklfpdvlfpADSEHNKLKASQArDLLSKMLVIDASKRISVDEALQHPYI 321
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
106-374 1.69e-11

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: 64.60  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDL---KDLGEIGRG------AYGSVNKMVHKPSgqIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFY 176
Cdd:cd05099    7 WEFPRDRLvlgKPLGEGCFGqvvraeAYGIDKSRPDQTV--TVAVKMLKDNATDKDLADLISEMELMKLIGKHKNIINLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 177 GALFREGDCWICMELMST-SFDKFYK--------YVYSVLDdvIPEEILGKITLAT-----VKALNHLkENLKIIHRDIK 242
Cdd:cd05099   85 GVCTQEGPLYVIVEYAAKgNLREFLRarrppgpdYTFDITK--VPEEQLSFKDLVScayqvARGMEYL-ESRRCIHRDLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 243 PSNILLDRSGNIKLCDFGISGQL--VDSIAKTRDaGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFP 317
Cdd:cd05099  162 ARNVLVTEDNVMKIADFGLARGVhdIDYYKKTSN-GRLPvkWMAPEALFDRV----YTHQSDVWSFGILMWEIFTlGGSP 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 318 YP--KWNSVFDQLTQVVKGDPPQLSNSEerefspsFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05099  237 YPgiPVEELFKLLREGHRMDKPSNCTHE-------LYMLMRECWHAVPTQRPTFKQLVE 288
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
112-374 1.77e-11

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members 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. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk 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: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 64.11  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNkmVHKPSGQI-MAVKRIR----STVDEKEQKQLLMDLDvvmrssdCPYIVQFYGALFREGDCW 186
Cdd:cd05114    5 ELTFMKELGSGLFGVVR--LGKWRAQYkVAIKAIRegamSEEDFIEEAKVMMKLT-------HPKLVQLYGVCTQQKPIY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTS-FDKFYKYVYSVLDdvipEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd05114   76 IVTEFMENGcLLNYLRQRRGKLS----RDMLLSMCQDVCEGMEYLERN-NFIHRDLAARNCLVNDTGVVKVSDFGMTRYV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSiAKTRDAGCR---PYMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWnSVFDQLTQVVKGD---PPQ 338
Cdd:cd05114  151 LDD-QYTSSSGAKfpvKWSPPEVFNYSK----FSSKSDVWSFGVLMWEVFTeGKMPFESK-SNYEVVEMVSRGHrlyRPK 224
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 339 LSnseerefSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05114  225 LA-------SKSVYEVMYSCWHEKPEGRPTFADLLR 253
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
234-379 1.82e-11

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: 62.42  E-value: 1.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   234 LKIIHRDIKPSNILLDRSGNIKLcdFGISGQLVDSIAKtrdaGCRPYMAPEridpSASRQGYDVRSDVWSLGITLYELAT 313
Cdd:smart00750  30 LRELHRQAKSGNILLTWDGLLKL--DGSVAFKTPEQSR----PDPYFMAPE----VIQGQSYTEKADIYSLGITLYEALD 99
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851   314 GRFPYPKWNSVFDQLTQVVKG----DPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFIL 379
Cdd:smart00750 100 YELPYNEERELSAILEILLNGmpadDPRDRSNLEGVSAARSFEDFMRLCASRLPQRREAANHYLAHCRAL 169
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
119-319 2.06e-11

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: 64.63  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRS----TVDEKE----QKQLLMdldvVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGELFAIKALKKgdiiARDEVEslmcEKRIFE----TVNSARHPFLVNLFACFQTPEHVCFVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 ------LMStsfdkfykyvySVLDDVIPEE---------ILGkitlatvkaLNHLKENlKIIHRDIKPSNILLDRSGNIK 255
Cdd:cd05589   83 yaaggdLMM-----------HIHEDVFSEPravfyaacvVLG---------LQFLHEH-KIVYRDLKLDNLLLDTEGYVK 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 256 LCDFGISGQLVDSIAKTRD-AGCRPYMAPERI-DPSASRQgydvrSDVWSLGITLYELATGRFPYP 319
Cdd:cd05589  142 IADFGLCKEGMGFGDRTSTfCGTPEFLAPEVLtDTSYTRA-----VDWWGLGVLIYEMLVGESPFP 202
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
163-327 2.07e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 65.02  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 163 VMRSSDCPYIVQFYGALFRegDCWICMELMSTSFDKfykYVYSVLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIK 242
Cdd:PHA03212 136 ILRAINHPSIIQLKGTFTY--NKFTCLILPRYKTDL---YCYLAAKRNIAICDILAIERSVLRAIQYLHEN-RIIHRDIK 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 243 PSNILLDRSGNIKLCDFGISGQLVDsIAKTRD---AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRfpyp 319
Cdd:PHA03212 210 AENIFINHPGDVCLGDFGAACFPVD-INANKYygwAGTIATNAPELL----ARDPYGPAVDIWSAGIVLFEMATCH---- 280

                 ....*...
gi 526479851 320 kwNSVFDQ 327
Cdd:PHA03212 281 --DSLFEK 286
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
110-312 2.27e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone 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. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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 BMPR1b, 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 BMPR1b 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: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 64.30  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVnkMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcpyIVQFYGALFREGDCWICM 189
Cdd:cd14219    4 AKQIQMVKQIGKGRYGEV--WMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHEN---ILGFIAADIKGTGSWTQL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSFDK--FYKYVYSVLDDvipEEILGKITLATVKALNHLKENL-------KIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd14219   79 YLITDYHENgsLYDYLKSTTLD---TKAMLKLAYSSVSGLCHLHTEIfstqgkpAIAHRDLKSKNILVKKNGTCCIADLG 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQL------VDSIAKTRdAGCRPYMAPERIDPSASRQGYD--VRSDVWSLGITLYELA 312
Cdd:cd14219  156 LAVKFisdtneVDIPPNTR-VGTKRYMPPEVLDESLNRNHFQsyIMADMYSFGLILWEVA 214
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
114-262 2.69e-11

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: 63.63  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKrIRSTvdEKEQKQLLMDLDVVMRSSDCPYI--VQFYGalfREGDC-WICME 190
Cdd:cd14016    3 KLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKK--DSKHPQLEYEAKVYKLLQGGPGIprLYWFG---QEGDYnVMVMD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKY------VYSVLddvipeeILGKITLATVKALnHLKenlKIIHRDIKPSNILLDRSGNIK---LCDFGI 261
Cdd:cd14016   77 LLGPSLEDLFNKcgrkfsLKTVL-------MLADQMISRLEYL-HSK---GYIHRDIKPENFLMGLGKNSNkvyLIDFGL 145

                 .
gi 526479851 262 S 262
Cdd:cd14016  146 A 146
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
119-386 4.34e-11

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; 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 TLK2 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: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 63.54  E-value: 4.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVK------RIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGD--CWICME 190
Cdd:cd14041   14 LGRGGFSEVYKAFDLTEQRYVAVKihqlnkNWRDEKKENYHKHACREYRI-HKELDHPRIVKLYDYFSLDTDsfCTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKYvysvlDDVIPEEILGKITLATVKALNHLKE-NLKIIHRDIKPSNILL---DRSGNIKLCDFGISGQLV 266
Cdd:cd14041   93 CEGNDLDFYLKQ-----HKLMSEKEARSIIMQIVNALKYLNEiKPPIIHYDLKPGNILLvngTACGEIKITDFGLSKIMD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRD--------AGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQ 338
Cdd:cd14041  168 DDSYNSVDgmeltsqgAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATE 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 526479851 339 LSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAV 386
Cdd:cd14041  248 VQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSV 295
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
118-367 4.81e-11

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: 62.89  E-value: 4.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSV----NKMVHKPSGqimavkrIRSTV--DEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFRE---GDCWIC 188
Cdd:cd13975    7 ELGRGQYGVVyacdSWGGHFPCA-------LKSVVppDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYsygGGSSIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMStsfDKFYKYVYSVLDD--VIPEEIlgKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFG------ 260
Cdd:cd13975   80 VLLIM---ERLHRDLYTGIKAglSLEERL--QIALDVVEGIRFL-HSQGLVHRDIKLKNVLLDKKNRAKITDLGfckpea 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 -ISGQLVdsiaktrdaGCRPYMAPERIDPSasrqgYDVRSDVWSLGITLYELATG--RFP--YPKWNSVFDQLTQVVKGD 335
Cdd:cd13975  154 mMSGSIV---------GTPIHMAPELFSGK-----YDNSVDVYAFGILFWYLCAGhvKLPeaFEQCASKDHLWNNVRKGV 219
                        250       260       270
                 ....*....|....*....|....*....|..
gi 526479851 336 PPQLSNSeereFSPSFINFVNLCLTKDESKRP 367
Cdd:cd13975  220 RPERLPV----FDEECWNLMEACWSGDPSQRP 247
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
106-319 5.01e-11

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck 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: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 62.74  E-value: 5.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQImAVKRIRSTVDEKEQkqlLMDLDVVMRSSDCPYIVQFYGALFREgDC 185
Cdd:cd05073    6 WEIPRESLKLEKKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSMSVEA---FLAEANVMKTLQHDKLVKLHAVVTKE-PI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfdKFYKYVYSVLDDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQL 265
Cdd:cd05073   81 YIITEFMAKG--SLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFI-EQRNYIHRDLRAANILVSASLVCKIADFGLARVI 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 266 VDSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYP 319
Cdd:cd05073  158 EDNEYTAREGAKFPikWTAPEAINFGS----FTIKSDVWSFGILLMEIVTyGRIPYP 210
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
119-373 5.20e-11

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. 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. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). 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 EphA 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: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 62.58  E-value: 5.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQ---IMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMST- 194
Cdd:cd05066   12 IGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQRRDFLSEASI-MGQFDHPNIIHLEGVVTRSKPVMIVTEYMENg 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKY---VYSVLDDVipeEILGKITlATVKALNhlkeNLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD--SI 269
Cdd:cd05066   91 SLDAFLRKhdgQFTVIQLV---GMLRGIA-SGMKYLS----DMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDdpEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 270 AKTRDAGCRP--YMAPERIdpsASRQgYDVRSDVWSLGITLYE-LATGRFPYpkWN-SVFDQLTQVVKGD--PPQLSnse 343
Cdd:cd05066  163 AYTTRGGKIPirWTAPEAI---AYRK-FTSASDVWSYGIVMWEvMSYGERPY--WEmSNQDVIKAIEEGYrlPAPMD--- 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 526479851 344 erefSPSFINFVNL-CLTKDESKRPKYKELL 373
Cdd:cd05066  234 ----CPAALHQLMLdCWQKDRNERPKFEQIV 260
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
119-372 5.44e-11

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 62.49  E-value: 5.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSV-NKMVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDlDVVMRSSDCPYIVQFYG-ALFREGDCWICMELMST 194
Cdd:cd05058    3 IGKGHFGCVyHGTLIDSDGQKIhcAVKSLNRITDIEEVEQFLKE-GIIMKDFSHPNVLSLLGiCLPSEGSPLVVLPYMKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SfdKFYKYVYSVLDDVIPEEILGkITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVD----SIA 270
Cdd:cd05058   82 G--DLRNFIRSETHNPTVKDLIG-FGLQVAKGMEYLASK-KFVHRDLAARNCMLDESFTVKVADFGLARDIYDkeyySVH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCR-PYMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYPKWNSvFDQLTQVVKGDP-PQlsnseeREF 347
Cdd:cd05058  158 NHTGAKLPvKWMALE----SLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPDVDS-FDITVYLLQGRRlLQ------PEY 226
                        250       260
                 ....*....|....*....|....*.
gi 526479851 348 SPSFINFVNL-CLTKDESKRPKYKEL 372
Cdd:cd05058  227 CPDPLYEVMLsCWHPKPEMRPTFSEL 252
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
110-376 6.67e-11

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: 62.73  E-value: 6.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKR----IRSTVDEKEQKQLLMDLDVVMRSsdcPYIVQFYGALFREGDC 185
Cdd:cd14138    4 ATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRskkpLAGSVDEQNALREVYAHAVLGQH---SHVVRYYSAWAEDDHM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTsfdkfykyvySVLDDVIPEEI----------LGKITLATVKALNHLkENLKIIHRDIKPSNILLDR----- 250
Cdd:cd14138   81 LIQNEYCNG----------GSLADAISENYrimsyftepeLKDLLLQVARGLKYI-HSMSLVHMDIKPSNIFISRtsipn 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 251 -----------SGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGydvRSDVWSLGITLYElATGRFPYP 319
Cdd:cd14138  150 aaseegdedewASNKVIFKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLP---KADIFALALTVVC-AAGAEPLP 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 320 KwNSvfDQLTQVVKGDPPQLSnseeREFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14138  226 T-NG--DQWHEIRQGKLPRIP----QVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
119-331 8.54e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 62.86  E-value: 8.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRST---VDEKEQKQLLMDLDV---------VMRSSDCPYIVQFYgALFREGDcW 186
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIeisNDVTKDRQLVGMCGIhfttlrelkIMNEIKHENIMGLV-DVYVEGD-F 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 IC--MELMSTSFDKfykyvysVLDDVI--PEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:PTZ00024  95 INlvMDIMASDLKK-------VVDRKIrlTESQVKCILLQILNGLNVL-HKWYFMHRDLSPANIFINSKGICKIADFGLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 263 -----GQLVDSIAKTRDAGCRP----------YMAPERIDPSasrQGYDVRSDVWSLGITLYELATGRFPYPKWNSVfDQ 327
Cdd:PTZ00024 167 rrygyPPYSDTLSKDETMQRREemtskvvtlwYRAPELLMGA---EKYHFAVDMWSVGCIFAELLTGKPLFPGENEI-DQ 242

                 ....
gi 526479851 328 LTQV 331
Cdd:PTZ00024 243 LGRI 246
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
111-378 9.42e-11

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: 61.94  E-value: 9.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 111 EDLKDLGE-IGRGAYGSVNKMVHKPSGQIMAVK-----RIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGD 184
Cdd:cd14195    4 EDHYEMGEeLGSGQFAIVRKCREKGTGKEYAAKfikkrRLSSSRRGVSREEIEREVNI-LREIQHPNIITLHDIFENKTD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 CWICMELMSTS--FDkFYKYVYSVLDDVIPEEIlgKITLATVKALNHLKenlkIIHRDIKPSNI-LLDRSG---NIKLCD 258
Cdd:cd14195   83 VVLILELVSGGelFD-FLAEKESLTEEEATQFL--KQILDGVHYLHSKR----IAHFDLKPENImLLDKNVpnpRIKLID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDSIAKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQV--VKGDP 336
Cdd:cd14195  156 FGIAHKIEAGNEFKNIFGTPEFVAPEIVN----YEPLGLEADMWSIGVITYILLSGASPFLG-ETKQETLTNIsaVNYDF 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 337 PQLSNSEEREFSPSFINFVnlcLTKDESKRPKYKELLKHPFI 378
Cdd:cd14195  231 DEEYFSNTSELAKDFIRRL---LVKDPKKRMTIAQSLEHSWI 269
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
108-313 1.06e-10

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: 62.22  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKP----SGQIMAVKRIR-STVDEKEQKQLLMDldvVMRSSDCPYIVQFYGalfre 182
Cdd:cd05081    1 FEERHLKYISQLGKGNFGSVELCRYDPlgdnTGALVAVKQLQhSGPDQQRDFQREIQ---ILKALHSDFIVKYRG----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 183 gdcwICMELMSTSFDKFYKYVYS-VLDDVIP--EEILGKITL-----ATVKALNHLKENlKIIHRDIKPSNILLDRSGNI 254
Cdd:cd05081   73 ----VSYGPGRRSLRLVMEYLPSgCLRDFLQrhRARLDASRLllyssQICKGMEYLGSR-RCVHRDLAARNILVESEAHV 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 255 KLCDFGISGQLV--DSIAKTRDAGCRP--YMAPERI-DPSASRQgydvrSDVWSLGITLYELAT 313
Cdd:cd05081  148 KIADFGLAKLLPldKDYYVVREPGQSPifWYAPESLsDNIFSRQ-----SDVWSFGVVLYELFT 206
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
225-318 1.08e-10

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, 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. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk 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: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 62.08  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 225 KALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSiaktrDAGC------RP--YMAPEridpSASRQGYD 296
Cdd:cd05043  127 CGMSYL-HRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPM-----DYHClgdnenRPikWMSLE----SLVNKEYS 196
                         90       100
                 ....*....|....*....|...
gi 526479851 297 VRSDVWSLGITLYELAT-GRFPY 318
Cdd:cd05043  197 SASDVWSFGVLLWELMTlGQTPY 219
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
117-378 1.20e-10

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 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: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 61.39  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVNKMVHK--PSGQIMAVKrIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALfregdcwicmELMST 194
Cdd:cd14112    9 SEIFRGRFSVIVKAVDSttETDAHCAVK-IFEVSDEASEAVREFESLRTLQHENVQRLIAAFKPS----------NFAYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVYS--VLDDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLD--RSGNIKLCDFGiSGQLVDSIA 270
Cdd:cd14112   78 VMEKLQEDVFTrfSSNDYYSEEQVATTVRQILDALHYLHFK-GIAHLDVQPDNIMFQsvRSWQVKLVDFG-RAQKVSKLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 271 KTRDAGCRPYMAPERIDPsasRQGYDVRSDVWSLGITLYELATGRFPYpkwNSVFDQLTQV------VKGDPPQLSnsee 344
Cdd:cd14112  156 KVPVDGDTDWASPEFHNP---ETPITVQSDIWGLGVLTFCLLSGFHPF---TSEYDDEEETkenvifVKCRPNLIF---- 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 345 REFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14112  226 VEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
118-341 1.24e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone 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. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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 BMPR1a, 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 BMPR1a 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: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 61.98  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVnkMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcpyIVQFYGALFREGDCWICMELMSTSFD 197
Cdd:cd14220    2 QIGKGRYGEV--WMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHEN---ILGFIAADIKGTGSWTQLYLITDYHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 198 K--FYKYV-YSVLDdvipEEILGKITLATVKALNHLKENL-------KIIHRDIKPSNILLDRSGNIKLCDFGISGQL-- 265
Cdd:cd14220   77 NgsLYDFLkCTTLD----TRALLKLAYSAACGLCHLHTEIygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAVKFns 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 ----VDSIAKTRdAGCRPYMAPERIDPSASRQGYD--VRSDVWSLGITLYELA----TG----RFPYPKWNSV-----FD 326
Cdd:cd14220  153 dtneVDVPLNTR-VGTKRYMAPEVLDESLNKNHFQayIMADIYSFGLIIWEMArrcvTGgiveEYQLPYYDMVpsdpsYE 231
                        250
                 ....*....|....*..
gi 526479851 327 QLTQVV--KGDPPQLSN 341
Cdd:cd14220  232 DMREVVcvKRLRPTVSN 248
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
106-374 1.49e-10

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: 61.96  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSV---------NKMVHKPSGqiMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFY 176
Cdd:cd05100    7 WELSRTRLTLGKPLGEGCFGQVvmaeaigidKDKPNKPVT--VAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 177 GALFREGDCWICMELMSTSFDKFYKYV-------YSVLDDVIPEEILGKITLAT-----VKALNHLKENlKIIHRDIKPS 244
Cdd:cd05100   85 GACTQDGPLYVLVEYASKGNLREYLRArrppgmdYSFDTCKLPEEQLTFKDLVScayqvARGMEYLASQ-KCIHRDLAAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 245 NILLDRSGNIKLCDFGISGQL--VDSIAKTRDaGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYP 319
Cdd:cd05100  164 NVLVTEDNVMKIADFGLARDVhnIDYYKKTTN-GRLPvkWMAPEALFDRV----YTHQSDVWSFGVLLWEIFTlGGSPYP 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 320 --KWNSVFDQLTQVVKGDPPQLSNSEerefspsFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05100  239 giPVEELFKLLKEGHRMDKPANCTHE-------LYMIMRECWHAVPSQRPTFKQLVE 288
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
119-319 1.58e-10

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 61.47  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKP---SGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFR---EGDCWICMELM 192
Cdd:cd05074   17 LGKGEFGSVREAQLKSedgSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRsraKGRLPIPMVIL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 193 StsfdkFYKY-------VYSVLDD---VIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd05074   97 P-----FMKHgdlhtflLMSRIGEepfTLPLQTLVRFMIDIASGMEYL-SSKNFIHRDLAARNCMLNENMTVCVADFGLS 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 263 GQLVDsiAKTRDAGCRP-----YMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP 319
Cdd:cd05074  171 KKIYS--GDYYRQGCASklpvkWLALE----SLADNVYTTHSDVWAFGVTMWEIMTrGQTPYA 227
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
119-378 1.88e-10

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: 61.16  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTvDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSfdK 198
Cdd:cd14183   14 IGDGNFAVVKECVERSTGREYALKIINKS-KCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGG--D 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 FYKYVYSVldDVIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL----DRSGNIKLCDFGISgQLVDSIAKTRd 274
Cdd:cd14183   91 LFDAITST--NKYTERDASGMLYNLASAIKYL-HSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLA-TVVDGPLYTV- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 275 AGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY----PKWNSVFDQ-LTQVVKGDPPQLSNseereFSP 349
Cdd:cd14183  166 CGTPTYVAPEII----AETGYGLKVDIWAAGVITYILLCGFPPFrgsgDDQEVLFDQiLMGQVDFPSPYWDN-----VSD 236
                        250       260
                 ....*....|....*....|....*....
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14183  237 SAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
236-377 2.47e-10

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: 61.35  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 236 IIHRDIKPSNILLDRSGNIKLCDFGISGQ-LVDSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATG 314
Cdd:cd05591  117 VIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGKTTTTFCGTPDYIAPEIL----QELEYGPSVDWWALGVLMYEMMAG 192
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 315 RFPYPKWNSvfDQLTQVVKGD----PPQLSNSEerefspsfINFVNLCLTKDESKR-------PKYKELLKHPF 377
Cdd:cd05591  193 QPPFEADNE--DDLFESILHDdvlyPVWLSKEA--------VSILKAFMTKNPAKRlgcvasqGGEDAIRQHPF 256
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
119-317 2.69e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; 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. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 60.99  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSgqIMAVKRIrstvdeKEQKQLlmDLDVVMRSSDC----------PYIVQFYGALFREGD-CWI 187
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT--EYAVKRL------KEDSEL--DWSVVKNSFLTeveklsrfrhPNIVDLAGYSAQQGNyCLI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 188 CMELMSTSFDKFYKYVYSVLDDVIPEEIlgKITLATVKALNHL-KENLKIIHRDIKPSNILLDRSGNIKLCDFGI----- 261
Cdd:cd14159   71 YVYLPNGSLEDRLHCQVSCPCLSWSQRL--HVLLGTARAIQYLhSDSPSLIHGDVKSSNILLDAALNPKLGDFGLarfsr 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 ---SGQLVDSIAKTRDA-GCRPYMAPERIdpSASRQGYDVrsDVWSLGITLYELATGRFP 317
Cdd:cd14159  149 rpkQPGMSSTLARTQTVrGTLAYLPEEYV--KTGTLSVEI--DVYSFGVVLLELLTGRRA 204
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
119-344 2.69e-10

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: 60.94  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIrstVDEKEQKQllmDLDVVMRSSDCPYIV----------QFYGALFREGDCWIC 188
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL---LDRPKART---EVRLHMMCSGHPNIVqiydvyansvQFPGESSPRARLLIV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTS--FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILL-DRSGN--IKLCDFGisg 263
Cdd:cd14171   88 MELMEGGelFDRISQHRH------FTEKQAAQYTKQIALAVQHC-HSLNIAHRDLKPENLLLkDNSEDapIKLCDFG--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 264 qlvdsIAKTRDAGCRP------YMAPERID-------------PSASRQGYDVRSDVWSLGITLYELATG---------- 314
Cdd:cd14171  158 -----FAKVDQGDLMTpqftpyYVAPQVLEaqrrhrkersgipTSPTPYTYDKSCDMWSLGVIIYIMLCGyppfysehps 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 526479851 315 ----------------RFPYPKWNSVFDQLTQVVKG----DPPQLSNSEE 344
Cdd:cd14171  233 rtitkdmkrkimtgsyEFPEEEWSQISEMAKDIVRKllcvDPEERMTIEE 282
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
110-312 2.88e-10

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: 60.92  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKpsGQIMAVKrIRSTVDEKEQKQLLMDLDVVM-RSSDcpyIVQFYGALFREGDCWIC 188
Cdd:cd14142    4 ARQITLVECIGKGRYGEVWRGQWQ--GESVAVK-IFSSRDEKSWFRETEIYNTVLlRHEN---ILGFIASDMTSRNSCTQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENL-------KIIHRDIKPSNILLDRSGNIKLCDFGI 261
Cdd:cd14142   78 LWLITHYHENGSLYDYLQRTTLDHQEML-RLALSAASGLVHLHTEIfgtqgkpAIAHRDLKSKNILVKSNGQCCIADLGL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 -------SGQLvdSIAKTRDAGCRPYMAPERIDPSASRQGYDV--RSDVWSLGITLYELA 312
Cdd:cd14142  157 avthsqeTNQL--DVGNNPRVGTKRYMAPEVLDETINTDCFESykRVDIYAFGLVLWEVA 214
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
187-377 3.14e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 61.40  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSFDkFYKYVYSVldDVIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:PHA03207 161 VCMVMPKYKCD-LFTYVDRS--GPLPLEQAITIQRRLLEALAYLHGR-GIIHRDVKTENIFLDEPENAVLGDFGAACKLD 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYM---APE--RIDPsasrqgYDVRSDVWSLGITLYELATGRFPY--PKWNSVFDQLTQVVKgdppqL 339
Cdd:PHA03207 237 AHPDTPQCYGWSGTLetnSPEllALDP------YCAKTDIWSAGLVLFEMSVKNVTLfgKQVKSSSSQLRSIIR-----C 305
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 526479851 340 SNSEEREFSPSfiNFVNLCltkdeSKRPKYKELLKHPF 377
Cdd:PHA03207 306 MQVHPLEFPQN--GSTNLC-----KHFKQYAIVLRPPY 336
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
114-385 3.43e-10

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: 61.20  E-value: 3.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 114 KDLGEIGRGAYGSVNKMVHKPSGQIMAVKRI-RSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYG------ALFREGDCW 186
Cdd:cd07876   24 QQLKPIGSGAQGIVCAAFDTVLGINVAVKKLsRPFQNQTHAKRAYREL-VLLKCVNHKNIISLLNvftpqkSLEEFQDVY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMSTSFdkfYKYVYSVLDdvipEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd07876  103 LVMELMDANL---CQVIHMELD----HERMSYLLYQMLCGIKHL-HSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAC 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 267 DSIAKTRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYP------KWNSVFDQL-----------T 329
Cdd:cd07876  175 TNFMMTPYVVTRYYRAPEVI----LGMGYKENVDIWSVGCIMGELVKGSVIFQgtdhidQWNKVIEQLgtpsaefmnrlQ 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 330 QVVKG---DPPQLSNSEEREFSPSFI----------------NFVNLCLTKDESKRPKYKELLKHPFILMYEERA 385
Cdd:cd07876  251 PTVRNyveNRPQYPGISFEELFPDWIfpseserdklktsqarDLLSKMLVIDPDKRISVDEALRHPYITVWYDPA 325
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
106-313 4.47e-10

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 60.05  E-value: 4.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 106 WDFTAEDLKDLGEIGRGAYGSVNKMVHK------PSGQImAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGAL 179
Cdd:cd05062    1 WEVAREKITMSRELGQGSFGMVYEGIAKgvvkdePETRV-AIKTVNEAASMRERIEFLNEASV-MKEFNCHHVVRLLGVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 180 FREGDCWICMELMSTSfdKFYKYVYSVLDDVIPEEILGKITLATV--------KALNHLKENlKIIHRDIKPSNILLDRS 251
Cdd:cd05062   79 SQGQPTLVIMELMTRG--DLKSYLRSLRPEMENNPVQAPPSLKKMiqmageiaDGMAYLNAN-KFVHRDLAARNCMVAED 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 252 GNIKLCDFGISGQLVDS-IAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT 313
Cdd:cd05062  156 FTVKIGDFGMTRDIYETdYYRKGGKGLLPvrWMSPESLKDGV----FTTYSDVWSFGVVLWEIAT 216
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
235-331 5.15e-10

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 60.79  E-value: 5.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRS-GNIKLCDFGISGQLVDS-IAKTRDA-GCRPYMAPERIdpsasrQGYDV-RSDVWSLGITLYE 310
Cdd:COG5752  158 NVIHRDIKPANIIRRRSdGKLVLIDFGVAKLLTITaLLQTGTIiGTPEYMAPEQL------RGKVFpASDLYSLGVTCIY 231
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 526479851 311 LATGRFPY----------------PKWNSVFDQLTQV 331
Cdd:COG5752  232 LLTGVSPFdlfdvsedrwvwrdflPPGTKVSDRLGQI 268
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
113-334 6.26e-10

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: 59.53  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 113 LKDLGEIGRGAYGSVNKMVHKP----SGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGD--CW 186
Cdd:cd05080    6 LKKIRDLGEGHFGKVSLYCYDPtndgTGEMVAVKALKADCGPQHRSGWKQEIDI-LKTLYHENIVKYKGCCSEQGGksLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 187 ICMELMStsfdkfykyvYSVLDDVIPEEilgKITLATV--------KALNHLKENlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd05080   85 LIMEYVP----------LGSLRDYLPKH---SIGLAQLllfaqqicEGMAYLHSQ-HYIHRDLAARNVLLDNDRLVKIGD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGISGQLVDS--IAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKG 334
Cdd:cd05080  151 FGLAKAVPEGheYYRVREDGDSPvfWYAPECLKEYK----FYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQG 226
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
119-385 6.95e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 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: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 59.69  E-value: 6.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVK---RIRSTVDEKEQ---KQLLMDLDVvMRSSDCPYIVQFYGALFREGD--CWICME 190
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVKihqLNKSWRDEKKEnyhKHACREYRI-HKELDHPRIVKLYDYFSLDTDtfCTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTSFDKFYKYvysvlDDVIPEEILGKITLATVKALNHLKE-NLKIIHRDIKPSNILL---DRSGNIKLCDFGISGQL- 265
Cdd:cd14040   93 CEGNDLDFYLKQ-----HKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMd 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 -----VDSIAKT-RDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQL 339
Cdd:cd14040  168 ddsygVDGMDLTsQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEV 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 526479851 340 SNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERA 385
Cdd:cd14040  248 QFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRS 293
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
117-312 7.23e-10

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: 59.59  E-value: 7.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 117 GEIGRGAYGSVnkMVHKPSGQIMAVKRIRST-----VDEKEQKQLLMdldvvMRSsdcPYIVQFYGALFREGDCWICMEL 191
Cdd:cd14056    1 KTIGKGRYGEV--WLGKYRGEKVAVKIFSSRdedswFRETEIYQTVM-----LRH---ENILGFIAADIKSTGSWTQLWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 192 MsTSFDK---FYKYV-YSVLDdviPEEILgKITLATVKALNHL-------KENLKIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd14056   71 I-TEYHEhgsLYDYLqRNTLD---TEEAL-RLAYSAASGLAHLhteivgtQGKPAIAHRDLKSKNILVKRDGTCCIADLG 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 261 I-----SGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYD--VRSDVWSLGITLYELA 312
Cdd:cd14056  146 LavrydSDTNTIDIPPNPRVGTKRYMAPEVLDDSINPKSFEsfKMADIYSFGLVLWEIA 204
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
119-260 7.41e-10

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: 56.68  E-value: 7.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEkEQKQLLMDLDVVMRSSD-CPYIVQFYGALFREGDCWICMELMSTSfd 197
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNE-EGEDLESEMDILRRLKGlELNIPKVLVTEDVDGPNILLMELVKGG-- 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 198 kfykyvysVLDDVIPEEILGKItlATVKALNHLKENLK------IIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd13968   78 --------TLIAYTQEEELDEK--DVESIMYQLAECMRllhsfhLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
227-377 7.61e-10

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: 59.64  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 227 LNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAG------------CRPYMAPERIdpsASRQG 294
Cdd:cd07866  128 INYLHEN-HILHRDIKAANILIDNQGILKIADFGLARPYDGPPPNPKGGGgggtrkytnlvvTRWYRPPELL---LGERR 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 295 YDVRSDVWSLGITLYELATGRfPYPKWNSVFDQLTQVVK--GDPPQ--------LSNSEE---------------REFSP 349
Cdd:cd07866  204 YTTAVDIWGIGCVFAEMFTRR-PILQGKSDIDQLHLIFKlcGTPTEetwpgwrsLPGCEGvhsftnyprtleerfGKLGP 282
                        170       180
                 ....*....|....*....|....*...
gi 526479851 350 SFINFVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd07866  283 EGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
115-381 9.21e-10

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 59.79  E-value: 9.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTvDEKEQKQLLMDLDVVmRSSDCPYIVQFYGALFREGD---------- 184
Cdd:cd07854    9 DLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLT-DPQSVKHALREIKII-RRLDHDNIVKVYEVLGPSGSdltedvgslt 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 185 ----CWICMELMSTSFDKfykyvysVLD-DVIPEEilgKITLATVKALNHLK--ENLKIIHRDIKPSNILLDRSGNI-KL 256
Cdd:cd07854   87 elnsVYIVQEYMETDLAN-------VLEqGPLSEE---HARLFMYQLLRGLKyiHSANVLHRDLKPANVFINTEDLVlKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGISgQLVDSIAK-----TRDAGCRPYMAPERIdpsASRQGYDVRSDVWSLGITLYELATGRFPYP------KWNSVF 325
Cdd:cd07854  157 GDFGLA-RIVDPHYShkgylSEGLVTKWYRSPRLL---LSPNNYTKAIDMWAAGCIFAEMLTGKPLFAgaheleQMQLIL 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526479851 326 DQLTQVVKGDPPQL----------SNSEER--------EFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMY 381
Cdd:cd07854  233 ESVPVVREEDRNELlnvipsfvrnDGGEPRrplrdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCY 306
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
227-358 1.11e-09

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: 59.16  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 227 LNHLKENlKIIHRDIKPSNILL-DRSGNI--KLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDpsasRQGYDVRSDVWS 303
Cdd:cd14039  112 IQYLHEN-KIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDLDQGSLCTSFVGTLQYLAPELFE----NKSYTVTVDYWS 186
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 304 LGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEER----EFSPSFINFVNLC 358
Cdd:cd14039  187 FGTMVFECIAGFRPFLHNLQPFTWHEKIKKKDPKHIFAVEEMngevRFSTHLPQPNNLC 245
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
116-344 1.16e-09

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: 59.24  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEK------EQKQLLMDL---------DVVMRSSDCPYIVQFYGALF 180
Cdd:cd07872   11 LEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGapctaiREVSLLKDLkhanivtlhDIVHTDKSLTLVFEYLDKDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 RE--GDCWICMELMSTSFdkfykYVYSVLDDVipeeilgkitlatvkALNHLKenlKIIHRDIKPSNILLDRSGNIKLCD 258
Cdd:cd07872   91 KQymDDCGNIMSMHNVKI-----FLYQILRGL---------------AYCHRR---KVLHRDLKPQNLLINERGELKLAD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 259 FGIS-GQLVDSIAKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVK--GD 335
Cdd:cd07872  148 FGLArAKSVPTKTYSNEVVTLWYRPPDVLLGSSE---YSTQIDMWGVGCIFFEMASGRPLFPG-STVEDELHLIFRllGT 223
                        250
                 ....*....|....
gi 526479851 336 P-----PQLSNSEE 344
Cdd:cd07872  224 PteetwPGISSNDE 237
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
237-374 1.18e-09

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 59.53  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 237 IHRDIKPSNILLDRSGNIKLCDFGISGQL-VDSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYEL-A 312
Cdd:cd05104  236 IHRDLAARNILLTHGRITKICDFGLARDIrNDSNYVVKGNARLPvkWMAPESIFECV----YTFESDVWSYGILLWEIfS 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 313 TGRFPYPKWnSVFDQLTQVVKGDPPQLSNseerEFSPS-FINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd05104  312 LGSSPYPGM-PVDSKFYKMIKEGYRMDSP----EFAPSeMYDIMRSCWDADPLKRPTFKQIVQ 369
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
119-377 1.21e-09

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: 59.64  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRS--TVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd05626    9 LGIGAFGEVCLACKVDTHALYAMKTLRKkdVLNRNQVAHVKAERDI-LAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKYVYSVLDDVIPEEILGKITLATVKAlnhlkENLKIIHRDIKPSNILLDRSGNIKLCDFGI--------------- 261
Cdd:cd05626   88 MMSLLIRMEVFPEVLARFYIAELTLAIESV-----HKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthnskyyqk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 262 ----------SGQLVDSIAKTRDA-----------------------GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITL 308
Cdd:cd05626  163 gshirqdsmePSDLWDDVSNCRCGdrlktleqratkqhqrclahslvGTPNYIAPEVL----LRKGYTQLCDWWSVGVIL 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 309 YELATGRFPYPKWNSVFDQLtQVVKGD-----PPQLsnseerEFSPSFINFV-NLCLTKDES-KRPKYKELLKHPF 377
Cdd:cd05626  239 FEMLVGQPPFLAPTPTETQL-KVINWEntlhiPPQV------KLSPEAVDLItKLCCSAEERlGRNGADDIKAHPF 307
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
237-319 1.59e-09

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 59.09  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 237 IHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCR---PYMAPERIDPSAsrqgYDVRSDVWSLGITLYEL-A 312
Cdd:cd05106  234 IHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARlpvKWMAPESIFDCV----YTVQSDVWSYGILLWEIfS 309

                 ....*..
gi 526479851 313 TGRFPYP 319
Cdd:cd05106  310 LGKSPYP 316
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
119-312 1.73e-09

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: 58.22  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKpsGQIMAVKRI-----RSTVDEKEQKQLLMdldvvMRSSDcpyIVQFYGALFREGDCWICMELMS 193
Cdd:cd14143    3 IGKGRFGEVWRGRWR--GEDVAVKIFssreeRSWFREAEIYQTVM-----LRHEN---ILGFIAADNKDNGTWTQLWLVS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 ------TSFDKFYKYVYSVlddvipeEILGKITLATVKALNHLKENL-------KIIHRDIKPSNILLDRSGNIKLCDFG 260
Cdd:cd14143   73 dyhehgSLFDYLNRYTVTV-------EGMIKLALSIASGLAHLHMEIvgtqgkpAIAHRDLKSKNILVKKNGTCCIADLG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 261 ISGQLvDSIAKTRD------AGCRPYMAPERIDPSASRQGYDV--RSDVWSLGITLYELA 312
Cdd:cd14143  146 LAVRH-DSATDTIDiapnhrVGTKRYMAPEVLDDTINMKHFESfkRADIYALGLVFWEIA 204
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
237-372 2.22e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 58.88  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 237 IHRDIKPSNILLDRSGNIKLCDFGISGQLV-DSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYEL-A 312
Cdd:cd05105  259 VHRDLAARNVLLAQGKIVKICDFGLARDIMhDSNYVSKGSTFLPvkWMAPESIFDNL----YTTLSDVWSYGILLWEIfS 334
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 313 TGRFPYPKW---NSVFDQLTQVVKGDPPQLSNSEEREFSPSfinfvnlCLTKDESKRPKYKEL 372
Cdd:cd05105  335 LGGTPYPGMivdSTFYNKIKSGYRMAKPDHATQEVYDIMVK-------CWNSEPEKRPSFLHL 390
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
112-375 2.33e-09

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 58.02  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEI-GRGAYGSVNK-MVHKPSG--QIMAVKRIRstVDEKEQKQL--LMDLDVVMRSSDCPYIVQFYGalfregdc 185
Cdd:cd14204    7 NLLSLGKVlGEGEFGSVMEgELQQPDGtnHKVAVKTMK--LDNFSQREIeeFLSEAACMKDFNHPNVIRLLG-------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 wICMELMSTSFDK------FYKY-------VYSVLDD---VIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLD 249
Cdd:cd14204   77 -VCLEVGSQRIPKpmvilpFMKYgdlhsflLRSRLGSgpqHVPLQTLLKFMIDIALGMEYL-SSRNFLHRDLAARNCMLR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 250 RSGNIKLCDFGISGQLV--DSIAKTRDAGCR-PYMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP--KWNS 323
Cdd:cd14204  155 DDMTVCVADFGLSKKIYsgDYYRQGRIAKMPvKWIAVE----SLADRVYTVKSDVWAFGVTMWEIATrGMTPYPgvQNHE 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 526479851 324 VFDQLT--QVVKGDPPQLSNSEEREFSpsfinfvnlCLTKDESKRPKYKELLKH 375
Cdd:cd14204  231 IYDYLLhgHRLKQPEDCLDELYDIMYS---------CWRSDPTDRPTFTQLREN 275
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
237-320 2.39e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 58.87  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 237 IHRDIKPSNILLDRSGNIKLCDFGISGQLV-DSIAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT 313
Cdd:cd05107  261 VHRDLAARNVLICEGKLVKICDFGLARDIMrDSNYISKGSTFLPlkWMAPESIFNNL----YTTLSDVWSFGILLWEIFT 336

                 ....*...
gi 526479851 314 -GRFPYPK 320
Cdd:cd05107  337 lGGTPYPE 344
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
108-313 2.58e-09

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: 58.02  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVNKMVHKP----SGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREG 183
Cdd:cd05079    1 FEKRFLKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEI-LRNLYHENIVKYKGICTEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 184 DCWI--CMELMSTSFDKFYkyvysvlddvIPEEIlGKITLATV--------KALNHLKENlKIIHRDIKPSNILLDRSGN 253
Cdd:cd05079   80 GNGIklIMEFLPSGSLKEY----------LPRNK-NKINLKQQlkyavqicKGMDYLGSR-QYVHRDLAARNVLVESEHQ 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526479851 254 IKLCDFGISGQLVD-----SIAKTRDAGCRPYmAPERIDPSAsrqgYDVRSDVWSLGITLYELAT 313
Cdd:cd05079  148 VKIGDFGLTKAIETdkeyyTVKDDLDSPVFWY-APECLIQSK----FYIASDVWSFGVTLYELLT 207
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
107-379 3.53e-09

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 57.68  E-value: 3.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 107 DFTAEDLKDLGEIGRGAYGSV----------------NKMVHKPSgqIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcP 170
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVhlceaeglaeflgegaPEFDGQPV--LVAVKMLRADVTKTARNDFLKEIKIMSRLKN-P 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 171 YIVQFYGALFREGDCWICMELMST-SFDKFY--KYVYSVL--DDVIPEEILGKITLATVKALNHLK--ENLKIIHRDIKP 243
Cdd:cd05097   78 NIIRLLGVCVSDDPLCMITEYMENgDLNQFLsqREIESTFthANNIPSVSIANLLYMAVQIASGMKylASLNFVHRDLAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 244 SNILLDRSGNIKLCDFGISGQLVDS-IAKTRDAGCRP--YMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT--GRFPY 318
Cdd:cd05097  158 RNCLVGNHYTIKIADFGMSRNLYSGdYYRIQGRAVLPirWMAWESILLGK----FTTASDVWAFGVTLWEMFTlcKEQPY 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 319 PKWN--SVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELlkHPFIL 379
Cdd:cd05097  234 SLLSdeQVIENTGEFFRNQGRQIYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI--HHFLR 294
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
119-335 3.61e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 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: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 57.73  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDL--DVVMRSSDCPYIVQFYGAL-FREGDCWICMELMSTS 195
Cdd:cd14229    8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGIlaRLSNENADEFNFVRAYECFqHRNHTCLVFEMLEQNL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 196 FDKFYKYVYSVLddviPEEILGKITLATVKALNHLKeNLKIIHRDIKPSNILL----DRSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14229   88 YDFLKQNKFSPL----PLKVIRPILQQVATALKKLK-SLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSKTVCS 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 272 TRdAGCRPYMAPERIDPSASRQGYdvrsDVWSLGITLYELATGRFPYPKWNSvFDQL-----TQVVKGD 335
Cdd:cd14229  163 TY-LQSRYYRAPEIILGLPFCEAI----DMWSLGCVIAELFLGWPLYPGALE-YDQIryisqTQGLPGE 225
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
119-313 3.87e-09

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: 57.37  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNK-MVHkpsGQIMAVKrirstVDEKEQKQLLMDLDVVMRSS--DCPYIVQFYGALFREG-DCWICMELMST 194
Cdd:cd14054    3 IGQGRYGTVWKgSLD---ERPVAVK-----VFPARHRQNFQNEKDIYELPlmEHSNILRFIGADERPTaDGRMEYLLVLE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENLK--------IIHRDIKPSNILLDRSGNIKLCDFGISGQLV 266
Cdd:cd14054   75 YAPKGSLCSYLRENTLDWMSSC-RMALSLTRGLAYLHTDLRrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLAMVLR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 267 DS-----------IAKTRDAGCRPYMAPERIDPSAS---RQGYDVRSDVWSLGITLYELAT 313
Cdd:cd14054  154 GSslvrgrpgaaeNASISEVGTLRYMAPEVLEGAVNlrdCESALKQVDVYALGLVLWEIAM 214
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
112-388 4.43e-09

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 57.31  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGAYGSVNKMVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd05088    8 DIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMS-------------TSFDKFYKYVYSVLDDVIPEEILgKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKL 256
Cdd:cd05088   88 EYAPhgnlldflrksrvLETDPAFAIANSTASTLSSQQLL-HFAADVARGMDYLSQK-QFIHRDLAARNILVGENYVAKI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 257 CDFGIS-GQLVdSIAKTRDAGCRPYMAPERIDPSAsrqgYDVRSDVWSLGITLYELAT-GRFPYPKWN--SVFDQLTQVV 332
Cdd:cd05088  166 ADFGLSrGQEV-YVKKTMGRLPVRWMAIESLNYSV----YTTNSDVWSYGVLLWEIVSlGGTPYCGMTcaELYEKLPQGY 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 333 KGDPPQLSNSEEREfspsfinFVNLCLTKDESKRPKYKELLKhPFILMYEERAVEV 388
Cdd:cd05088  241 RLEKPLNCDDEVYD-------LMRQCWREKPYERPSFAQILV-SLNRMLEERKTYV 288
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
115-376 5.41e-09

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: 56.86  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQL-LMDLDVVMRSSDCPYIVQFYGAlFREGDCWICMELMS 193
Cdd:cd14139    4 ELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLaLHEVYAHAVLGHHPHVVRYYSA-WAEDDHMIIQNEYC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TSfdkfykyvySVLDDVIPEEI----------LGKITLATVKALNHLkENLKIIHRDIKPSNILLDR------------- 250
Cdd:cd14139   83 NG---------GSLQDAISENTksgnhfeepeLKDILLQVSMGLKYI-HNSGLVHLDIKPSNIFICHkmqsssgvgeevs 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 251 -------SGNI--KLCDFGisgqLVDSIAKTR-DAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLyELATGRFPYPK 320
Cdd:cd14139  153 needeflSANVvyKIGDLG----HVTSINKPQvEEGDSRFLANEILQEDYR---HLPKADIFALGLTV-ALAAGAEPLPT 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 321 WNSVFDQLTqvvKGDPPQLSnseeREFSPSFINFVNLCLTKDESKRPKYKELLKHP 376
Cdd:cd14139  225 NGAAWHHIR---KGNFPDVP----QELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
102-378 5.80e-09

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: 57.45  E-value: 5.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 102 PEQHWDFTAEDLKdlgEIGRGAYGSVNKMVHKPSGQIMAVKRIRstvDEK-------EQKQLLMDLDVVMRSSDCPYIVQ 174
Cdd:cd14224   59 PHDHIAYRYEVLK---VIGKGSFGQVVKAYDHKTHQHVALKMVR---NEKrfhrqaaEEIRILEHLKKQDKDNTMNVIHM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 175 FYGALFREGDCwICMELMSTSF------DKFYKYvysvlddviPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILL 248
Cdd:cd14224  133 LESFTFRNHIC-MTFELLSMNLyelikkNKFQGF---------SLQLVRKFAHSILQCLDALHRN-KIIHCDLKPENILL 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 249 D---RSGnIKLCDFGIS---GQLVDSIAKTRDagcrpYMAPERIdpSASRQGYDVrsDVWSLGITLYELATGRFPYPKWN 322
Cdd:cd14224  202 KqqgRSG-IKVIDFGSScyeHQRIYTYIQSRF-----YRAPEVI--LGARYGMPI--DMWSFGCILAELLTGYPLFPGED 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 323 SVfDQLTQVVK--GDPPQ---------------------------------LSNS-----------EEREFS-------- 348
Cdd:cd14224  272 EG-DQLACMIEllGMPPQklletskraknfisskgypryctvttlpdgsvvLNGGrsrrgkmrgppGSKDWVtalkgcdd 350
                        330       340       350
                 ....*....|....*....|....*....|
gi 526479851 349 PSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14224  351 PLFLDFLKRCLEWDPAARMTPSQALRHPWL 380
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
211-315 6.01e-09

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 56.40  E-value: 6.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 211 IPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIakTRDAGCRPYMAPERIDPSA 290
Cdd:cd05576  110 IPEECIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC--DSDAIENMYCAPEVGGISE 186
                         90       100
                 ....*....|....*....|....*
gi 526479851 291 SRQGydvrSDVWSLGITLYELATGR 315
Cdd:cd05576  187 ETEA----CDWWSLGALLFELLTGK 207
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
110-336 6.61e-09

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: 56.62  E-value: 6.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 110 AEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVvMRSSDCPYIVQFYGALFREGDCWICM 189
Cdd:cd07869    4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASL-LKGLKHANIVLLHDIIHTKETLTLVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 ELMSTSFdkfYKYVYSVLDDVIPEEIlgKITL-ATVKALNHLKENLkIIHRDIKPSNILLDRSGNIKLCDFGIS-GQLVD 267
Cdd:cd07869   83 EYVHTDL---CQYMDKHPGGLHPENV--KLFLfQLLRGLSYIHQRY-ILHRDLKPQNLLISDTGELKLADFGLArAKSVP 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 268 SIAKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQV--VKGDP 336
Cdd:cd07869  157 SHTYSNEVVTLWYRPPDVLLGSTE---YSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIflVLGTP 224
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
122-326 7.66e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 56.81  E-value: 7.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 122 GAYGSVnkMVHKPSGQIMAVkrirstVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGdcWICMELMSTSFDkFYK 201
Cdd:PHA03209  77 GSEGRV--FVATKPGQPDPV------VLKIGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGA--ITCMVLPHYSSD-LYT 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 202 YVySVLDDVIPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYM 281
Cdd:PHA03209 146 YL-TKRSRPLPIDQALIIEKQILEGLRYLHA-QRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETN 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 526479851 282 APERIdpsaSRQGYDVRSDVWSLGITLYELatgrFPYPKwnSVFD 326
Cdd:PHA03209 224 APEVL----ARDKYNSKADIWSAGIVLFEM----LAYPS--TIFE 258
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
116-377 8.62e-09

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: 56.52  E-value: 8.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEIGRGAYGSVNKMVHKPS--GQIMAVKRIRSTVDEKE--------QKQLLMDL---------DVVMRSSD-CPYIVQF 175
Cdd:cd07842    5 EGCIGRGTYGRVYKAKRKNGkdGKEYAIKKFKGDKEQYTgisqsacrEIALLRELkhenvvslvEVFLEHADkSVYLLFD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 176 YGalfrEGDCW-ICmelmstsfdkfyKYVYSVLDDVIPEEILGKITLATVKALNHLKENLkIIHRDIKPSNILL----DR 250
Cdd:cd07842   85 YA----EHDLWqII------------KFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNW-VLHRDLKPANILVmgegPE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 251 SGNIKLCDFGISgQLVDSIAKTRDAGCRP-----YMAPERIdpSASRQgYDVRSDVWSLGITLYELATGRFPYP------ 319
Cdd:cd07842  148 RGVVKIGDLGLA-RLFNAPLKPLADLDPVvvtiwYRAPELL--LGARH-YTKAIDIWAIGCIFAELLTLEPIFKgreaki 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 320 KWNSVF--DQLTQV--VKGDPPQ---------------LSNSEEREFS-PSFINFVNLC--------------LTKDESK 365
Cdd:cd07842  224 KKSNPFqrDQLERIfeVLGTPTEkdwpdikkmpeydtlKSDTKASTYPnSLLAKWMHKHkkpdsqgfdllrklLEYDPTK 303
                        330
                 ....*....|..
gi 526479851 366 RPKYKELLKHPF 377
Cdd:cd07842  304 RITAEEALEHPY 315
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
119-374 9.65e-09

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: 55.99  E-value: 9.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDekeQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMSTSfdk 198
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVD---QHKIVREISLLQKLSH-PNIVRYLGICVKDEKLHPILEYVSGG--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 fykyvysVLDDVIPEEILG-----KITLAT--VKALNHLKENlKIIHRDIKPSNILLDRSGNIK---LCDFGISGQLVDS 268
Cdd:cd14156   74 -------CLEELLAREELPlswreKVELACdiSRGMVYLHSK-NIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGEM 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 269 IAKTRD-----AGCRPYMAPE--RIDPsasrqgYDVRSDVWSLGITLYELaTGRFPYPKwnsvfDQLTQVVK-GDPPQLS 340
Cdd:cd14156  146 PANDPErklslVGSAFWMAPEmlRGEP------YDRKVDVFSFGIVLCEI-LARIPADP-----EVLPRTGDfGLDVQAF 213
                        250       260       270
                 ....*....|....*....|....*....|....
gi 526479851 341 NSEEREFSPSFINFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14156  214 KEMVPGCPEPFLDLAASCCRMDAFKRPSFAELLD 247
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
109-378 1.15e-08

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: 55.69  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 109 TAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRStvdEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREgDCWIC 188
Cdd:cd14110    1 TEKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPY---KPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSP-RHLVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 189 MELMSTSFDKFY----KYVYSvldDVIPEEILGKItLATVKALNhlkeNLKIIHRDIKPSNILLDRSGNIKLCDFGISGQ 264
Cdd:cd14110   77 IEELCSGPELLYnlaeRNSYS---EAEVTDYLWQI-LSAVDYLH----SRRILHLDLRSENMIITEKNLLKIVDLGNAQP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 265 LVDSIAKTRDAgCRPY---MAPERIDpsasRQGYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVVKGDpPQLSN 341
Cdd:cd14110  149 FNQGKVLMTDK-KGDYvetMAPELLE----GQGAGPQTDIWAIGVTAFIMLSADYPVSS-DLNWERDRNIRKGK-VQLSR 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 526479851 342 SEErEFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14110  222 CYA-GLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
108-320 1.19e-08

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: 55.93  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 108 FTAEDLKDLGEIGRGAYGSVnkMVHKPSG-------QIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDcPYIVQFYGaLF 180
Cdd:cd05046    2 FPRSNLQEITTLGRGEFGEV--FLAKAKGieeeggeTLVLVKALQKTKDENLQSEFRRELDMFRKLSH-KNVVRLLG-LC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 181 REGDCWiCMELMSTSF---DKFYKYVYSVLDDVIPEEILGKITLATV----KALNHLKeNLKIIHRDIKPSNILLDRSGN 253
Cdd:cd05046   78 REAEPH-YMILEYTDLgdlKQFLRATKSKDEKLKPPPLSTKQKVALCtqiaLGMDHLS-NARFVHRDLAARNCLVSSQRE 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 254 IKLCDFGISG--------QLVDSIAKTRdagcrpYMAPERIdpsaSRQGYDVRSDVWSLGITLYELAT-GRFPYPK 320
Cdd:cd05046  156 VKVSLLSLSKdvynseyyKLRNALIPLR------WLAPEAV----QEDDFSTKSDVWSFGVLMWEVFTqGELPFYG 221
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
235-409 1.66e-08

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: 55.91  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGIS--GQLVDSIAKTRDAGCRPYMAPERIdpSASRQgYDVRSDVWSLGITLYELA 312
Cdd:cd07853  123 GILHRDIKPGNLLVNSNCVLKICDFGLArvEEPDESKHMTQEVVTQYYRAPEIL--MGSRH-YTSAVDIWSVGCIFAELL 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 313 TGRFPYpKWNSVFDQLTQVVK--GDPPQLSNSEEREFS-----------PSF--------------INFVNLCLTKDESK 365
Cdd:cd07853  200 GRRILF-QAQSPIQQLDLITDllGTPSLEAMRSACEGArahilrgphkpPSLpvlytlssqatheaVHLLCRMLVFDPDK 278
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 526479851 366 RPKYKELLKHPFILMYEERAVEVACYVCKIldqmpaTPSSPMYV 409
Cdd:cd07853  279 RISAADALAHPYLDEGRLRYHTCMCKCCYT------TSGGRVYT 316
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
119-338 2.06e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK 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: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 55.53  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCP--YIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd14211    7 LGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADefNFVRAYECFQHKNHTCLVFEMLEQNL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKY-VYSVLddviPEEILGKITLATVKALNHLKEnLKIIHRDIKPSNILLDRSGN----IKLCDFGiSGQLVDSIAK 271
Cdd:cd14211   87 YDFLKQnKFSPL----PLKYIRPILQQVLTALLKLKS-LGLIHADLKPENIMLVDPVRqpyrVKVIDFG-SASHVSKAVC 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 272 TRDAGCRPYMAPERI--DPsasrqgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQVV--KGDPPQ 338
Cdd:cd14211  161 STYLQSRYYRAPEIIlgLP------FCEAIDMWSLGCVIAELFLGWPLYPG-SSEYDQIRYISqtQGLPAE 224
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
118-331 2.09e-08

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 55.21  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMVHKPSGQIMAVKRIR-STVDEKEQKQLLMDLDVV--MRSSDcpyIVQFYGALFREGDCWICMELMST 194
Cdd:PLN00009   9 KIGEGTYGVVYKARDRVTNETIALKKIRlEQEDEGVPSTAIREISLLkeMQHGN---IVRLQDVVHSEKRLYLVFEYLDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDK-------FYK-------YVYSVLDDVipeeilgkitlatvkALNHlkeNLKIIHRDIKPSNILLDRSGN-IKLCDF 259
Cdd:PLN00009  86 DLKKhmdsspdFAKnprliktYLYQILRGI---------------AYCH---SHRVLHRDLKPQNLLIDRRTNaLKLADF 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526479851 260 GISGQL-VDSIAKTRDAGCRPYMAPERIdpSASRQgYDVRSDVWSLGITLYELATGRFPYPKwNSVFDQLTQV 331
Cdd:PLN00009 148 GLARAFgIPVRTFTHEVVTLWYRAPEIL--LGSRH-YSTPVDIWSVGCIFAEMVNQKPLFPG-DSEIDELFKI 216
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
118-372 2.50e-08

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: 54.66  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 118 EIGRGAYGSVNKMV-HKPSGQIM--AVKRIRStvDEKEQKQLLMDLDV---VMRSSDCPYIVQFYGALFregDCWICM-- 189
Cdd:cd05040    2 KLGDGSFGVVRRGEwTTPSGKVIqvAVKCLKS--DVLSQPNAMDDFLKevnAMHSLDHPNLIRLYGVVL---SSPLMMvt 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 190 EL--MSTSFDKFYKYVYSVLddvIPeeILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGisgqLVD 267
Cdd:cd05040   77 ELapLGSLLDRLRKDQGHFL---IS--TLCDYAVQIANGMAYL-ESKRFIHRDLAARNILLASKDKVKIGDFG----LMR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTRD------------AGCrpymAPERIDpsaSRQgYDVRSDVWSLGITLYELAT-GRFPYPKWNSVfdQLTQVVKG 334
Cdd:cd05040  147 ALPQNEDhyvmqehrkvpfAWC----APESLK---TRK-FSHASDVWMFGVTLWEMFTyGEEPWLGLNGS--QILEKIDK 216
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 526479851 335 DPPQLsnsEEREFSPSFINFVNL-CLTKDESKRPKYKEL 372
Cdd:cd05040  217 EGERL---ERPDDCPQDIYNVMLqCWAHKPADRPTFVAL 252
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
216-313 4.25e-08

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: 54.26  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 216 LGKITLATVKALNHLKENLK---------IIHRDIKPSNILLdrSGNIKLC--DFGISGQLVDSIaKTRDA----GCRPY 280
Cdd:cd14053   94 LCKIAESMARGLAYLHEDIPatngghkpsIAHRDFKSKNVLL--KSDLTACiaDFGLALKFEPGK-SCGDThgqvGTRRY 170
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 526479851 281 MAPERIDP--SASRQGYdVRSDVWSLGITLYELAT 313
Cdd:cd14053  171 MAPEVLEGaiNFTRDAF-LRIDMYAMGLVLWELLS 204
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
235-336 4.33e-08

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: 54.31  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGIS-GQLVDSIAKTRDAGCRPYMAPERIDPSASrqgYDVRSDVWSLGITLYELAT 313
Cdd:cd07844  118 RVLHRDLKPQNLLISERGELKLADFGLArAKSVPSKTYSNEVVTLWYRPPDVLLGSTE---YSTSLDMWGVGCIFYEMAT 194
                         90       100
                 ....*....|....*....|....*
gi 526479851 314 GRFPYPKWNSVFDQLTQVVK--GDP 336
Cdd:cd07844  195 GRPLFPGSTDVEDQLHKIFRvlGTP 219
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
115-374 4.55e-08

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 53.86  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 115 DLGE-IGRGAYGSVnkmVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMS 193
Cdd:cd14153    3 EIGElIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 194 TsfdkfyKYVYSVLDD---VIPEEILGKITLATVKALNHLKENlKIIHRDIKPSNILLDrSGNIKLCDFG---ISGQLVD 267
Cdd:cd14153   80 G------RTLYSVVRDakvVLDVNKTRQIAQEIVKGMGYLHAK-GILHKDLKSKNVFYD-NGKVVITDFGlftISGVLQA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 268 SIAKTR---DAGCRPYMAPERI-----DPSASRQGYDVRSDVWSLGITLYELATGRFPYpKWNSVFDQLTQVVKGDPPQL 339
Cdd:cd14153  152 GRREDKlriQSGWLCHLAPEIIrqlspETEEDKLPFSKHSDVFAFGTIWYELHAREWPF-KTQPAEAIIWQVGSGMKPNL 230
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 526479851 340 SN-SEEREFSpsfiNFVNLCLTKDESKRPKYKELLK 374
Cdd:cd14153  231 SQiGMGKEIS----DILLFCWAYEQEERPTFSKLME 262
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
112-378 5.06e-08

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-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 uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized 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: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 53.88  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 112 DLKDLGEIGRGA-YGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLdVVMRSSDCPYIVQFYGALFREGDCWICME 190
Cdd:cd14088    1 DRYDLGQVIKTEeFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKNEI-NILKMVKHPNILQLVDVFETRKEYFIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 191 LMSTS--FDKFYKYVYsvlddvIPEEILGKITLATVKALNHLkENLKIIHRDIKPSNIL-LDRSGNIKLC--DFGISgQL 265
Cdd:cd14088   80 LATGRevFDWILDQGY------YSERDTSNVIRQVLEAVAYL-HSLKIVHRNLKLENLVyYNRLKNSKIVisDFHLA-KL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 266 VDSIAKtRDAGCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYpkWNSVFDQ---------LTQVVKGDp 336
Cdd:cd14088  152 ENGLIK-EPCGTPEYLAPEVV----GRQRYGRPVDCWAIGVIMYILLSGNPPF--YDEAEEDdyenhdknlFRKILAGD- 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 526479851 337 PQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFI 378
Cdd:cd14088  224 YEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
210-377 5.45e-08

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: 54.28  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 210 VIPEEiLGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGI--------------SGQLV--DSIAKTR 273
Cdd:cd05625   97 VFPED-LARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqSGDHLrqDSMDFSN 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 274 DAG----CR----------------------------PYMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPYPKW 321
Cdd:cd05625  176 EWGdpenCRcgdrlkplerraarqhqrclahslvgtpNYIAPEVL----LRTGYTQLCDWWSVGVILFEMLVGQPPFLAQ 251
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 322 NSVFDQLT----QVVKGDPPQLSNSEErefSPSFInfVNLCL-TKDESKRPKYKELLKHPF 377
Cdd:cd05625  252 TPLETQMKvinwQTSLHIPPQAKLSPE---ASDLI--IKLCRgPEDRLGKNGADEIKAHPF 307
PTZ00284 PTZ00284
protein kinase; Provisional
216-318 5.87e-08

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 54.59  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 216 LGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGN----------------IKLCDFGisGQLVDSIAKTRDAGCRP 279
Cdd:PTZ00284 233 LAQIIFQTGVALDYFHTELHLMHTDLKPENILMETSDTvvdpvtnralppdpcrVRICDLG--GCCDERHSRTAIVSTRH 310
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 526479851 280 YMAPERIdpsaSRQGYDVRSDVWSLGITLYELATGRFPY 318
Cdd:PTZ00284 311 YRSPEVV----LGLGWMYSTDMWSMGCIIYELYTGKLLY 345
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
116-319 8.25e-08

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 53.31  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 116 LGEI-GRGAYGSVNK-MVHKPSGQIM--AVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDC------ 185
Cdd:cd05035    3 LGKIlGEGEFGSVMEaQLKQDDGSQLkvAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppsp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 186 WICMELMSTSfDKFYKYVYSVLDDV---IPEEILGKITLATVKALNHLkENLKIIHRDIKPSNILLDRSGNIKLCDFGIS 262
Cdd:cd05035   83 MVILPFMKHG-DLHSYLLYSRLGGLpekLPLQTLLKFMVDIAKGMEYL-SNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526479851 263 GQLV--DSIAKTRDAGCR-PYMAPEridpSASRQGYDVRSDVWSLGITLYELAT-GRFPYP 319
Cdd:cd05035  161 RKIYsgDYYRQGRISKMPvKWIALE----SLADNVYTSKSDVWSFGVTMWEIATrGQTPYP 217
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
226-337 8.30e-08

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: 53.41  E-value: 8.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 226 ALNHLKENlKIIHRDIKPSNILLDR--SGNIKLCDFG---ISGQLVDSIAKTRDagcrpYMAPERI--DPsasrqgYDVR 298
Cdd:cd14212  115 ALSVLKDA-RIIHCDLKPENILLVNldSPEIKLIDFGsacFENYTLYTYIQSRF-----YRSPEVLlgLP------YSTA 182
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 526479851 299 SDVWSLGITLYELATG--RFPypkWNSVFDQLTQVVK--GDPP 337
Cdd:cd14212  183 IDMWSLGCIAAELFLGlpLFP---GNSEYNQLSRIIEmlGMPP 222
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
276-377 1.05e-07

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 52.73  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 276 GCRPYMAPERIDPSASRQGYdvRSDVWSLGITLYELATGRFPYP--KWNSVFDQLTQVVKGDPPQLsnseerefSPSFIN 353
Cdd:cd14022  148 GCPAYVSPEILNTSGSYSGK--AADVWSLGVMLYTMLVGRYPFHdiEPSSLFSKIRRGQFNIPETL--------SPKAKC 217
                         90       100
                 ....*....|....*....|....
gi 526479851 354 FVNLCLTKDESKRPKYKELLKHPF 377
Cdd:cd14022  218 LIRSILRREPSERLTSQEILDHPW 241
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
119-328 1.28e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 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: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 53.17  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLlmDLDVVMR----SSDCPYIVQFYGALFREGDCWICMELMST 194
Cdd:cd14227   23 LGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI--EVSILARlsteSADDYNFVRAYECFQHKNHTCLVFEMLEQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 195 SFDKFYKY-VYSVLddviPEEILGKITLATVKALNHLKeNLKIIHRDIKPSNILL----DRSGNIKLCDFGISGQLVDSI 269
Cdd:cd14227  101 NLYDFLKQnKFSPL----PLKYIRPILQQVATALMKLK-SLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASHVSKAV 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 526479851 270 AKTRdAGCRPYMAPERIDPSASRQGYdvrsDVWSLGITLYELATGRFPYPKwNSVFDQL 328
Cdd:cd14227  176 CSTY-LQSRYYRAPEIILGLPFCEAI----DMWSLGCVIAELFLGWPLYPG-ASEYDQI 228
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
235-338 1.38e-07

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: 52.66  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 235 KIIHRDIKPSNILLDRSGNIKLCDFGisgqlvdsIAKTRDAGCRPYMA--------PERIDPSASRqgYDVRSDVWSLGI 306
Cdd:cd07870  118 HILHRDLKPQNLLISYLGELKLADFG--------LARAKSIPSQTYSSevvtlwyrPPDVLLGATD--YSSALDIWGAGC 187
                         90       100       110
                 ....*....|....*....|....*....|....
gi 526479851 307 TLYELATGRFPYPKWNSVFDQLTQV--VKGDPPQ 338
Cdd:cd07870  188 IFIEMLQGQPAFPGVSDVFEQLEKIwtVLGVPTE 221
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
236-384 1.47e-07

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin 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: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 52.56  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 236 IIHRDIKPSNILL--DRSGNIKLCDFGISGQLvdsiaKTRDAGCRPYMAPERIDPSA-SRQGYDVRSDVWSLGITLYELA 312
Cdd:cd14104  118 IGHFDIRPENIIYctRRGSYIKIIEFGQSRQL-----KPGDKFRLQYTSAEFYAPEVhQHESVSTATDMWSLGCLVYVLL 192
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526479851 313 TGRFPYPKWNSvfDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEER 384
Cdd:cd14104  193 SGINPFEAETN--QQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWLKQGMET 262
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
119-328 1.58e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 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: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 52.78  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRS--SDCPYIVQFYGALFREGDCWICMELMSTSF 196
Cdd:cd14228   23 LGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSenADEYNFVRSYECFQHKNHTCLVFEMLEQNL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 197 DKFYKY-VYSVLddviPEEILGKITLATVKALNHLKeNLKIIHRDIKPSNILL----DRSGNIKLCDFGISGQLVDSIAK 271
Cdd:cd14228  103 YDFLKQnKFSPL----PLKYIRPILQQVATALMKLK-SLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSKAVCS 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 526479851 272 TRdAGCRPYMAPERIDPSASRQGYdvrsDVWSLGITLYELATGRFPYPKwNSVFDQL 328
Cdd:cd14228  178 TY-LQSRYYRAPEIILGLPFCEAI----DMWSLGCVIAELFLGWPLYPG-ASEYDQI 228
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
218-347 1.59e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. 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. The LRRK1 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: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 52.27  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 218 KITLATVKALNHLKENlKIIHRDIKPSNILL-----DRSGNIKLCDFGISGQLVDSIAKTRDaGCRPYMAPErIDPsasR 292
Cdd:cd14067  118 KIAYQIAAGLAYLHKK-NIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHEGALGVE-GTPGYQAPE-IRP---R 191
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526479851 293 QGYDVRSDVWSLGITLYELATGRFPYPKWNSVfdQLT-QVVKGDPPQLSNSEEREF 347
Cdd:cd14067  192 IVYDEKVDMFSYGMVLYELLSGQRPSLGHHQL--QIAkKLSKGIRPVLGQPEEVQF 245
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
119-375 1.59e-07

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: 52.09  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 119 IGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDekeQKQLLMDLDVVMRSSDcPYIVQFYGALFREGDCWICMELMStsfdk 198
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSN---RANMLREVQLMNRLSH-PNILRFMGVCVHQGQLHALTEYIN----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 199 fYKYVYSVLDDVIPEEILGKITLA--TVKALNHLKENlKIIHRDIKPSNILLDRSGN---IKLCDFGISGQLVD-SIAKT 272
Cdd:cd14155   72 -GGNLEQLLDSNEPLSWTVRVKLAldIARGLSYLHSK-GIFHRDLTSKNCLIKRDENgytAVVGDFGLAEKIPDySDGKE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479851 273 RDA--GCRPYMAPERIdpsaSRQGYDVRSDVWSLGITLYELaTGRFP-----YPKWNSV---FDQLTQVVkGDPPqlsns 342
Cdd:cd14155  150 KLAvvGSPYWMAPEVL----RGEPYNEKADVFSYGIILCEI-IARIQadpdyLPRTEDFgldYDAFQHMV-GDCP----- 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 526479851 343 eerefsPSFINFVNLCLTKDESKRPKYKELLKH 375
Cdd:cd14155  219 ------PDFLQLAFNCCNMDPKSRPSFHDIVKT 245
 
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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