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Conserved domains on  [gi|66773086|ref|NP_001019572|]
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serine/threonine-protein kinase SBK1 [Homo sapiens]

Protein Classification

SBK1 family serine/threonine-protein kinase( domain architecture ID 10195655)

SBK1 (SH3 domain binding kinase 1) family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
59-317 6.29e-178

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: 496.46  E-value: 6.29e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYAPAGDLFD 138
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKRVSGTIPYTAPE 218
Cdd:cd13987  81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTVKRVSGTIPYTAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 219 VCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWRRFTEPALRMFQRLLAL 298
Cdd:cd13987 161 VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMFKKLLAP 240
                       250
                ....*....|....*....
gi 66773086 299 EPERRGPAKEVFRFLKHEL 317
Cdd:cd13987 241 EPERRCSIKEVFKYLGDRW 259
 
Name Accession Description Interval E-value
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
59-317 6.29e-178

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: 496.46  E-value: 6.29e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYAPAGDLFD 138
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKRVSGTIPYTAPE 218
Cdd:cd13987  81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTVKRVSGTIPYTAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 219 VCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWRRFTEPALRMFQRLLAL 298
Cdd:cd13987 161 VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMFKKLLAP 240
                       250
                ....*....|....*....
gi 66773086 299 EPERRGPAKEVFRFLKHEL 317
Cdd:cd13987 241 EPERRCSIKEVFKYLGDRW 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
53-316 3.77e-72

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 227.03  E-value: 3.77e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086     53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKkdRERILREIKILKKLKH-PNIVRLYDV-FEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVGCRVKRVS- 209
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDG-HVKLADFGLARQLDPGEKLTTf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    210 -GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWqrgrLPGLPSQWRRFTEPA 288
Cdd:smart00220 157 vGTPEYMAPEVLL-----GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKP----KPPFPPPEWDISPEA 227
                          250       260
                   ....*....|....*....|....*...
gi 66773086    289 LRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEA---LQHP 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
52-407 2.11e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 171.73  E-value: 2.11e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFA 127
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARERFRREARALARLNH-PNIVRVYDV-GEEDGRPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVG----C 203
Cdd:COG0515  86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL--TPDGRVKLIDFGIARALGgatlT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAdaffeEFVRWQRGRLPGLPSQWRR 283
Cdd:COG0515 164 QTGTVVGTPGYMAPE-----QARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPA-----ELLRAHLREPPPPPSELRP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 284 FTEPAL-RMFQRLLALEPERRGP-AKEVFRFLKHELTSELRRRPSHRARKPPGDRPPAAGPLRLEAPGPLKRTVLTESGS 361
Cdd:COG0515 234 DLPPALdAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 362 GSRPAPPAVGSVPLPVPVPVPVPVPVPVPEPGLAPQGPPGRTDGRA 407
Cdd:COG0515 314 AAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALA 359
Pkinase pfam00069
Protein kinase domain;
53-315 5.97e-36

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 131.60  E-value: 5.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---TKLKNFLREVSITNSLsSSPFIIKVFDvVFETEDCYVFAQE 129
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKikkKKDKNILREIKILKKL-NHPNIVRLYD-AFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDfmhgrqlvhrdikpenvllfdrecRRVKLADFgmtrrvgCrvkrvs 209
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE------------------------SGSSLTTF-------V------ 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   210 GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPGLPSqwrRFTEPAL 289
Cdd:pfam00069 122 GTPWYMAPEVLG-----GNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIY--ELIIDQPYAFPELPS---NLSEEAK 191
                         250       260
                  ....*....|....*....|....*.
gi 66773086   290 RMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQA---LQH 214
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
47-275 1.54e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 113.03  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   47 SDVTKHYELVRELG--KGTYGKVDLVVYKGTGtKMalkFVNKS-KTKLKNFLrEVSITNSLSSSPFIIKVFDVVFeTEDC 123
Cdd:PHA03390  10 VQFLKNCEIVKKLKliDGKFGKVSVLKHKPTQ-KL---FVQKIiKAKNFNAI-EPMVHQLMKDNPNFIKLYYSVT-TLKG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVlLFDRECRRVKLADFGMTRRVG- 202
Cdd:PHA03390  84 HVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENV-LYDRAKDRIYLCDYGLCKIIGt 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086  203 --CRvkrvSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLP 275
Cdd:PHA03390 163 psCY----DGTLDYFSPE-----KIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLP 228
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
94-257 8.58e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 79.45  E-value: 8.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   94 FLREV-SITnSLSSsPFIIKVFDVVfETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVH 172
Cdd:NF033483  54 FRREAqSAA-SLSH-PNIVSVYDVG-EDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  173 RDIKPENVLLfDREcRRVKLADFG---------MTRRVGcrvkrVSGTIPYTAPEvcQAgRadGLAVDTGVDVWAFGVLI 243
Cdd:NF033483 131 RDIKPQNILI-TKD-GRVKVTDFGiaralssttMTQTNS-----VLGTVHYLSPE--QA-R--GGTVDARSDIYSLGIVL 198
                        170
                 ....*....|....
gi 66773086  244 FCVLTGNFPWEAAS 257
Cdd:NF033483 199 YEMLTGRPPFDGDS 212
 
Name Accession Description Interval E-value
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
59-317 6.29e-178

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: 496.46  E-value: 6.29e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYAPAGDLFD 138
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKRVSGTIPYTAPE 218
Cdd:cd13987  81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTVKRVSGTIPYTAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 219 VCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWRRFTEPALRMFQRLLAL 298
Cdd:cd13987 161 VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMFKKLLAP 240
                       250
                ....*....|....*....
gi 66773086 299 EPERRGPAKEVFRFLKHEL 317
Cdd:cd13987 241 EPERRCSIKEVFKYLGDRW 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
53-316 3.77e-72

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 227.03  E-value: 3.77e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086     53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKkdRERILREIKILKKLKH-PNIVRLYDV-FEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVGCRVKRVS- 209
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDG-HVKLADFGLARQLDPGEKLTTf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    210 -GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWqrgrLPGLPSQWRRFTEPA 288
Cdd:smart00220 157 vGTPEYMAPEVLL-----GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKP----KPPFPPPEWDISPEA 227
                          250       260
                   ....*....|....*....|....*...
gi 66773086    289 LRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEA---LQHP 252
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
52-316 3.11e-62

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: 201.59  E-value: 3.11e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---LKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKeeiEEKIKREIEIMKLLNH-PNIIKLYEV-IETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRV--GCRVK 206
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-DKNG-NLKIIDFGLSNEFrgGSLLK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASGAdaffEEFVRWQRGRLPgLPSqwrRFTE 286
Cdd:cd14003 157 TFCGTPAYAAPEVLLGRKYDGPK----ADVWSLGVILYAMLTGYLPFDDDNDS----KLFRKILKGKYP-IPS---HLSP 224
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 287 PALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14003 225 DARDLIRRMLVVDPSKRITIEEI---LNHP 251
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
51-309 4.22e-60

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: 196.40  E-value: 4.22e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---LKNFLREVSItNSLSSSPFIIKVFDVVFETEDCYVFa 127
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPgdcPENIKKEVCI-QKMLSHKNVVRFYGHRREGEFQYLF- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRVK- 206
Cdd:cd14069  79 LEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEND--NLKISDFGLATVFRYKGKe 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVS----GTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWEAASGADaffEEFVRWQRGRLPGLpSQWR 282
Cdd:cd14069 157 RLLnkmcGTLPYVAPELLAKKKYRA----EPVDVWSCGIVLFAMLAGELPWDQPSDSC---QEYSDWKENKKTYL-TPWK 228
                       250       260
                ....*....|....*....|....*..
gi 66773086 283 RFTEPALRMFQRLLALEPERRGPAKEV 309
Cdd:cd14069 229 KIDTAALSLLRKILTENPNKRITIEDI 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
59-313 2.33e-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: 2.33e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAPAGDL 136
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKklLEELLREIEILKKLNH-PNIVKLYDV-FETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVGCRVKRVSGTIPYT 215
Cdd:cd00180  79 KDLLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSD--GTVKLADFGLAKDLDSDDSLLKTTGGTT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 216 APEVCQAGRADGLAVDTGVDVWAFGVLIFCVltgnfpweaasgadaffeefvrwqrgrlpglpsqwrrftEPALRMFQRL 295
Cdd:cd00180 157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------------EELKDLIRRM 197
                       250
                ....*....|....*...
gi 66773086 296 LALEPERRGPAKEVFRFL 313
Cdd:cd00180 198 LQYDPKKRPSAKELLEHL 215
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
48-311 4.50e-52

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: 175.66  E-value: 4.50e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---------TKLKNFLREVSITNSLSSsPFIIKVFDVvF 118
Cdd:cd14084   3 ELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrreiNKPRNIETEIEILKKLSH-PCIIKIEDF-F 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECR-RVKLADFGM 197
Cdd:cd14084  81 DAEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEcLIKITDFGL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCR--VKRVSGTIPYTAPEVCQAGRADGLAvdTGVDVWAFGVLIFCVLTGNFPWeaasgADAFFEEFVRWQ--RGR 273
Cdd:cd14084 161 SKILGETslMKTLCGTPTYLAPEVLRSFGTEGYT--RAVDCWSLGVILFICLSGYPPF-----SEEYTQMSLKEQilSGK 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 274 LPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14084 234 YTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALE 271
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
52-316 1.33e-50

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: 171.51  E-value: 1.33e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---TKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlksEDEEMLRREIEILKRLDH-PNIVKLYEV-FEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRE-CRRVKLADFGMTRRV--GCRV 205
Cdd:cd05117  79 ELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDpDSPIKIIDFGLAKIFeeGEKL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVcqagrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADaFFEEFvrwQRGRLPGLPSQWRRFT 285
Cdd:cd05117 159 KTVCGTPYYVAPEV-----LKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQE-LFEKI---LKGKYSFDSPEWKNVS 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 66773086 286 EPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd05117 230 EEAKDLIKRLLVVDPKKRLTAAEA---LNHP 257
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
52-315 5.53e-49

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: 167.38  E-value: 5.53e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGkvdlVVYKGT----GTKMALKFVNKSKTK----LKNFLREVSITNSLSSsPFIIKVFDVvFETEDC 123
Cdd:cd14014   1 RYRLVRLLGRGGMG----EVYRARdtllGRPVAIKVLRPELAEdeefRERFLREARALARLSH-PNIVRVYDV-GEDDGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGC 203
Cdd:cd14014  75 PYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG--RVKLTDFGIARALGD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 ----RVKRVSGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASgadafFEEFVRWQRGRLPGLPS 279
Cdd:cd14014 153 sgltQTGSVLGTPAYMAPEQARGGPVDPRS-----DIYSLGVVLYELLTGRPPFDGDS-----PAAVLAKHLQEAPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 280 QWRRFTEPAL-RMFQRLLALEPERRGP-AKEVFRFLKH 315
Cdd:cd14014 223 PLNPDVPPALdAIILRALAKDPEERPQsAAELLAALRA 260
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
52-407 2.11e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 171.73  E-value: 2.11e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFA 127
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARERFRREARALARLNH-PNIVRVYDV-GEEDGRPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVG----C 203
Cdd:COG0515  86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL--TPDGRVKLIDFGIARALGgatlT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAdaffeEFVRWQRGRLPGLPSQWRR 283
Cdd:COG0515 164 QTGTVVGTPGYMAPE-----QARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPA-----ELLRAHLREPPPPPSELRP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 284 FTEPAL-RMFQRLLALEPERRGP-AKEVFRFLKHELTSELRRRPSHRARKPPGDRPPAAGPLRLEAPGPLKRTVLTESGS 361
Cdd:COG0515 234 DLPPALdAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 362 GSRPAPPAVGSVPLPVPVPVPVPVPVPVPEPGLAPQGPPGRTDGRA 407
Cdd:COG0515 314 AAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALA 359
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
59-311 3.98e-45

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: 157.33  E-value: 3.98e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKS---------------KTKLKNFLREVSITNSLSSsPFIIK---VFDVVFET 120
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSrlrkrregkndrgkiKNALDDVRREIAIMKKLDH-PNIVRlyeVIDDPESD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFaqEYAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFG-- 196
Cdd:cd14008  80 KLYLVL--EYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTAD--GTVKISDFGvs 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 -MTRRVGCRVKRVSGTIPYTAPEVCQAGRA--DGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASgadaFFEEFVRWQRGr 273
Cdd:cd14008 156 eMFEDGNDTLQKTAGTPAFLAPELCDGDSKtySGKA----ADIWALGVTLYCLVFGRLPFNGDN----ILELYEAIQNQ- 226
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 66773086 274 lpGLPSQWRRFTEPALR-MFQRLLALEPERRGPAKEVFR 311
Cdd:cd14008 227 --NDEFPIPPELSPELKdLLRRMLEKDPEKRITLKEIKE 263
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
52-315 1.64e-44

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: 155.33  E-value: 1.64e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS---KTKL-KNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFA 127
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSqlqKSGLeHQLRREIEIQSHLRH-PNILRLYGY-FEDKKRIYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVgCRVKR 207
Cdd:cd14007  79 LEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNG--ELKLADFGWSVHA-PSNRR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VS--GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAffeeFVRWQRGRLPgLPSQwrrFT 285
Cdd:cd14007 156 KTfcGTLDYLPPEMVE-----GKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQET----YKRIQNVDIK-FPSS---VS 222
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 286 EPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd14007 223 PEAKDLISKLLQKDPSKRLSLEQV---LNH 249
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
53-316 6.45e-44

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: 153.83  E-value: 6.45e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALK---FVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFaQE 129
Cdd:cd06606   2 WKKGELLGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEELEALEREIRILSSLKH-PNIVRYLGTERTENTLNIF-LE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVG-----CR 204
Cdd:cd06606  80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSD--GVVKLADFGCAKRLAeiatgEG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVCQAGRAdglavDTGVDVWAFGVLIFCVLTGNFPWE------AASGADAFFEEfvrwqrgrLPGLP 278
Cdd:cd06606 158 TKSLRGTPYWMAPEVIRGEGY-----GRAADIWSLGCTVIEMATGKPPWSelgnpvAALFKIGSSGE--------PPPIP 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 279 SqwrRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd06606 225 E---HLSEEAKDFLRKCLQRDPKKRPTADEL---LQHP 256
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
59-311 4.35e-43

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: 152.08  E-value: 4.35e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLV--VYKGTGTKMALKFVNKSK--TKLKNF----LREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQEY 130
Cdd:cd13994   1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRRDdeSKRKDYvkrlTSEYIISSKLHH-PNIVKVLDLCQDLHGKWCLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVG-------C 203
Cdd:cd13994  80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL-DEDG-VLKLTDFGTAEVFGmpaekesP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRwQRGRLPGLPSQWRR 283
Cdd:cd13994 158 MSAGLCGSEPYMAPEVFTSGSYDGRA----VDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEK-SGDFTNGPYEPIEN 232
                       250       260
                ....*....|....*....|....*....
gi 66773086 284 FT-EPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd13994 233 LLpSECRRLIYRMLHPDPEKRITIDEALN 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
52-316 9.47e-42

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: 148.24  E-value: 9.47e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL--REVSITNSLSSsPFIIKVFDVvFETEDCYVFAQE 129
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMieNEVAILRRVKH-PNIVQLIEE-YDTDTELYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRE--CRRVKLADFGMTRRVGCRVKR 207
Cdd:cd14095  79 LVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgSKSLKLADFGLATEVKEPLFT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVcqagradgLAvDTG----VDVWAFGVLIFCVLTGnFPWEAASGADAffEE-FVRWQRGRLPGLPSQWR 282
Cdd:cd14095 159 VCGTPTYVAPEI--------LA-ETGyglkVDIWAAGVITYILLCG-FPPFRSPDRDQ--EElFDLILAGEFEFLSPYWD 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 66773086 283 RFTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14095 227 NISDSAKDLISRMLVVDPEKRYSAGQV---LDHP 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
52-316 1.14e-41

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: 148.01  E-value: 1.14e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN-----FLREVSITNSLSSsPFIIKVFDVvFETEDCYVF 126
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDknlqlFQREINILKSLEH-PGIVRLIDW-YEDDQHIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRV--GCR 204
Cdd:cd14098  79 VMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIhtGTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVC-QAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADafFEEFVRwqRGRLPGLPSQWRR 283
Cdd:cd14098 159 LVTFCGTMAYLAPEILmSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLP--VEKRIR--KGRYTQPPLVDFN 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 284 FTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14098 235 ISEEAIDFILRLLDVDPEKRMTAAQA---LDHP 264
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
59-309 2.13e-41

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: 146.89  E-value: 2.13e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITnSLSSSPFIIKVFdVVFETEDCYVFAQEYAPAG 134
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKevehTLNERNIL-ERVNHPFIVKLH-YAFQTEEKLYLVLDYVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVGCRVKR---VSGT 211
Cdd:cd05123  79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL-DSD-GHIKLTDFGLAKELSSDGDRtytFCGT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IPYTAPEVCQaGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEaASGADAFFEEFVRWQrgrlPGLPSqwrRFTEPALRM 291
Cdd:cd05123 157 PEYLAPEVLL-GKGYGKA----VDWWSLGVLLYEMLTGKPPFY-AENRKEIYEKILKSP----LKFPE---YVSPEAKSL 223
                       250       260
                ....*....|....*....|.
gi 66773086 292 FQRLLALEPERR---GPAKEV 309
Cdd:cd05123 224 ISGLLQKDPTKRlgsGGAEEI 244
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
52-311 1.65e-40

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: 145.09  E-value: 1.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL--REVSITNSLSSsPFIIKVFDVvFETEDCYVFAQE 129
Cdd:cd14185   1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMieSEILIIKSLSH-PNIVKLFEV-YETEKEIYLILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRE--CRRVKLADFGMTRRVGCRVKR 207
Cdd:cd14185  79 YVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkSTTLKLADFGLAKYVTGPIFT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCqAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASGADAffEEFVRWQRGRLPGLPSQWRRFTEP 287
Cdd:cd14185 159 VCGTPTYVAPEIL-SEKGYGLE----VDMWAAGVILYILLCGFPPFRSPERDQE--ELFQIIQLGHYEFLPPYWDNISEA 231
                       250       260
                ....*....|....*....|....
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14185 232 AKDLISRLLVVDPEKRYTAKQVLQ 255
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
52-309 1.26e-39

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: 142.41  E-value: 1.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK-------TKLKnflREVSITnSLSSSPFIIKVFDVVFETEDCY 124
Cdd:cd14079   3 NYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKiksldmeEKIR---REIQIL-KLFRHPHIIRLYEVIETPTDIF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VfAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDReCRRVKLADFGMTR--RVG 202
Cdd:cd14079  79 M-VMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL-DS-NMNVKIADFGLSNimRDG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSGTIPYTAPEVCqAGRadgLAVDTGVDVWAFGVLIFCVLTGNFPweaasgadaFFEE-----FVRWQRGRLPgL 277
Cdd:cd14079 156 EFLKTSCGSPNYAAPEVI-SGK---LYAGPEVDVWSCGVILYALLCGSLP---------FDDEhipnlFKKIKSGIYT-I 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 278 PSQwrrFTEPALRMFQRLLALEPERRGPAKEV 309
Cdd:cd14079 222 PSH---LSPGARDLIKRMLVVDPLKRITIPEI 250
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-303 6.74e-39

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: 140.62  E-value: 6.74e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL----REVSITnSLSSSPFIIKVFDVVFETEDCYvFAQ 128
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVeqikREIAIM-KLLRHPNIVELHEVMATKTKIF-FVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMT-----RRVGC 203
Cdd:cd14663  80 ELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDG--NLKISDFGLSalseqFRQDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEV-CQAGRaDGLAvdtgVDVWAFGVLIFCVLTGNFPWEaasgADAFFEEFVRWQRGRLPgLPSqWr 282
Cdd:cd14663 158 LLHTTCGTPNYVAPEVlARRGY-DGAK----ADIWSCGVILFVLLAGYLPFD----DENLMALYRKIMKGEFE-YPR-W- 225
                       250       260
                ....*....|....*....|.
gi 66773086 283 rFTEPALRMFQRLLALEPERR 303
Cdd:cd14663 226 -FSPGAKSLIKRILDPNPSTR 245
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
48-315 8.32e-39

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: 140.56  E-value: 8.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELV-RELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDC 123
Cdd:cd14106   4 NINEVYTVEsTPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrrGQDCRNEILHEIAVLELCKDCPRVVNLHEV-YETRSE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADFGMTRRV- 201
Cdd:cd14106  83 LILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFPLGDIKLCDFGISRVIg 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPWeaasGADAFFEEFVRWQRGRLPGLPSQ 280
Cdd:cd14106 163 eGEEIREILGTPDYVAPEILS---YEPISLAT--DMWSIGVLTYVLLTGHSPF----GGDDKQETFLNISQCNLDFPEEL 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 66773086 281 WRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd14106 234 FKDVSPLAIDFIKRLLVKDPEKRLTAKEC---LEH 265
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
52-312 1.02e-38

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: 139.91  E-value: 1.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKlKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFA 127
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlsnmSEKER-EEALNEVKLLSKLKH-PNIVKYYES-FEENGKLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVGC 203
Cdd:cd08215  78 MEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKD--GVVKLGDFGISKVLES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RV---KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASgadaFFEEFVRWQRGRLPGLPSQ 280
Cdd:cd08215 156 TTdlaKTVVGTPYYLSPELCE-----NKPYNYKSDIWALGCVLYELCTLKHPFEANN----LPALVYKIVKGQYPPIPSQ 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 281 WRRFtepaLRMF-QRLLALEPERRGPAKEVFRF 312
Cdd:cd08215 227 YSSE----LRDLvNSMLQKDPEKRPSANEILSS 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
53-252 1.27e-38

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: 140.01  E-value: 1.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYK--GTGTKMALKFVNKSKTK---LKNFL-REVSITNSLSSsPFIIKVFDVvFETEDCYVF 126
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTksGLKEKVACKIIDKKKAPkdfLEKFLpRELEILRKLRH-PNIIQVYSI-FERGSKVFI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd14080  80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL--DSNNNVKLSDFGFARLCPDDDG 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 207 RVS-----GTIPYTAPEVCQagradGLAVD-TGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd14080 158 DVLsktfcGSAAYAAPEILQ-----GIPYDpKKYDIWSLGVILYIMLCGSMP 204
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
59-303 5.79e-38

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: 137.78  E-value: 5.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAPAGDLFD 138
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQH-PRIIQLHEA-YESPTELVLILELCSGGELLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRV--GCRVKRVSGTIPYTA 216
Cdd:cd14006  79 RLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLnpGEELKEIFGTPEFVA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 217 PEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAD----------AFFEEFvrwqrgrlpglpsqWRRFTE 286
Cdd:cd14006 159 PEIVN-----GEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQEtlanisacrvDFSEEY--------------FSSVSQ 219
                       250
                ....*....|....*..
gi 66773086 287 PALRMFQRLLALEPERR 303
Cdd:cd14006 220 EAKDFIRKLLVKEPRKR 236
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
56-315 1.38e-37

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: 137.23  E-value: 1.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQEYA 131
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSdmiaKNQVTNVKAERAIMMIQGESPYVAKLY-YSFQSKDYLYLVMEYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDrECRRVKLADFGMTR--RVGCRVKRVS 209
Cdd:cd05611  80 NGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPEN-LLID-QTGHLKLTDFGLSRngLEKRHNKKFV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASgADAFFEEFVRwqrgRLPGLPSQWRRFTEP-A 288
Cdd:cd05611 158 GTPDYLAPETIL-----GVGDDKMSDWWSLGCVIFEFLFGYPPFHAET-PDAVFDNILS----RRINWPEEVKEFCSPeA 227
                       250       260
                ....*....|....*....|....*..
gi 66773086 289 LRMFQRLLALEPERRGPAKEVFRFLKH 315
Cdd:cd05611 228 VDLINRLLCMDPAKRLGANGYQEIKSH 254
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
53-311 6.58e-37

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: 135.07  E-value: 6.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL----REVSITNsLSSSPFIIKVFDVVFETEDCYVfAQ 128
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLmkveREIAIMK-LIEHPNVLKLYDVYENKKYLYL-VL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTR--RVGCRVK 206
Cdd:cd14081  81 EYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEK--NNIKIADFGMASlqPEGSLLE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASgADAFFEefvRWQRGRlPGLPSqwrrFTE 286
Cdd:cd14081 159 TSCGSPHYACPEVIKGEKYDGRK----ADIWSCGVILYALLVGALPFDDDN-LRQLLE---KVKRGV-FHIPH----FIS 225
                       250       260
                ....*....|....*....|....*.
gi 66773086 287 PALR-MFQRLLALEPERRGPAKEVFR 311
Cdd:cd14081 226 PDAQdLLRRMLEVNPEKRITIEEIKK 251
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
53-316 1.45e-36

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: 134.79  E-value: 1.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---------LKNFLREVSITNSLSSSPFIIKVFDVvFETeDC 123
Cdd:cd14093   5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKsseneaeelREATRREIEILRQVSGHPNIIELHDV-FES-PT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQ-EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV- 201
Cdd:cd14093  83 FIFLVfELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL--NVKISDFGFATRLd 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQAGRADGLA-VDTGVDVWAFGVLIFCVLTGNFPWeaasgadaffeefvrWQRGRLPGL-- 277
Cdd:cd14093 161 eGEKLRELCGTPGYLAPEVLKCSMYDNAPgYGKEVDMWACGVIMYTLLAGCPPF---------------WHRKQMVMLrn 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 278 --------PS-QWRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14093 226 imegkyefGSpEWDDISDTAKDLISKLLVVDPKKRLTAEEA---LEHP 270
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
53-309 2.50e-36

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: 133.67  E-value: 2.50e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS---KTKLKNFLREVSITNSLSSsPFIIKVFDVVfETEDCYVFAQE 129
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSqldEENLKKIYREVQIMKMLNH-PHIIKLYQVM-ETKDMLYLVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR--RVGCRVKR 207
Cdd:cd14071  80 YASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL--DANMNIKIADFGFSNffKPGELLKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWEAASGADafFEEFVRWQRGRLPGLPSQwrrFTEP 287
Cdd:cd14071 158 WCGSPPYAAPEVFEGKEYEG----PQLDIWSLGVVLYVLVCGALPFDGSTLQT--LRDRVLSGRFRIPFFMST---DCEH 228
                       250       260
                ....*....|....*....|..
gi 66773086 288 ALRmfqRLLALEPERRGPAKEV 309
Cdd:cd14071 229 LIR---RMLVLDPSKRLTIEQI 247
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
53-311 3.54e-36

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: 133.41  E-value: 3.54e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---TKLKNFLREVSITNSLSSsPFIIKVFDVVfETEDCYVFAQE 129
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnpSSLQKLFREVRIMKILNH-PNIVKLFEVI-ETEKTLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTR--RVGCRVKR 207
Cdd:cd14072  80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL-DADM-NIKIADFGFSNefTPGNKLDT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWEAASGADafFEEFVRWQRGRLPGLPSqwrrfTEp 287
Cdd:cd14072 158 FCGSPPYAAPELFQGKKYDG----PEVDVWSLGVILYTLVSGSLPFDGQNLKE--LRERVLRGKYRIPFYMS-----TD- 225
                       250       260
                ....*....|....*....|....
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14072 226 CENLLKKFLVLNPSKRGTLEQIMK 249
Pkinase pfam00069
Protein kinase domain;
53-315 5.97e-36

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 131.60  E-value: 5.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---TKLKNFLREVSITNSLsSSPFIIKVFDvVFETEDCYVFAQE 129
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKikkKKDKNILREIKILKKL-NHPNIVRLYD-AFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDfmhgrqlvhrdikpenvllfdrecRRVKLADFgmtrrvgCrvkrvs 209
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE------------------------SGSSLTTF-------V------ 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   210 GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPGLPSqwrRFTEPAL 289
Cdd:pfam00069 122 GTPWYMAPEVLG-----GNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIY--ELIIDQPYAFPELPS---NLSEEAK 191
                         250       260
                  ....*....|....*....|....*.
gi 66773086   290 RMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQA---LQH 214
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
53-257 1.15e-35

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: 131.99  E-value: 1.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKG----TGTKMALKFVNK---SKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYV 125
Cdd:cd14002   3 YHVLELIGEGSFGKV----YKGrrkyTGQVVALKFIPKrgkSEKELRNLRQEIEILRKLNH-PNIIEMLDS-FETKKEFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYApAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVGCR- 204
Cdd:cd14002  77 VVTEYA-QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG--GVVKLCDFGFARAMSCNt 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 205 --VKRVSGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd14002 154 lvLTSIKGTPLYMAPELVQEQPYDHTA-----DLWSLGCILYELFVGQPPFYTNS 203
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
59-252 1.22e-35

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: 131.96  E-value: 1.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKS---KTKL-KNFLREVSITNSLSSsPFIIKVFDVVFETEDCYvFAQEYAPAG 134
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhivQTRQqEHIFSEKEILEECNS-PFIVKLYRTFKDKKYLY-MLMEYCLGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRVKRVS--GTI 212
Cdd:cd05572  79 ELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNG--YVKLVDFGFAKKLGSGRKTWTfcGTP 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 66773086 213 PYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd05572 157 EYVAPEIIL-----NKGYDFSVDYWSLGILLYELLTGRPP 191
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
53-303 1.69e-35

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: 131.36  E-value: 1.69e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK----LKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEdeqdMVRIRREIEIMSSLNH-PHIIRIYEV-FENKDKIVIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVGCR--VK 206
Cdd:cd14073  81 EYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL-DQNG-NAKIADFGLSNLYSKDklLQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQAGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWEaasGADafFEEFVRwQRGRlpglpSQWRRFTE 286
Cdd:cd14073 159 TFCGSPLYASPEIVNGTPYQGPEVDC----WSLGVLLYTLVYGTMPFD---GSD--FKRLVK-QISS-----GDYREPTQ 223
                       250
                ....*....|....*....
gi 66773086 287 P--ALRMFQRLLALEPERR 303
Cdd:cd14073 224 PsdASGLIRWMLTVNPKRR 242
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
52-303 2.02e-35

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: 131.22  E-value: 2.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT----KLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYvFA 127
Cdd:cd05578   1 HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCiekdSVRNVLNELEILQELEH-PFLVNLWYSFQDEEDMY-MV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDrECRRVKLADFGMTRRV--GCRV 205
Cdd:cd05578  79 VDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL-D-EQGHVHITDFNIATKLtdGTLA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQAgRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASGADAffEEFVRWQRGRLPGLPSQWrrfT 285
Cdd:cd05578 157 TSTSGTKPYMAPEVFMR-AGYSFA----VDWWSLGVTAYEMLRGKRPYEIHSRTSI--EEIRAKFETASVLYPAGW---S 226
                       250
                ....*....|....*...
gi 66773086 286 EPALRMFQRLLALEPERR 303
Cdd:cd05578 227 EEAIDLINKLLERDPQKR 244
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
53-303 3.09e-35

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: 131.55  E-value: 3.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT-KLK---NFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIiKLKqveHVLNEKRILSEVRH-PFIVNLLGS-FQDDRNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDReCRRVKLADFGMTRRVGCRVKRV 208
Cdd:cd05580  81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL-DS-DGHIKITDFGFAKRVKDRTYTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTGNFPweaasgadaFFEE--FVRWQR---GRL--Pglp 278
Cdd:cd05580 159 CGTPEYLAPEIILSkghGKA--------VDWWALGILIYEMLAGYPP---------FFDEnpMKIYEKileGKIrfP--- 218
                       250       260
                ....*....|....*....|....*
gi 66773086 279 sqwRRFTEPALRMFQRLLALEPERR 303
Cdd:cd05580 219 ---SFFDPDAKDLIKRLLVVDLTKR 240
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
53-266 2.91e-34

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: 128.62  E-value: 2.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS--------KTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCY 124
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgnDFQKLPQLREIDLHRRVSRHPNIITLHDV-FETEVAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDT--VKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcRRVKLADFG--MTRR 200
Cdd:cd13993  81 YIVLEYCPNGDLFEAITENRIYVGKTelIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDE-GTVKLCDFGlaTTEK 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 201 VGCRVKRvsGTIPYTAPEvCQAGRADGLAV-DT-GVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEF 266
Cdd:cd13993 160 ISMDFGV--GSEFYMAPE-CFDEVGRSLKGyPCaAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDY 224
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
53-252 3.62e-34

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: 128.42  E-value: 3.62e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKfvnKSKTKLKNF-----LREVSITNSLSSSPFIIKVFDVVFETEDCY-VF 126
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIK---KMKKKFYSWeecmnLREVKSLRKLNEHPNIVKLKEVFRENDELYfVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aqEYAPaGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCR 204
Cdd:cd07830  78 --EYME-GNLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV--VKIADFGLAREIRSR 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086 205 VkrvsgtiPYT---------APEVcqagradgLAVDTG----VDVWAFGVLIFCVLTGN--FP 252
Cdd:cd07830 153 P-------PYTdyvstrwyrAPEI--------LLRSTSysspVDIWALGCIMAELYTLRplFP 200
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
53-316 1.34e-33

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: 126.20  E-value: 1.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSI---TNSLSSSPFIIKVFDVVFETED---CYVF 126
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLlkhLNDVEGHPNIVKLLDVFEHRGGnhlCLVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aqEYAPAgDLFDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFGMTRRVGCRV 205
Cdd:cd05118  81 --ELMGM-NLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPEN-ILINLELGQLKLADFGLARSFTSPP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVS-GTIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFvrwqrgRLPGlpsqwrrf 284
Cdd:cd05118 157 YTPYvATRWYRAPEVLLGAK----PYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV------RLLG-------- 218
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 285 TEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd05118 219 TPEALDLLSKMLKYDPAKRITASQA---LAHP 247
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
53-303 2.50e-33

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: 126.18  E-value: 2.50e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSsPFIIKVFdVVFETEDCYVFAQ 128
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiikEKKVKYVTIEKEVLSRLAH-PGIVKLY-YTFQDESKLYFVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGmTRRVGC----- 203
Cdd:cd05581  81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILL-DED-MHIKITDFG-TAKVLGpdssp 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 --------------RVKRVS--GTIPYTAPEVCQAGRAdglavDTGVDVWAFGVLIFCVLTGNFPWEAASgadaffeEFV 267
Cdd:cd05581 158 estkgdadsqiaynQARAASfvGTAEYVSPELLNEKPA-----GKSSDLWALGCIIYQMLTGKPPFRGSN-------EYL 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 66773086 268 RWQRgRLPGLPSQWRRFTEPALRMFQRLLALEPERR 303
Cdd:cd05581 226 TFQK-IVKLEYEFPENFPPDAKDLIQKLLVLDPSKR 260
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
52-255 7.79e-33

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: 124.37  E-value: 7.79e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK--TKLKNFL-REVSITNSLSSsPFIIKVFDVVfETEDCYVFAQ 128
Cdd:cd14075   3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKldQKTQRLLsREISSMEKLHH-PNIIRLYEVV-ETLSKLHLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTrrvgCRVKRV 208
Cdd:cd14075  81 EYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNC--VKVGDFGFS----THAKRG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 209 S------GTIPYTAPEVCQagraDGLAVDTGVDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd14075 155 EtlntfcGSPPYAAPELFK----DEHYIGIYVDIWALGVLLYFMVTGVMPFRA 203
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
53-311 1.22e-32

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: 123.68  E-value: 1.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK--TKLKN-FLREVSITNSLSSsPFIIKVFDVVFETEDCYVFaQE 129
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRmsRKMREeAIDEARVLSKLNS-PYVIKYYDSFVDKGKLNIV-ME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCR--- 204
Cdd:cd08529  80 YAENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL--DKGDNVKIGDLGVAKILSDTtnf 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAAS-GAdaffeEFVRWQRGRLPGLPSQwrr 283
Cdd:cd08529 158 AQTIVGTPYYLSPELCE-----DKPYNEKSDVWALGCVLYELCTGKHPFEAQNqGA-----LILKIVRGKYPPISAS--- 224
                       250       260
                ....*....|....*....|....*...
gi 66773086 284 FTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd08529 225 YSQDLSQLIDSCLTKDYRQRPDTTELLR 252
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
53-315 1.28e-32

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: 124.86  E-value: 1.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVY-KGTGTKMALKFVNK--------SKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDC 123
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAIKVVRKadlssdnlKGSSRANILKEVQIMKRLSH-PNIVKLLDF-QESDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDR------------------ 185
Cdd:cd14096  81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPEN-LLFEPipfipsivklrkadddet 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 186 --------------ECRRVKLADFGMTRRV-GCRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGn 250
Cdd:cd14096 160 kvdegefipgvgggGIGIVKLADFGLSKQVwDSNTKTPCGTVGYTAPEVVKDER-----YSKKVDMWALGCVLYTLLCG- 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 251 FPweaasgadAFFEEFV-----RWQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEvfrFLKH 315
Cdd:cd14096 234 FP--------PFYDESIetlteKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDE---FLAH 292
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
52-308 6.76e-32

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: 121.93  E-value: 6.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKF--VNKSKTKLKNFLREVSItNSLSSSPFIIKVFDVVFETEDCYVfAQE 129
Cdd:cd06623   2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLRELKT-LRSCESPYVVKCYGAFYKEGEISI-VLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHG-RQLVHRDIKPENVLLFDRECrrVKLADFG----MTRRVGCR 204
Cdd:cd06623  80 YMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGE--VKIADFGiskvLENTLDQC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVsGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADaFFEEFVRWQRGRLPGLPSQwrrF 284
Cdd:cd06623 158 NTFV-GTVTYMSPE-----RIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPS-FFELMQAICDGPPPSLPAE---E 227
                       250       260
                ....*....|....*....|....*
gi 66773086 285 TEPALRMF-QRLLALEPERRGPAKE 308
Cdd:cd06623 228 FSPEFRDFiSACLQKDPKKRPSAAE 252
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
52-315 1.04e-31

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: 121.19  E-value: 1.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGkvdlVVYKGT----GTKMALKFVNKSKTKLKNFLR-------EVSITNSLSSS--PFIIKVFDVvF 118
Cdd:cd14005   1 QYEVGDLLGKGGFG----TVYSGVrirdGLPVAVKFVPKSRVTEWAMINgpvpvplEIALLLKASKPgvPGVIRLLDW-Y 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVFAQEY-APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGM 197
Cdd:cd14005  76 ERPDGFLLIMERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI-NLRTGEVKLIDFGC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCRVKR-VSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEaasgadaFFEEFVRWQrgrlpg 276
Cdd:cd14005 155 GALLKDSVYTdFDGTRVYSPPEWIRHGRYHGRP----ATVWSLGILLYDMLCGDIPFE-------NDEQILRGN------ 217
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 66773086 277 lPSQWRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd14005 218 -VLFRPRLSKECCDLISRCLQFDPSKRPSLEQI---LSH 252
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
59-303 3.33e-31

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: 119.63  E-value: 3.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGkvdlVVYKG----TGTKMALKFVNKSK--TKLK-NFLREVSITNSLSSsPFIIKVFDVVfETEDCYVFAQEYA 131
Cdd:cd14009   1 IGRGSFA----TVWKGrhkqTGEVVAIKEISRKKlnKKLQeNLESEIAILKSIKH-PNIVRLYDVQ-KTEDFIYLVLEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECR-RVKLADFGMTR--RVGCRVKRV 208
Cdd:cd14009  75 AGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDpVLKIADFGFARslQPASMAETL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASgadaFFEEFVRWQRGRLPgLPSQWRRFTEPA 288
Cdd:cd14009 155 CGSPLYMAPEILQFQKYDAKA-----DLWSVGAILFEMLVGKPPFRGSN----HVQLLRNIERSDAV-IPFPIAAQLSPD 224
                       250
                ....*....|....*.
gi 66773086 289 LR-MFQRLLALEPERR 303
Cdd:cd14009 225 CKdLLRRLLRRDPAER 240
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
59-281 8.51e-31

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: 118.41  E-value: 8.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT--GTKMA---LKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYAPA 133
Cdd:cd13999   1 IGSGSFGEV----YKGKwrGTDVAikkLKVEDDNDELLKEFRREVSILSKLRH-PNIVQFIGACLSPPPLCIVT-EYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDII-PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV---GCRVKRVS 209
Cdd:cd13999  75 GSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT--VKIADFGLSRIKnstTEKMTGVV 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 210 GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEfvrWQRGRLPGLPSQW 281
Cdd:cd13999 153 GTPRWMAPEVLR-----GEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAV---VQKGLRPPIPPDC 216
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
51-309 9.99e-31

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: 118.52  E-value: 9.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KH-YELVRELGKGTYGKVDLVVyKGTGTKMALKFVNKSKTK----LKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYV 125
Cdd:cd14161   2 KHrYEFLETLGKGTYGRVKKAR-DSSGRLVAIKSIRKDRIKdeqdLLHIRREIEIMSSLNH-PHIISVYEV-FENSSKIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR--RVGC 203
Cdd:cd14161  79 IVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL--DANGNIKIADFGLSNlyNQDK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQAGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWEaasGADafFEEFVRWQRG---RLPGLPSQ 280
Cdd:cd14161 157 FLQTYCGSPLYASPEIVNGRPYIGPEVDS----WSLGVLLYILVHGTMPFD---GHD--YKILVKQISSgayREPTKPSD 227
                       250       260
                ....*....|....*....|....*....
gi 66773086 281 wrrftepALRMFQRLLALEPERRGPAKEV 309
Cdd:cd14161 228 -------ACGLIRWLLMVNPERRATLEDV 249
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
61-311 1.26e-30

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: 118.86  E-value: 1.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  61 KGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITN---SLSSSPFIIKVFdVVFETEDCYVFAQEYAPAGDLF 137
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERnilSQAQNPFVVKLY-YSFQGKKNLYLVMEYLPGGDLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DIIPpQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDREcRRVKLADFGMTrRVGC------------- 203
Cdd:cd05579  82 SLLE-NVGaLDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDN-ILIDAN-GHLKLTDFGLS-KVGLvrrqiklsiqkks 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 ------RVKRVSGTIPYTAPEVCQaGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASgADAFFEEFVrwqRGRLPgl 277
Cdd:cd05579 158 ngapekEDRRIVGTPDYLAPEILL-GQGHGKT----VDWWSLGVILYEFLVGIPPFHAET-PEEIFQNIL---NGKIE-- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 278 psqWRRFTEP---ALRMFQRLLALEPERR---GPAKEVFR 311
Cdd:cd05579 227 ---WPEDPEVsdeAKDLISKLLTPDPEKRlgaKGIEEIKN 263
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
57-306 2.60e-30

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: 117.72  E-value: 2.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK---NFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAPA 133
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcraEILHEIAVLELAKSNPRVVNLHEV-YETTSEIILILEYAAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD-RECRRVKLADFGMTRRVG--CRVKRV 208
Cdd:cd14198  93 GEIFNLCVPDLAemVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiYPLGDIKIVDFGMSRKIGhaCELREI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWeaaSGADAfFEEFVRWQRGRLPGLPSQWRRFTEPA 288
Cdd:cd14198 173 MGTPEYLAPEILNYD-----PITTATDMWNIGVIAYMLLTHESPF---VGEDN-QETFLNISQVNVDYSEETFSSVSQLA 243
                       250
                ....*....|....*...
gi 66773086 289 LRMFQRLLALEPERRGPA 306
Cdd:cd14198 244 TDFIQKLLVKNPEKRPTA 261
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
49-308 3.08e-30

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: 117.48  E-value: 3.08e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK--TKLKNFLREVSITNSLSSsPFIIKVFDVVfETEDCYVF 126
Cdd:cd14078   1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgDDLPRVKTEIEALKNLSH-QHICRLYHVI-ETDNKIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDREcRRVKLADFGMTRR----VG 202
Cdd:cd14078  79 VLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPEN-LLLDED-QNLKLIDFGLCAKpkggMD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWEaasgADAFFEEFVRWQRGRLPgLPSqWr 282
Cdd:cd14078 157 HHLETCCGSPAYAAPELIQGKPYIG----SEADVWSMGVLLYALLCGFLPFD----DDNVMALYRKIQSGKYE-EPE-W- 225
                       250       260
                ....*....|....*....|....*.
gi 66773086 283 rFTEPALRMFQRLLALEPERRGPAKE 308
Cdd:cd14078 226 -LSPSSKLLLDQMLQVDPKKRITVKE 250
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
53-254 3.18e-30

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: 117.55  E-value: 3.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----------------KSKTKLKNFLREVSITnSLSSSPFIIKVFDV 116
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglkkerekrleKEISRDIRTIREAALS-SLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 117 VFeTEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFG 196
Cdd:cd14077  82 LR-TPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILI--SKSGNIKIIDFG 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTR--RVGCRVKRVSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14077 159 LSNlyDPRRLLRTFCGSLYFAAPELLQAQPYTG----PEVDVWSFGVVLYVLVCGKVPFD 214
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
48-253 1.16e-29

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: 116.27  E-value: 1.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK-------LKNFLREVSITNSLSSsPFIIKVFDVvFET 120
Cdd:cd14194   2 NVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKssrrgvsREDIEREVSILKEIQH-PNVITLHEV-YEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREC--RRVKLADFGMT 198
Cdd:cd14194  80 KTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkPRIKIIDFGLA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRV--GCRVKRVSGTIPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14194 160 HKIdfGNEFKNIFGTPEFVAPEIVN---YEPLGLEA--DMWSIGVITYILLSGASPF 211
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
51-303 1.49e-29

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: 116.95  E-value: 1.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITnSLSSSPFIIKVFdVVFETEDCYVF 126
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEemikRNKVKRVLTEREIL-ATLDHPFLPTLY-ASFQTSTHLCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCR 204
Cdd:cd05574  79 VMDYCPGGELFRLLQKQPGkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILL--HESGHIMLTDFDLSKQSSVT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVS--------------------------------GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd05574 157 PPPVRkslrkgsrrssvksieketfvaepsarsnsfvGTEEYIAPEVIK-----GDGHGSAVDWWTLGILLYEMLYGTTP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 253 WEAASgADAFFEEFVRwQRGRLPGLPsqwrRFTEPALRMFQRLLALEPERR 303
Cdd:cd05574 232 FKGSN-RDETFSNILK-KELTFPESP----PVSSEAKDLIRKLLVKDPSKR 276
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
51-257 1.62e-29

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: 115.34  E-value: 1.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS---KTKLKN-FLREVSITNSLSSsPFIIKvFDVVFETEDCYVF 126
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltKPKQREkLKSEIKIHRSLKH-PNIVK-FHDCFEDEENVYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV---GC 203
Cdd:cd14099  79 LLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL-DEN-MNVKIGDFGLAARLeydGE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 204 RVKRVSGTIPYTAPEVCQAGRADGLavdtGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd14099 157 RKKTLCGTPNYIAPEVLEKKKGHSF----EVDIWSLGVILYTLLVGKPPFETSD 206
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
51-309 4.36e-29

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: 114.57  E-value: 4.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---TKLKNFLREVSITNSLSSSPFIikVFDVVFETEDCYVFA 127
Cdd:cd14097   1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKagsSAVKLLEREVDILKHVNHAHII--HLEEVFETPKRMYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVL----LFDRECR-RVKLADFGMTRRVG 202
Cdd:cd14097  79 MELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNDKlNIKVTDFGLSVQKY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CR----VKRVSGTIPYTAPEVcqagrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASgADAFFEEFvrwQRGRLPGLP 278
Cdd:cd14097 159 GLgedmLQETCGTPIYMAPEV-----ISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKS-EEKLFEEI---RKGDLTFTQ 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 66773086 279 SQWRRFTEPALRMFQRLLALEPERRGPAKEV 309
Cdd:cd14097 230 SVWQSVSDAAKNVLQQLLKVDPAHRMTASEL 260
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
51-254 5.82e-29

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: 114.11  E-value: 5.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---LKNFL-REVSITNSLSSsPFIIKVFDVvFETEDCYVF 126
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPddfVEKFLpRELEILARLNH-KSIIKTYEI-FETSDGKVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 -AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRV---- 201
Cdd:cd14165  79 iVMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL-DKDF-NIKLTDFGFSKRClrde 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 202 -GCRV--KRVSGTIPYTAPEVCQagradGLAVDTGV-DVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14165 157 nGRIVlsKTFCGSAAYAAPEVLQ-----GIPYDPRIyDIWSLGVILYIMVCGSMPYD 208
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
52-243 6.35e-29

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: 113.45  E-value: 6.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINlESKEKKESILNEIAILKKCKH-PNIVKYYGSYLKKDELWI-VMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV--GCRVKR 207
Cdd:cd05122  79 CSGGSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG--EVKLIDFGLSAQLsdGKTRNT 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 66773086 208 VSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLI 243
Cdd:cd05122 157 FVGTPYWMAPEVIQ-----GKPYGFKADIWSLGITA 187
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
53-256 6.79e-29

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: 113.66  E-value: 6.79e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKtklknfLREVSITN--------SLSSSPFIIKVFDVVfETEDCY 124
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTK------LDDVSKAHlfqevrcmKLVQHPNVVRLYEVI-DTQTKL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFD-IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcRRVKLADFGMTRRV-- 201
Cdd:cd14074  78 YLILELGDGGDMYDyIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ-GLVKLTDFGFSNKFqp 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAA 256
Cdd:cd14074 157 GEKLETSCGSLAYSAPEILLGDEYDAPA----VDIWSLGVILYMLVCGQPPFQEA 207
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
53-303 7.07e-29

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: 113.64  E-value: 7.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN---KSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQE 129
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNlgsLSQKEREDSVNEIRLLASVNH-PNIIRYKEAFLDGNRLCI-VME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVG----LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-GCR 204
Cdd:cd08530  80 YAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGD--LVKIGDLGISKVLkKNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAffeeFVRWQRGRLPGLPSqwrRF 284
Cdd:cd08530 158 AKTQIGTPLYAAPEVWK-----GRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQEL----RYKVCRGKFPPIPP---VY 225
                       250
                ....*....|....*....
gi 66773086 285 TEPALRMFQRLLALEPERR 303
Cdd:cd08530 226 SQDLQQIIRSLLQVNPKKR 244
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
54-308 1.26e-28

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: 113.21  E-value: 1.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALKFV--NKSKTKLKNFLREVSITNSlSSSPFIIKVFDVVFETEDCYVfAQEYA 131
Cdd:cd06605   4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIrlEIDEALQKQILRELDVLHK-CNSPYIVGFYGAFYSEGDISI-CMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMH-GRQLVHRDIKPENVLLFDREcrRVKLADFGM-TRRVGCRVKRVS 209
Cdd:cd06605  82 DGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRG--QVKLCDFGVsGQLVDSLAKTFV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 GTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPW--EAASGADAFFEEFVRWQRGRLPGLPSQwrRFTEP 287
Cdd:cd06605 160 GTRSYMAPE-----RISGGKYTVKSDIWSLGLSLVELATGRFPYppPNAKPSMMIFELLSYIVDEPPPLLPSG--KFSPD 232
                       250       260
                ....*....|....*....|.
gi 66773086 288 ALRMFQRLLALEPERRGPAKE 308
Cdd:cd06605 233 FQDFVSQCLQKDPTERPSYKE 253
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
47-275 1.54e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 113.03  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   47 SDVTKHYELVRELG--KGTYGKVDLVVYKGTGtKMalkFVNKS-KTKLKNFLrEVSITNSLSSSPFIIKVFDVVFeTEDC 123
Cdd:PHA03390  10 VQFLKNCEIVKKLKliDGKFGKVSVLKHKPTQ-KL---FVQKIiKAKNFNAI-EPMVHQLMKDNPNFIKLYYSVT-TLKG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVlLFDRECRRVKLADFGMTRRVG- 202
Cdd:PHA03390  84 HVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENV-LYDRAKDRIYLCDYGLCKIIGt 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086  203 --CRvkrvSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLP 275
Cdd:PHA03390 163 psCY----DGTLDYFSPE-----KIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLP 228
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
53-310 1.60e-28

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: 112.82  E-value: 1.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL--REVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd14184   3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLieNEVSILRRVKH-PNIIMLIEEMDTPAELYL-VMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL--FDRECRRVKLADFGMTRRVGCRVKRV 208
Cdd:cd14184  81 VKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceYPDGTKSLKLGDFGLATVVEGPLYTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVCqAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASG-ADAFFEEFVrwqRGRLPGLPSQWRRFTEP 287
Cdd:cd14184 161 CGTPTYVAPEII-AETGYGLK----VDIWAAGVITYILLCGFPPFRSENNlQEDLFDQIL---LGKLEFPSPYWDNITDS 232
                       250       260
                ....*....|....*....|...
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVF 310
Cdd:cd14184 233 AKELISHMLQVNVEARYTAEQIL 255
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
57-315 1.66e-28

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: 113.11  E-value: 1.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK---NFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAPA 133
Cdd:cd14197  15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmEIIHEIAVLELAQANPWVINLHEV-YETASEMILVLEYAAG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFD--IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLF-DRECRRVKLADFGMTRRVGC--RVKRV 208
Cdd:cd14197  94 GEIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTsESPLGDIKIVDFGLSRILKNseELREI 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEaasgADAFFEEFVRWQRGRLPGLPSQWRRFTEPA 288
Cdd:cd14197 174 MGTPEYVAPEILSYE-----PISTATDMWSIGVLAYVMLTGISPFL----GDDKQETFLNISQMNVSYSEEEFEHLSESA 244
                       250       260
                ....*....|....*....|....*..
gi 66773086 289 LRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd14197 245 IDFIKTLLIKKPENRATAEDC---LKH 268
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
47-311 2.02e-28

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: 112.58  E-value: 2.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  47 SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL-------KNFLREVSITNSLSSsPFIIKVFDVvFE 119
Cdd:cd14105   1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsrrgvsrEDIEREVSILRQVLH-PNIITLHDV-FE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 TEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREC--RRVKLADFGM 197
Cdd:cd14105  79 NKTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiPRIKLIDFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRV--GCRVKRVSGTIPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPWEaasgADAFFEEFVRWQRGRLP 275
Cdd:cd14105 159 AHKIedGNEFKNIFGTPEFVAPEIVN---YEPLGLEA--DMWSIGVITYILLSGASPFL----GDTKQETLANITAVNYD 229
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 66773086 276 GLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14105 230 FDDEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLR 265
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
53-316 2.15e-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: 113.11  E-value: 2.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKtklKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQEYAP 132
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSK---RDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYL-VTELLR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECR--RVKLADFG------------MT 198
Cdd:cd14091  78 GGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeSLRICDFGfakqlraengllMT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RrvgCRvkrvsgTIPYTAPEVCqagRADGLavDTGVDVWAFGVLIFCVLTGNFPWeaASGADAFFEEFV-RWQRGRLPGL 277
Cdd:cd14091 158 P---CY------TANFVAPEVL---KKQGY--DAACDIWSLGVLLYTMLAGYTPF--ASGPNDTPEVILaRIGSGKIDLS 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 66773086 278 PSQWRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14091 222 GGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQV---LQHP 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
53-315 2.69e-28

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: 112.58  E-value: 2.69e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKfvnksKTKLKNF--------LREVSITNSLSSsPFIIKVFDVVFET 120
Cdd:cd07829   1 YEKLEKLGEGTYG----VVYKAkdkkTGEIVALK-----KIRLDNEeegipstaLREISLLKELKH-PNIVKLLDVIHTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCY-VFaqEYApAGDLFDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMT 198
Cdd:cd07829  71 NKLYlVF--EYC-DQDLKKYLDkRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLI-NRDG-VLKLADFGLA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRVGCRVKR---VSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGvlifCV----LTGN--FP----------------- 252
Cdd:cd07829 146 RAFGIPLRTythEVVTLWYRAPEILLGSKHYS----TAVDIWSVG----CIfaelITGKplFPgdseidqlfkifqilgt 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 253 -----WEAASGADAFFEEFVRWQRGRLPG-LPsqwrRFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd07829 218 pteesWPGVTKLPDYKPTFPKWPKNDLEKvLP----RLDPEGIDLLSKMLQYNPAKRISAKEA---LKH 279
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
59-303 4.09e-28

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: 111.23  E-value: 4.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGkvdlVVYKG---TGTK--MALKFVNKS---KTKLKNFLREVSITNSLSSsPFIIKVFDvvFETEDCYVF-AQE 129
Cdd:cd14121   3 LGSGTYA----TVYKAyrkSGARevVAVKCVSKSslnKASTENLLTEIELLKKLKH-PHIVELKD--FQWDEEHIYlIME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKRVS 209
Cdd:cd14121  76 YCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 --GTIPYTAPE-VCQAgradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASgadafFEEFV-RWQRGRLPGLPSQWRrfT 285
Cdd:cd14121 156 lrGSPLYMAPEmILKK------KYDARVDLWSVGVILYECLFGRAPFASRS-----FEELEeKIRSSKPIEIPTRPE--L 222
                       250
                ....*....|....*....
gi 66773086 286 EPALR-MFQRLLALEPERR 303
Cdd:cd14121 223 SADCRdLLLRLLQRDPDRR 241
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
52-253 5.11e-28

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: 111.14  E-value: 5.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLR-EVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:cd14114   3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRkEIQIMNQLHH-PKLINLHDA-FEDDNEMVLILEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQ-VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCR--VKR 207
Cdd:cd14114  81 LSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKesVKV 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 208 VSGTIPYTAPEVcqagrADGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14114 161 TTGTAEFAAPEI-----VEREPVGFYTDMWAVGVLSYVLLSGLSPF 201
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
53-303 6.86e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 112.60  E-value: 6.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT-KLK---NFLREVSITNSLSSsPFIIKVFdVVFETEDCYVFAQ 128
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlKMKqvqHVAQEKSILMELSH-PFIVNMM-CSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVGCRVKRV 208
Cdd:PTZ00263  98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL-DNK-GHVKVTDFGFAKKVPDRTFTL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  209 SGTIPYTAPEVCQAgRADGLAVDTgvdvWAFGVLIFCVLTGNFPweaasgadaFFEE--FVRWQR---GRLPgLPSqWrr 283
Cdd:PTZ00263 176 CGTPEYLAPEVIQS-KGHGKAVDW----WTMGVLLYEFIAGYPP---------FFDDtpFRIYEKilaGRLK-FPN-W-- 237
                        250       260
                 ....*....|....*....|
gi 66773086  284 FTEPALRMFQRLLALEPERR 303
Cdd:PTZ00263 238 FDGRARDLVKGLLQTDHTKR 257
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
59-249 9.16e-28

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 110.39  E-value: 9.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK-NFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAPAGDLF 137
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDReDVRNEIEIMNQLRH-PRLLQLYDA-FETPREMVLVMEYVAGGELF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 D-IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVK-RVS-GTIPY 214
Cdd:cd14103  79 ErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDPDKKlKVLfGTPEF 158
                       170       180       190
                ....*....|....*....|....*....|....*
gi 66773086 215 TAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd14103 159 VAPEVVNYE-----PISYATDMWSVGVICYVLLSG 188
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-254 1.17e-27

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: 110.24  E-value: 1.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKvFDVVFETEDCYVFAQEYAP 132
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRH-PNIIR-FKEVVLTPTHLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRR--VGCRVKRVSG 210
Cdd:cd14662  80 GGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSsvLHSQPKSTVG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 66773086 211 TIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14662 160 TPAYIAPEVLSRKEYDGKV----ADVWSCGVTLYVMLVGAYPFE 199
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
59-311 1.80e-27

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: 109.80  E-value: 1.80e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVN------KSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYAP 132
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKEVSlvdddkKSRESVKQLEQEIALLSKLRH-PNIVQYYGTEREEDNLYIFL-EYVP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVG--CRVKRVSG 210
Cdd:cd06632  86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV-DTN-GVVKLADFGMAKHVEafSFAKSFKG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVC-QAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFvrwQRGRLPGLPSQwrrfTEPAL 289
Cdd:cd06632 164 SPYWMAPEVImQKNSGYGLA----VDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIG---NSGELPPIPDH----LSPDA 232
                       250       260
                ....*....|....*....|...
gi 66773086 290 RMFQRL-LALEPERRGPAKEVFR 311
Cdd:cd06632 233 KDFIRLcLQRDPEDRPTASQLLE 255
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
53-255 1.82e-27

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: 110.57  E-value: 1.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK-TKLKNF---LREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQ 128
Cdd:cd14209   3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKvVKLKQVehtLNEKRILQAINF-PFLVKLEYSFKDNSNLYM-VM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRVKRV 208
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQG--YIKVTDFGFAKRVKGRTWTL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 209 SGTIPYTAPEVCQAgRADGLAVDTgvdvWAFGVLIFCVLTGNFPWEA 255
Cdd:cd14209 159 CGTPEYLAPEIILS-KGYNKAVDW----WALGVLIYEMAAGYPPFFA 200
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
53-253 3.62e-27

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: 109.01  E-value: 3.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT---------KLKNFLREVSITNSL--SSSPFIIKVFDVvFETE 121
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvdtwvrdrKLGTVPLEIHILDTLnkRSHPNIVKLLDF-FEDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFAQE-YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTrr 200
Cdd:cd14004  81 EFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT--IKLIDFGSA-- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 201 vgCRVKR-----VSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14004 157 --AYIKSgpfdtFVGTIDYAAPEVLRGNPYGG----KEQDIWALGVLLYTLVFKENPF 208
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-328 3.72e-27

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 109.82  E-value: 3.72e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL---REVSITNSLSSsPFIIKVFDVvFETEDCYVFAQE 129
Cdd:cd14086   3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQkleREARICRLLKH-PNIVRLHDS-ISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRE-CRRVKLADFGMTRRVGCRVKR- 207
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSkGAAVKLADFGLAIEVQGDQQAw 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 --VSGTIPYTAPEVCqagRADglAVDTGVDVWAFGVLIFCVLTGNFPweaasgadaFFEE-----FVRWQRGRLPGLPSQ 280
Cdd:cd14086 161 fgFAGTPGYLSPEVL---RKD--PYGKPVDIWACGVILYILLVGYPP---------FWDEdqhrlYAQIKAGAYDYPSPE 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 281 WRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHELTSELRRRPS--HR 328
Cdd:cd14086 227 WDTVTPEAKDLINQMLTVNPAKRITAAEA---LKHPWICQRDRVASmvHR 273
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
51-303 3.78e-27

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: 110.08  E-value: 3.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYEL-VRE--LGKGTYGKVDLVVYKGTGTKMALKFVnkskTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFA 127
Cdd:cd14092   3 QNYELdLREeaLGDGSFSVCRKCVHKKTGQEFAVKIV----SRRLDTSREVQLLRLCQGHPNIVKLHEV-FQDELHTYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLF--DRECRRVKLADFGMTR-RVGCR 204
Cdd:cd14092  78 MELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPEN-LLFtdEDDDAEIKIVDFGFARlKPENQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSG-TIPYTAPEVC-QAGRADGLavDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWR 282
Cdd:cd14092 157 PLKTPCfTLPYAAPEVLkQALSTQGY--DESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKSGDFSFDGEEWK 234
                       250       260
                ....*....|....*....|.
gi 66773086 283 RFTEPALRMFQRLLALEPERR 303
Cdd:cd14092 235 NVSSEAKSLIQGLLTVDPSKR 255
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
45-311 9.79e-27

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: 108.13  E-value: 9.79e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  45 AASDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL---------KNFLREVSITNSLSSSPFIIKVFD 115
Cdd:cd14181   4 GAKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLspeqleevrSSTLKEIHILRQVSGHPSIITLID 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 116 VvFETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDreCRRVKLADF 195
Cdd:cd14181  84 S-YESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDD--QLHIKLSDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 196 GMTRRV--GCRVKRVSGTIPYTAPEVCQAGRAD---GLAVDtgVDVWAFGVLIFCVLTGNFPWeaasgadaffeefvrWQ 270
Cdd:cd14181 161 GFSCHLepGEKLRELCGTPGYLAPEILKCSMDEthpGYGKE--VDLWACGVILFTLLAGSPPF---------------WH 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 271 R-----------GRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14181 224 RrqmlmlrmimeGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQ 275
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
70-303 1.30e-26

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: 107.45  E-value: 1.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  70 VVYKGTGTK-----MALKFVNKSK-TKLKNFL-REVSITNSLSSSPfIIKVFDVVfETEDCYVFAQEYAPAGDLFDIIPP 142
Cdd:cd14120   8 VVFKGRHRKkpdlpVAIKCITKKNlSKSQNLLgKEIKILKELSHEN-VVALLDCQ-ETSSSVYLVMEYCNGGDLADYLQA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 143 QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECR------RVKLADFGMTRRV--GCRVKRVSGTIP 213
Cdd:cd14120  86 KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLsHNSGRKpspndiRLKIADFGFARFLqdGMMAATLCGSPM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 214 YTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASGAD--AFFEEfvrwQRGRLPGLPSQwrrfTEPALR- 290
Cdd:cd14120 166 YMAPEVIMSLQYDAKA-----DLWSIGTIVYQCLTGKAPFQAQTPQElkAFYEK----NANLRPNIPSG----TSPALKd 232
                       250
                ....*....|...
gi 66773086 291 MFQRLLALEPERR 303
Cdd:cd14120 233 LLLGLLKRNPKDR 245
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
53-298 1.91e-26

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: 107.40  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRE--LGKGTYGkvdlVVYKGT-----GTKMALKFVNKSK-TKLKNFL-REVSITNSLSSSPfIIKVFDVVfETEDC 123
Cdd:cd14202   2 FEFSRKdlIGHGAFA----VVFKGRhkekhDLEVAVKCINKKNlAKSQTLLgKEIKILKELKHEN-IVALYDFQ-EIANS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECR-------RVKLADFG 196
Cdd:cd14202  76 VYLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRksnpnniRIKIADFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRV--GCRVKRVSGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASGADafFEEFVRWQRGRL 274
Cdd:cd14202 156 FARYLqnNMMAATLCGSPMYMAPEVIMSQHYDAKA-----DLWSIGTIIYQCLTGKAPFQASSPQD--LRLFYEKNKSLS 228
                       250       260
                ....*....|....*....|....
gi 66773086 275 PGLPsqwrRFTEPALRmfQRLLAL 298
Cdd:cd14202 229 PNIP----RETSSHLR--QLLLGL 246
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
59-309 2.07e-26

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: 108.55  E-value: 2.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSlSSSPFiIKVFDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKILRKeviiAKDEVAHTVTESRVLQN-TRHPF-LTALKYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR---VGCRVKRVSGT 211
Cdd:cd05595  81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML-DKD-GHIKITDFGLCKEgitDGATMKTFCGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IPYTAPEVCQ---AGRAdglavdtgVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPglpsqwRRFTEPA 288
Cdd:cd05595 159 PEYLAPEVLEdndYGRA--------VDWWGLGVVMYEMMCGRLPFYNQDHERLF--ELILMEEIRFP------RTLSPEA 222
                       250       260
                ....*....|....*....|....*.
gi 66773086 289 LRMFQRLLALEPERR---GP--AKEV 309
Cdd:cd05595 223 KSLLAGLLKKDPKQRlggGPsdAKEV 248
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
47-303 2.40e-26

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: 107.01  E-value: 2.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  47 SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK-------TKLKNFLREVSITNSLSSsPFIIKVFDVvFE 119
Cdd:cd14195   1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRlsssrrgVSREEIEREVNILREIQH-PNIITLHDI-FE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 TEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREC--RRVKLADFGM 197
Cdd:cd14195  79 NKTDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnPRIKLIDFGI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRV--GCRVKRVSGTIPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPWEAASGADA----------FFEE 265
Cdd:cd14195 159 AHKIeaGNEFKNIFGTPEFVAPEIVN---YEPLGLEA--DMWSIGVITYILLSGASPFLGETKQETltnisavnydFDEE 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 266 FvrwqrgrlpglpsqWRRFTEPALRMFQRLLALEPERR 303
Cdd:cd14195 234 Y--------------FSNTSELAKDFIRRLLVKDPKKR 257
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
53-316 2.63e-26

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: 106.99  E-value: 2.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKfvnksKTKLKN--------FLREVSITNSLSSsPFIIKVFDVVFET 120
Cdd:cd07835   1 YQKLEKIGEGTYG----VVYKArdklTGEIVALK-----KIRLETedegvpstAIREISLLKELNH-PNIVRLLDVVHSE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCY-VFaqEYAPAgDL---FDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDREcRRVKLADFG 196
Cdd:cd07835  71 NKLYlVF--EFLDL-DLkkyMDSSPLT-GLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQN-LLIDTE-GALKLADFG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCRVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVL----------------------IFCVL--TG 249
Cdd:cd07835 145 LARAFGVPVRTYTHevvTLWYRAPEILLGSK----HYSTPVDIWSVGCIfaemvtrrplfpgdseidqlfrIFRTLgtPD 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 250 NFPWEAASGADAFFEEFVRWQRGRLPGL-PSqwrrFTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd07835 221 EDVWPGVTSLPDYKPTFPKWARQDLSKVvPS----LDEDGLDLLSQMLVYDPAKRISAKAA---LQHP 281
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-303 2.81e-26

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: 107.22  E-value: 2.81e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKlKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDK-KIVRTEIGVLLRLSH-PNIIKLKEI-FETPTEISLVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD-RECRRVKLADFGMTRRVGCRV-- 205
Cdd:cd14085  78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpAPDAPLKIADFGLSKIVDQQVtm 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQrgrLPGLPSQWRRFT 285
Cdd:cd14085 158 KTVCGTPGYCAPEILR-----GCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCD---YDFVSPWWDDVS 229
                       250
                ....*....|....*...
gi 66773086 286 EPALRMFQRLLALEPERR 303
Cdd:cd14085 230 LNAKDLVKKLIVLDPKKR 247
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
59-303 3.70e-26

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: 107.47  E-value: 3.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQEYAPAG 134
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKALKKDvvleDDDVECTMIERRVLALASQHPFLTHLF-CTFQTESHLFFVMEYLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVGCRVKRVS---GT 211
Cdd:cd05592  82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL-DRE-GHIKIADFGMCKENIYGENKAStfcGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEaASGADAFFEEFVRWQrgrlPGLPsqwRRFTEPALRM 291
Cdd:cd05592 160 PDYIAPEILK-----GQKYNQSVDWWSFGVLLYEMLIGQSPFH-GEDEDELFWSICNDT----PHYP---RWLTKEAASC 226
                       250
                ....*....|..
gi 66773086 292 FQRLLALEPERR 303
Cdd:cd05592 227 LSLLLERNPEKR 238
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
53-254 4.46e-26

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: 105.84  E-value: 4.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---LKNFL-REVSITNSLSSSPfIIKVFDVVFETEDCYVFAQ 128
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPeefIQRFLpRELQIVERLDHKN-IIHVYEMLESADGKIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdrECRRVKLADFGMTRRVGCRVKRV 208
Cdd:cd14163  81 ELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL---QGFTLKLTDFGFAKQLPKGGREL 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 209 S----GTIPYTAPEVCQagradGLAVDTGV-DVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14163 158 SqtfcGSTAYAAPEVLQ-----GVPHDSRKgDIWSMGVVLYVMLCAQLPFD 203
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
47-310 5.16e-26

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: 106.23  E-value: 5.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  47 SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL--REVSITNSLSSSPFIIKVFDVVFETEdcY 124
Cdd:cd14183   2 ASISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMiqNEVSILRRVKHPNIVLLIEEMDMPTE--L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRE--CRRVKLADFGMTRRVG 202
Cdd:cd14183  80 YLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgSKSLKLGDFGLATVVD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSGTIPYTAPEVCqAGRADGLAvdtgVDVWAFGVLIFCVLTGnFPWEAASGAD--AFFEEFVrwqRGRLPGLPSQ 280
Cdd:cd14183 160 GPLYTVCGTPTYVAPEII-AETGYGLK----VDIWAAGVITYILLCG-FPPFRGSGDDqeVLFDQIL---MGQVDFPSPY 230
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 281 WRRFTEPALRMFQRLLALEPERRGPAKEVF 310
Cdd:cd14183 231 WDNVSDSAKELITMMLQVDVDQRYSALQVL 260
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-303 6.26e-26

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 105.94  E-value: 6.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKG---TGTKMALK------FVNKSKTkLKNFLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQE 129
Cdd:cd05583   2 LGTGAYGKVFLVRKVGghdAGKLYAMKvlkkatIVQKAKT-AEHTMTERQVLEAVRQSPFLVTLH-YAFQTDAKLHLILD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV----GCRV 205
Cdd:cd05583  80 YVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL-DSE-GHVVLTDFGLSKEFlpgeNDRA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQAGRAdglAVDTGVDVWAFGVLIFCVLTGNFPWeAASGADAFFEEFVRWQRGRLPGLPsqwRRFT 285
Cdd:cd05583 158 YSFCGTIEYMAPEVVRGGSD---GHDKAVDWWSLGVLTYELLTGASPF-TVDGERNSQSEISKRILKSHPPIP---KTFS 230
                       250
                ....*....|....*...
gi 66773086 286 EPALRMFQRLLALEPERR 303
Cdd:cd05583 231 AEAKDFILKLLEKDPKKR 248
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
59-303 6.41e-26

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: 106.92  E-value: 6.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKsktklknflrEVSITN-------------SLSSS-PFIIKVFdVVFETEDCY 124
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKVLKK----------EVIIEDddvectmtekrvlALANRhPFLTGLH-ACFQTEDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR---RV 201
Cdd:cd05570  72 YFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL-DAE-GHIKIADFGMCKegiWG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPglpsqw 281
Cdd:cd05570 150 GNTTSTFCGTPDYIAPEILR-----EQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELF--EAILNDEVLYP------ 216
                       250       260
                ....*....|....*....|..
gi 66773086 282 RRFTEPALRMFQRLLALEPERR 303
Cdd:cd05570 217 RWLSREAVSILKGLLTKDPARR 238
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
53-324 6.57e-26

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: 105.72  E-value: 6.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS---KTKLKNFLR-EVSITNSLSSsPFIIKVFDVVFETEDCYVFAq 128
Cdd:cd14117   8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSqieKEGVEHQLRrEIEIQSHLRH-PNILRLYNYFHDRKRIYLIL- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-GCRVKR 207
Cdd:cd14117  86 EYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKG--ELKIADFGWSVHApSLRRRT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAdaffEEFVRWQRGRLPGLPSqwrrFTEP 287
Cdd:cd14117 164 MCGTLDYLPPEMIE-----GRTHDEKVDLWCIGVLCYELLVGMPPFESASHT----ETYRRIVKVDLKFPPF----LSDG 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVfrfLKHELTSELRRR 324
Cdd:cd14117 231 SRDLISKLLRYHPSERLPLKGV---MEHPWVKANSRR 264
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
53-244 7.57e-26

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: 105.82  E-value: 7.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL---KNFLREVSITNSLSSS--PFIIKVFDV----------- 116
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgipLSTIREIALLKQLESFehPNVVRLLDVchgprtdrelk 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 117 ---VFETEDCyvfaqeyapagDLFDIIP--PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVK 191
Cdd:cd07838  81 ltlVFEHVDQ-----------DLATYLDkcPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSD--GQVK 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 192 LADFGMTRRVGCRVKRVS--GTIPYTAPEV-CQAGRAdglavdTGVDVWAFGVLIF 244
Cdd:cd07838 148 LADFGLARIYSFEMALTSvvVTLWYRAPEVlLQSSYA------TPVDMWSVGCIFA 197
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-254 8.16e-26

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: 105.07  E-value: 8.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFeTEDCYVFAQEYAP 132
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRH-PNIVRFKEVIL-TPTHLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRR--VGCRVKRVSG 210
Cdd:cd14665  80 GGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSsvLHSQPKSTVG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 66773086 211 TIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14665 160 TPAYIAPEVLLKKEYDGKI----ADVWSCGVTLYVMLVGAYPFE 199
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
59-257 8.65e-26

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: 106.33  E-value: 8.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLV---VYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLS--SSPFIIKVFdVVFETEDCYVFAQEYAPA 133
Cdd:cd05582   3 LGQGSFGKVFLVrkiTGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILAdvNHPFIVKLH-YAFQTEGKLYLILDFLRG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVKRV---SG 210
Cdd:cd05582  82 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL--DEDGHIKLTDFGLSKESIDHEKKAysfCG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 211 TIPYTAPEVC-QAGRadglavDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd05582 160 TVEYMAPEVVnRRGH------TQSADWWSFGVLMFEMLTGSLPFQGKD 201
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-303 9.71e-26

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: 105.15  E-value: 9.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKnflrEVSITNSLS-----SSPFIIKVFDVvFETEDC 123
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGK----EDSLENEIAvlrkiKHPNIVQLLDI-YESKSH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD-RECRRVKLADFGMTR-RV 201
Cdd:cd14083  76 LYLVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSpDEDSKIMISDFGLSKmED 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTGNFPweaasgadaFFEE-----FVRWQRGR 273
Cdd:cd14083 156 SGVMSTACGTPGYVAPEVLAQkpyGKA--------VDCWSIGVISYILLCGYPP---------FYDEndsklFAQILKAE 218
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 274 LPGLPSQWRRFTEPALRMFQRLLALEPERR 303
Cdd:cd14083 219 YEFDSPYWDDISDSAKDFIRHLMEKDPNKR 248
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
54-275 9.76e-26

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 104.92  E-value: 9.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086     54 ELVRELGKGTYGKVDLVVYKGTGTKM----ALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfA 127
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGGKKkvevAVKTLKEDASEqqIEEFLREARIMRKLDH-PNVVKLLGVCTEEEPLYI-V 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    128 QEYAPAGDLFDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVG-CRV 205
Cdd:smart00219  80 MEYMEGGDLLSYLRkNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGEN--LVVKISDFGLSRDLYdDDY 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086    206 KRVSGT-IPY--TAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAFfeEFVRwQRGRLP 275
Cdd:smart00219 158 YRKRGGkLPIrwMAPESLKEGK-----FTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVL--EYLK-NGYRLP 223
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
54-275 1.00e-25

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: 104.94  E-value: 1.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086     54 ELVRELGKGTYGKVDLVVYKGTGT--------KMALKfvNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYV 125
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGDgkevevavKTLKE--DASEQQIEEFLREARIMRKLDH-PNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    126 fAQEYAPAGDLFDII--PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVG- 202
Cdd:smart00221  79 -VMEYMPGGDLLDYLrkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGEN--LVVKISDFGLSRDLYd 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086    203 CRVKRVSGT-IPY--TAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAFfeEFVRwQRGRLP 275
Cdd:smart00221 156 DDYYKVKGGkLPIrwMAPESLKEGK-----FTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVL--EYLK-KGYRLP 224
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
53-253 1.13e-25

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: 105.60  E-value: 1.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT----------KLKNFLREVSitnslssSPFIIKVFDVVFETED 122
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVirlkqeqhvhNEKRVLKEVS-------HPFIIRLFWTEHDQRF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVFaQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVG 202
Cdd:cd05612  76 LYML-MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL-DKE-GHIKLTDFGFAKKLR 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 203 CRVKRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd05612 153 DRTWTLCGTPEYLAPEVIQSK-----GHNKAVDWWALGILIYEMLVGYPPF 198
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
53-308 1.19e-25

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: 105.38  E-value: 1.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----------FLREVSITNSLSSSPFIIKVFDVvFETED 122
Cdd:cd14182   5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSpeevqelreaTLKEIDILRKVSGHPNIIQLKDT-YETNT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRV- 201
Cdd:cd14182  84 FFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDD--MNIKLTDFGFSCQLd 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQAGRADG-LAVDTGVDVWAFGVLIFCVLTGNFPWeaasgadaffeefvrWQRGRLPGL-- 277
Cdd:cd14182 162 pGEKLREVCGTPGYLAPEIIECSMDDNhPGYGKEVDMWSTGVIMYTLLAGSPPF---------------WHRKQMLMLrm 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 278 ---------PSQWRRFTEPALRMFQRLLALEPERRGPAKE 308
Cdd:cd14182 227 imsgnyqfgSPEWDDRSDTVKDLISRFLVVQPQKRYTAEE 266
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
53-310 1.39e-25

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: 104.65  E-value: 1.39e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS---KTKLKNFLR-EVSITNSLSSsPFIIKVFDVVFETEDCYVFAq 128
Cdd:cd14116   7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAqleKAGVEHQLRrEVEIQSHLRH-PNILRLYGYFHDATRVYLIL- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-GCRVKR 207
Cdd:cd14116  85 EYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAG--ELKIADFGWSVHApSSRRTT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASgadafFEEFVRwqrgRLPGLPSQWRRF-TE 286
Cdd:cd14116 163 LCGTLDYLPPEMIE-----GRMHDEKVDLWSLGVLCYEFLVGKPPFEANT-----YQETYK----RISRVEFTFPDFvTE 228
                       250       260
                ....*....|....*....|....
gi 66773086 287 PALRMFQRLLALEPERRGPAKEVF 310
Cdd:cd14116 229 GARDLISRLLKHNPSQRPMLREVL 252
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
59-314 3.24e-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: 103.89  E-value: 3.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT---GTKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVVFE-TEDCYVFaqEYAP 132
Cdd:cd14066   1 IGSGGFGTV----YKGVlenGTVVAVKRLNEMNCAasKKEFLTELEMLGRLRH-PNLVRLLGYCLEsDEKLLVY--EYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDII---PPQVGLPEDTVKRCVQQLGLALDFMHG---RQLVHRDIKPENVLLfDrECRRVKLADFGMTR-----RV 201
Cdd:cd14066  74 NGSLEDRLhchKGSPPLPWPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNILL-D-EDFEPKLTDFGLARlippsES 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPW--------------EAASGADAFFEEFV 267
Cdd:cd14066 152 VSKTSAVKGTIGYLAPEYIRTGR-----VSTKSDVYSFGVVLLELLTGKPAVdenrenasrkdlveWVESKGKEELEDIL 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 268 rwqRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFRFLK 314
Cdd:cd14066 227 ---DKRLVDDDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLE 270
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
59-253 3.41e-25

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: 103.46  E-value: 3.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNF-LREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAPAGDLF 137
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMvLLEIQVMNQLNH-RNLIQLYEA-IETPNEIVLFMEYVEGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 D-IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVK-RVS-GTIPY 214
Cdd:cd14190  90 ErIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREKlKVNfGTPEF 169
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 66773086 215 TAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14190 170 LSPEVVNYDQ-----VSFPTDMWSMGVITYMLLSGLSPF 203
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-309 3.60e-25

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: 103.27  E-value: 3.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFV---NKSKTKLKNFLREVSITnSLSSSPFIIKVFDVvFETEDCYVFAQE 129
Cdd:cd08220   2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveQMTKEERQAALNEVKVL-SMLHHPNIIEYYES-FLEDKALMIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGMTRRVGCRVK- 206
Cdd:cd08220  80 YAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILL-NKKRTVVKIGDFGISKILSSKSKa 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 -RVSGTIPYTAPEVCqagraDGLAVDTGVDVWAFGvlifCVLtgnfpWEAASGADAFFEE-----FVRWQRGRLPGLPSq 280
Cdd:cd08220 159 yTVVGTPCYISPELC-----EGKPYNQKSDIWALG----CVL-----YELASLKRAFEAAnlpalVLKIMRGTFAPISD- 223
                       250       260
                ....*....|....*....|....*....
gi 66773086 281 wrRFTEPALRMFQRLLALEPERRGPAKEV 309
Cdd:cd08220 224 --RYSEELRHLILSMLHLDPNKRPTLSEI 250
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
49-253 4.10e-25

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: 103.50  E-value: 4.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL-------KNFLREVSITNSLSSsPFIIKVFDVvFETE 121
Cdd:cd14196   3 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsrEEIEREVSILRQVLH-PNIITLHDV-YENR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREC--RRVKLADFGMTR 199
Cdd:cd14196  81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiPHIKLIDFGLAH 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 200 RV--GCRVKRVSGTIPYTAPEVCQAgRADGLAvdtgVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14196 161 EIedGVEFKNIFGTPEFVAPEIVNY-EPLGLE----ADMWSIGVITYILLSGASPF 211
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
59-253 5.80e-25

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: 103.07  E-value: 5.80e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNflrEVSITNSLSSSPfIIKVFDVvFETEDCYVFAQEYAPAG 134
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKIIKarsqKEKEEVKN---EIEVMNQLNHAN-LIQLYDA-FESRNDIVLVMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFD-IIPPQVGLPE-DTVKrCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVK-RVS-G 210
Cdd:cd14193  87 ELFDrIIDENYNLTElDTIL-FIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPREKlRVNfG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 66773086 211 TIPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14193 166 TPEFLAPEVVN---YEFVSFPT--DMWSLGVIAYMLLSGLSPF 203
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
53-311 5.85e-25

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: 102.97  E-value: 5.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK-----LKNFLREVSItNSLSSSPFIIKVFDVVfETEDCYVFA 127
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKkdsyvTKNLRREGRI-QQMIRHPNITQLLDIL-ETENSYYLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGC---- 203
Cdd:cd14070  82 MELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL--DENDNIKLIDFGLSNCAGIlgys 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 -RVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAAS-GADAFFEEFVrwqRGRLPGLPSQw 281
Cdd:cd14070 160 dPFSTQCGSPAYAAPELLARKK-----YGPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQKMV---DKEMNPLPTD- 230
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 282 rrFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14070 231 --LSPGAISFLRSLLEPDPLKRPNIKQALA 258
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
59-303 5.89e-25

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: 102.88  E-value: 5.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSK--TKLKNFLR-EVSITNSLSSsPFIIKvFDVVFETEDcYVFAQEYAPAGD 135
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRfpTKQESQLRnEVAILQQLSH-PGVVN-LECMFETPE-RVFVVMEKLHGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDII--PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLF-DRECRRVKLADFGMTRRVGCRVKR--VSG 210
Cdd:cd14082  88 MLEMIlsSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLAsAEPFPQVKLCDFGFARIIGEKSFRrsVVG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPW-EAASGADAFfeefvrwQRGRLPGLPSQWRRFTEPAL 289
Cdd:cd14082 168 TPAYLAPEVLRNKG-----YNRSLDMWSVGVIIYVSLSGTFPFnEDEDINDQI-------QNAAFMYPPNPWKEISPDAI 235
                       250
                ....*....|....
gi 66773086 290 RMFQRLLALEPERR 303
Cdd:cd14082 236 DLINNLLQVKMRKR 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
57-253 6.12e-25

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: 102.77  E-value: 6.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALK---FVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFaQEYAPA 133
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKeirFQDNDPKTIKEIADEMKVLEGLDH-PNLVRYYGVEVHREEVYIF-MEYCQE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFG--------MTRRVGCRV 205
Cdd:cd06626  84 GTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL--IKLGDFGsavklknnTTTMAPGEV 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 206 KRVSGTIPYTAPEVCQAGRADGLAvdTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd06626 162 NSLVGTPAYMAPEVITGNKGEGHG--RAADIWSLGCVVLEMATGKRPW 207
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
54-275 6.49e-25

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: 102.57  E-value: 6.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    54 ELVRELGKGTYGKVDLVVYKG----TGTKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFa 127
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTLKGegenTKIKVAVKTLKEGADEeeREDFLEEASIMKKLDH-PNIVKLLGVCTQGEPLYIV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   128 QEYAPAGDLFDII---PPQVGLPeDTVKRCvQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVGCR 204
Cdd:pfam07714  80 TEYMPGGDLLDFLrkhKRKLTLK-DLLSMA-LQIAKGMEYLESKNFVHRDLAARNCLVSEN--LVVKISDFGLSRDIYDD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086   205 VKRVSGT-----IPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAFfeEFVRwQRGRLP 275
Cdd:pfam07714 156 DYYRKRGggklpIKWMAPESLKDGK-----FTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVL--EFLE-DGYRLP 224
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
49-247 9.23e-25

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: 103.79  E-value: 9.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALK-----FVNKskTKLKNFLREVSITNSLSSSPFIIKVFDVvFETE-- 121
Cdd:cd07852   5 ILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKkifdaFRNA--TDAQRTFREIMFLQELNDHPNIIKLLNV-IRAEnd 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 -DCY-VFaqEYAPAgDLFDIIppQVGLPEDTVKRCVQ-QLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMT 198
Cdd:cd07852  82 kDIYlVF--EYMET-DLHAVI--RANILEDIHKQYIMyQLLKALKYLHSGGVIHRDLKPSNILL-NSDC-RVKLADFGLA 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 199 RRVGCRVKrvSGTIP----------YTAPEVCQAGRadglAVDTGVDVWAFGvlifCVL 247
Cdd:cd07852 155 RSLSQLEE--DDENPvltdyvatrwYRAPEILLGST----RYTKGVDMWSVG----CIL 203
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
57-262 1.40e-24

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 103.06  E-value: 1.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQEYAP 132
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKdvilQDDDVECTMTEKRILSLARNHPFLTQLY-CCFQTPDRLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR---RVGCRVKRVS 209
Cdd:cd05590  80 GGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL-DHE-GHCKLADFGMCKegiFNGKTTSTFC 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 210 GTIPYTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAF 262
Cdd:cd05590 158 GTPDYIAPEILQE-----MLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLF 205
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-311 1.55e-24

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: 102.42  E-value: 1.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVREL-GKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN-FLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:cd14174   3 YRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSrVFREVETLYQCQGNKNILELIEF-FEDDTRFYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADF----GMTRRVGC-- 203
Cdd:cd14174  82 LRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCeSPDKVSPVKICDFdlgsGVKLNSACtp 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 ----RVKRVSGTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEE-----------FVR 268
Cdd:cd14174 162 ittpELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRgevcrvcqnklFES 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 269 WQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14174 242 IQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQ 284
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
53-325 1.59e-24

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: 102.41  E-value: 1.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKnflREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQEYAP 132
Cdd:cd14175   3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS---EEIEILLRYGQHPNIITLKDVYDDGKHVYL-VTELMR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR----ECRRVklADFGMTRRVGCR---V 205
Cdd:cd14175  79 GGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsgnpESLRI--CDFGFAKQLRAEnglL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWeaASGADAFFEEFV-RWQRGRLPGLPSQWRRF 284
Cdd:cd14175 157 MTPCYTANFVAPEVLKRQ-----GYDEGCDIWSLGILLYTMLAGYTPF--ANGPSDTPEEILtRIGSGKFTLSGGNWNTV 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 66773086 285 TEPALRMFQRLLALEPERRGPAKEVfrfLKHELTSELRRRP 325
Cdd:cd14175 230 SDAAKDLVSKMLHVDPHQRLTAKQV---LQHPWITQKDKLP 267
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
52-316 2.21e-24

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: 100.92  E-value: 2.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKfvnKSKTKL------KNFLREVSITNSLSSSPFIIKVFDVVFETEDCYV 125
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVK---KSKKPFrgpkerARALREVEAHAALGQHPNIVRYYSSWEEGGHLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 fAQEYAPAG---DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFGMTRRVG 202
Cdd:cd13997  78 -QMELCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDN-IFISNKG-TCKIGDFGLATRLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSGTIPYTAPEVCQagraDGLAVDTGVDVWAFGVLIFCVLTGN-FPWEAASgadaffeefvrWQR---GRLPgLP 278
Cdd:cd13997 155 TSGDVEEGDSRYLAPELLN----ENYTHLPKADIFSLGVTVYEAATGEpLPRNGQQ-----------WQQlrqGKLP-LP 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 66773086 279 SQWRRFTEpalrmFQRLLAL----EPERRGPAKEVfrfLKHE 316
Cdd:cd13997 219 PGLVLSQE-----LTRLLKVmldpDPTRRPTADQL---LAHD 252
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
53-252 2.28e-24

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: 101.22  E-value: 2.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---TKLKNFL-REVSITNSLSSsPFIIKVFDVVfETEDCYVFAQ 128
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKapeDYLQKFLpREIEVIKGLKH-PNLICFYEAI-ETTSRVYIIM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-----GC 203
Cdd:cd14162  80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNN--NLKITDFGFARGVmktkdGK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 204 RV--KRVSGTIPYTAPEVCQagradGLAVD-TGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd14162 158 PKlsETYCGSYAYASPEILR-----GIPYDpFLSDIWSMGVVLYTMVYGRLP 204
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
53-316 3.38e-24

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: 100.69  E-value: 3.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAP 132
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRH-TNIIQLIEV-FETKERVYMVMELAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD-RECRRVKLADFGM--TRRVG--CRVKR 207
Cdd:cd14087  81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpGPDSKIMITDFGLasTRKKGpnCLMKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPWEaasgADAFFEEFVRWQRGRLPGLPSQWRRFTEP 287
Cdd:cd14087 161 TCGTPEYIAPEILLR-----KPYTQSVDMWAVGVIAYILLSGTMPFD----DDNRTRLYRQILRAKYSYSGEPWPSVSNL 231
                       250       260
                ....*....|....*....|....*....
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14087 232 AKDFIDRLLTVNPGERLSATQA---LKHP 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
53-316 4.49e-24

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: 100.35  E-value: 4.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFlREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYA 131
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPlRSSTRARAF-QERDILARLSH-RRLTCLLDQ-FETRKTLILILELC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKRVS-- 209
Cdd:cd14107  81 SSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSky 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPweaasgadaFFEE-----FVRWQRGRLPGLPSQWRRF 284
Cdd:cd14107 161 GSPEFVAPEIVHQE-----PVSAATDIWALGVIAYLSLTCHSP---------FAGEndratLLNVAEGVVSWDTPEITHL 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 285 TEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14107 227 SEDAKDFIKRVLQPDPEKRPSASEC---LSHE 255
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
50-311 4.54e-24

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: 102.02  E-value: 4.54e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  50 TKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKtklKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQE 129
Cdd:cd14176  18 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYV-VTE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREC--RRVKLADFGMTRRVGCR--- 204
Cdd:cd14176  94 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpESIRICDFGFAKQLRAEngl 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWeaASGADAFFEEFV-RWQRGRLPGLPSQWRR 283
Cdd:cd14176 174 LMTPCYTANFVAPEVLERQ-----GYDAACDIWSLGVLLYTMLTGYTPF--ANGPDDTPEEILaRIGSGKFSLSGGYWNS 246
                       250       260
                ....*....|....*....|....*...
gi 66773086 284 FTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14176 247 VSDTAKDLVSKMLHVDPHQRLTAALVLR 274
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
53-257 4.55e-24

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 103.16  E-value: 4.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQE 129
Cdd:cd05622  75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSAFFWEERDIMAFANSPWVVQLF-YAFQDDRYLYMVME 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFG----MTRRVGCRV 205
Cdd:cd05622 154 YMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGtcmkMNKEGMVRC 230
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 206 KRVSGTIPYTAPEVCQAGRADGLaVDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd05622 231 DTAVGTPDYISPEVLKSQGGDGY-YGRECDWWSVGVFLYEMLVGDTPFYADS 281
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
53-303 5.01e-24

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: 101.61  E-value: 5.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSS--PFIIKVFdVVFETEDCYVF 126
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKgdiiARDEVESLMCEKRIFETVNSArhPFLVNLF-ACFQTPEHVCF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTV--KRCVQqlgLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR---V 201
Cdd:cd05589  80 VMEYAAGGDLMMHIHEDVFSEPRAVfyAACVV---LGLQFLHEHKIVYRDLKLDNLLL-DTE-GYVKIADFGLCKEgmgF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQAG---RAdglavdtgVDVWAFGVLIFCVLTGNFPWeaaSGAD--AFFEEFVRwQRGRLPG 276
Cdd:cd05589 155 GDRTSTFCGTPEFLAPEVLTDTsytRA--------VDWWGLGVLIYEMLVGESPF---PGDDeeEVFDSIVN-DEVRYPR 222
                       250       260
                ....*....|....*....|....*..
gi 66773086 277 LPSqwrrfTEpALRMFQRLLALEPERR 303
Cdd:cd05589 223 FLS-----TE-AISIMRRLLRKNPERR 243
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
53-257 6.06e-24

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: 102.39  E-value: 6.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQE 129
Cdd:cd05621  54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfemIKRSDSAFFWEERDIMAFANSPWVVQLF-CAFQDDKYLYMVME 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVG----CRV 205
Cdd:cd05621 133 YMPGGDLVNLMS-NYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL-DKY-GHLKLADFGTCMKMDetgmVHC 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 206 KRVSGTIPYTAPEVCQAGRADGLaVDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd05621 210 DTAVGTPDYISPEVLKSQGGDGY-YGRECDWWSVGVFLFEMLVGDTPFYADS 260
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
51-255 6.50e-24

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: 101.23  E-value: 6.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK----NFLREVSITnSLSSSPFIIKVfDVVFETEDCYVF 126
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQeevsFFEEERDIM-AKANSPWITKL-QYAFQDSENLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDReCRRVKLADFGMTRRVGcRV 205
Cdd:cd05601  79 VMEYHPGGDLLSLLSRYDDiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI-DR-TGHIKLADFGSAAKLS-SD 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 206 KRVSGTIP-----YTAPEVCQA-GRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd05601 156 KTVTSKMPvgtpdYIAPEVLTSmNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTE 211
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
59-290 7.27e-24

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: 100.08  E-value: 7.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDL-------VVYKG-----TGTKMALKFVNKSKTKLKNFL--REVSITNSLSSSPfIIKVFDVVfETEDCY 124
Cdd:cd14201   3 VGDFEYSRKDLvghgafaVVFKGrhrkkTDWEVAIKSINKKNLSKSQILlgKEIKILKELQHEN-IVALYDVQ-EMPNSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECR-------RVKLADFGM 197
Cdd:cd14201  81 FLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKkssvsgiRIKIADFGF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCRVKRVS--GTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASGAD--AFFEEfvrwQRGR 273
Cdd:cd14201 161 ARYLQSNMMAATlcGSPMYMAPEVIMSQHYDAKA-----DLWSIGTVIYQCLVGKPPFQANSPQDlrMFYEK----NKNL 231
                       250
                ....*....|....*..
gi 66773086 274 LPGLPSQwrrfTEPALR 290
Cdd:cd14201 232 QPSIPRE----TSPYLA 244
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
52-305 7.65e-24

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 100.46  E-value: 7.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVY---KGTGTKMALKFVNKS----KTKLKNFLR-EVSITNSLSSSPFIIkVFDVVFETEDC 123
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKAtivqKAKTAEHTRtERQVLEHIRQSPFLV-TLHYAFQTDTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGC 203
Cdd:cd05613  80 LHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL--DSSGHVVLTDFGLSKEFLL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 ----RVKRVSGTIPYTAPEVCQAGRAdglAVDTGVDVWAFGVLIFCVLTGNFPWeAASGADAFFEEFVRWQRGRLPGLPS 279
Cdd:cd05613 158 deneRAYSFCGTIEYMAPEIVRGGDS---GHDKAVDWWSLGVLMYELLTGASPF-TVDGEKNSQAEISRRILKSEPPYPQ 233
                       250       260
                ....*....|....*....|....*....
gi 66773086 280 QwrrFTEPALRMFQRLLALEPERR---GP 305
Cdd:cd05613 234 E---MSALAKDIIQRLLMKDPKKRlgcGP 259
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
55-332 7.75e-24

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: 101.15  E-value: 7.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSS----SPFIIKVFdVVFETEDCYVFAQEY 130
Cdd:cd05619   9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSlaweHPFLTHLF-CTFQTKENLFFVMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPP--QVGLPEDTVKrcVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR--VG-CRV 205
Cdd:cd05619  88 LNGGDLMFHIQSchKFDLPRATFY--AAEIICGLQFLHSKGIVYRDLKLDNILL-DKD-GHIKIADFGMCKEnmLGdAKT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEaasGADAffEEFVRWQRGRLPGLPsqwRRFT 285
Cdd:cd05619 164 STFCGTPDYIAPEILL-----GQKYNTSVDWWSFGVLLYEMLIGQSPFH---GQDE--EELFQSIRMDNPFYP---RWLE 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 286 EPALRMFQRLLALEPERRGPAKEVFR---FLKHELTSELRRRPSHRARKP 332
Cdd:cd05619 231 KEAKDILVKLFVREPERRLGVRGDIRqhpFFREINWEALEEREIEPPFKP 280
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
52-311 8.30e-24

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: 99.92  E-value: 8.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN--KSKTKLKNFL-REVSITNSLsSSPFIIKVFDVVFETEDCYVF-A 127
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDygKMSEKEKQQLvSEVNILREL-KHPNIVRYYDRIVDRANTTLYiV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIppQVG------LPEDTVKRCVQQLGLALDFMHGRQ-----LVHRDIKPENVLLFDRECrrVKLADFG 196
Cdd:cd08217  80 MEYCEGGDLAQLI--KKCkkenqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNN--VKLGDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCRVKRVS---GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIF--CVLTGnfPWEAASgadaFFEEFVRWQR 271
Cdd:cd08217 156 LARVLSHDSSFAKtyvGTPYYMSPELLN-----EQSYDEKSDIWSLGCLIYelCALHP--PFQAAN----QLELAKKIKE 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 272 GRLPGLPSqwrRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd08217 225 GKFPRIPS---RYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
22-337 9.42e-24

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: 101.64  E-value: 9.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  22 APGPGAGvpllTEDMQALTLRTlaASDVTKH-YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLR 96
Cdd:cd05594   1 SPSDNSG----AEEMEVSLTKP--KHKVTMNdFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKevivAKDEVAHTLT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  97 EVSITNSlSSSPFIIKVfDVVFETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHG-RQLVHRDI 175
Cdd:cd05594  75 ENRVLQN-SRHPFLTAL-KYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 176 KPENVLLfDREcRRVKLADFGMTR---RVGCRVKRVSGTIPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTG 249
Cdd:cd05594 153 KLENLML-DKD-GHIKITDFGLCKegiKDGATMKTFCGTPEYLAPEVLEDndyGRA--------VDWWGLGVVMYEMMCG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 250 NFPWEAASGADAFfeEFVRWQRGRLPglpsqwRRFTEPALRMFQRLLALEPERR---GP--AKEVfrfLKHELTSELRRR 324
Cdd:cd05594 223 RLPFYNQDHEKLF--ELILMEEIRFP------RTLSPEAKSLLSGLLKKDPKQRlggGPddAKEI---MQHKFFAGIVWQ 291
                       330
                ....*....|...
gi 66773086 325 PSHRARKPPGDRP 337
Cdd:cd05594 292 DVYEKKLVPPFKP 304
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
53-252 1.03e-23

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: 99.28  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRE-LGKGTYGKVDLVVYKGTGTKMALKFVNKS-KTKlknflREVSITNSLSSSPFIIKVFDV---VFETEDCYVFA 127
Cdd:cd14089   2 YTISKQvLGLGINGKVLECFHKKTGEKFALKVLRDNpKAR-----REVELHWRASGCPHIVRIIDVyenTYQGRKCLLVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLP--EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADFGMTRRVgcr 204
Cdd:cd14089  77 MECMEGGELFSRIQERADSAftEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAIlKLTDFGFAKET--- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 205 VKRVSGTIP-----YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGnFP 252
Cdd:cd14089 154 TTKKSLQTPcytpyYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCG-YP 200
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
52-252 1.06e-23

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: 99.21  E-value: 1.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSlSSSPFIIKVFDVvFETEDCYVFAQEYA 131
Cdd:cd06614   1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKE-CKHPNIVDYYDS-YLVGDELWVVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFG----MTRRVGCRvK 206
Cdd:cd06614  79 DGGSLTDIITQnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG--SVKLADFGfaaqLTKEKSKR-N 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 207 RVSGTiPY-TAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd06614 156 SVVGT-PYwMAPEVIK-----RKDYGPKVDIWSLGIMCIEMAEGEPP 196
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
58-303 1.95e-23

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: 99.36  E-value: 1.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFV--NKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYAPAGD 135
Cdd:cd06616  13 EIGRGAFGTVNKMLHKPSGTIMAVKRIrsTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICMELMDISLD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDIIPPQVG---LPED--------TVKrcvqqlglALDFMHGR-QLVHRDIKPENVLLFDRECrrVKLADFGM------ 197
Cdd:cd06616  93 KFYKYVYEVLdsvIPEEilgkiavaTVK--------ALNYLKEElKIIHRDVKPSNILLDRNGN--IKLCDFGIsgqlvd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 ----TRRVGCRvkrvsgtiPYTAPEVCQAGRA-DGLavDTGVDVWAFGVLIFCVLTGNFPWeaaSGADAFFEEFVRWQRG 272
Cdd:cd06616 163 siakTRDAGCR--------PYMAPERIDPSASrDGY--DVRSDVWSLGITLYEVATGKFPY---PKWNSVFDQLTQVVKG 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 273 RLPGL-PSQWRRFTEPALRMFQRLLALEPERR 303
Cdd:cd06616 230 DPPILsNSEEREFSPSFVNFVNLCLIKDESKR 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
53-315 2.01e-23

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: 99.31  E-value: 2.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKL--KNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQE 129
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKkFKESEDDEDvkKTALREVKVLRQLRH-ENIVNLKEA-FRRKGRLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRvkrvs 209
Cdd:cd07833  81 YVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILV--SESGVLKLCDFGFARALTAR----- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 GTIPYT---------APEVcqagradgLAVDT----GVDVWAFGVLIFCVLTGN--FPWEA---------------ASGA 259
Cdd:cd07833 154 PASPLTdyvatrwyrAPEL--------LVGDTnygkPVDVWAIGCIMAELLDGEplFPGDSdidqlyliqkclgplPPSH 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086 260 DAFFEEFVRWQRGRLPGLP---SQWRRF----TEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd07833 226 QELFSSNPRFAGVAFPEPSqpeSLERRYpgkvSSPALDFLKACLRMDPKERLTCDEL---LQH 285
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
49-315 2.01e-23

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: 98.91  E-value: 2.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRE-LGKGTYGKVDLVVYKGTGTKMALKFVNKS-KTKlknflREVSITNSLSSSPFIIKVFDV---VFETEDC 123
Cdd:cd14172   1 VTDDYKLSKQvLGLGVNGKVLECFHRRTGQKCALKLLYDSpKAR-----REVEHHWRASGGPHIVHILDVyenMHHGKRC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADFGMTRR 200
Cdd:cd14172  76 LLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVlKLTDFGFAKE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCR--VKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAASGaDAFFEEFVRWQRGRLPGLP 278
Cdd:cd14172 156 TTVQnaLQTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGFPPFYSNTG-QAISPGMKRRIRMGQYGFP 229
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 279 S-QWRRFTEPALRMFQRLLALEPERRgpaKEVFRFLKH 315
Cdd:cd14172 230 NpEWAEVSEEAKQLIRHLLKTDPTER---MTITQFMNH 264
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
52-313 2.13e-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: 98.95  E-value: 2.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALK--FVNKSKtKLKNFLREVSITNSLSSSPFIIKVFDVVF---ETEDCYVF 126
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKrmYFNDEE-QLRVAIKEIEIMKRLCGHPNIVQYYDSAIlssEGRKEVLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPaGDLFDIIP--PQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLFDRecRRVKLADFG------ 196
Cdd:cd13985  80 LMEYCP-GSLVDILEksPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNT--GRFKLCDFGsatteh 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 --MTRRVGCRV------KRVsgTIPYTAPEVcqAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFvr 268
Cdd:cd13985 157 ypLERAEEVNIieeeiqKNT--TPMYRAPEM--IDLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKY-- 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 66773086 269 wqrgRLPGLPSQWRRFTEPALRMFQRllalEPERRGPAKEVFRFL 313
Cdd:cd13985 231 ----SIPEQPRYSPELHDLIRHMLTP----DPAERPDIFQVINII 267
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
53-315 2.47e-23

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: 99.03  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRE-LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN-FLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:cd14090   3 YKLTGElLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSrVFREVETLHQCQGHPNILQLIEY-FEDDERFYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLlfdreCRR------VKLADFGMTRRVGCR 204
Cdd:cd14090  82 MRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENIL-----CESmdkvspVKICDFDLGSGIKLS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVS-----------GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEE-------- 265
Cdd:cd14090 157 STSMTpvttpelltpvGSAEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDCGWDRgeacqdcq 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 266 ---FVRWQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd14090 237 ellFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQV---LQH 286
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
53-328 2.94e-23

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: 99.61  E-value: 2.94e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKG---TGTKMALKFVNKS----KTKLKNFLR-EVSITNSLSSSPFIIkVFDVVFETEDCY 124
Cdd:cd05614   2 FELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAalvqKAKTVEHTRtERNVLEHVRQSPFLV-TLHYAFQTDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVGC- 203
Cdd:cd05614  81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL-DSE-GHVVLTDFGLSKEFLTe 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 ---RVKRVSGTIPYTAPEVCQAGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRlPGLPSq 280
Cdd:cd05614 159 ekeRTYSFCGTIEYMAPEIIRGKSGHGKAVDW----WSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCD-PPFPS- 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 281 wrRFTEPALRMFQRLLALEPERR---GP--AKEV-----FRFLKHELTSELRRRPSHR 328
Cdd:cd05614 233 --FIGPVARDLLQKLLCKDPKKRlgaGPqgAQEIkehpfFKGLDWEALALRKVNPPFR 288
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
50-311 3.30e-23

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 98.93  E-value: 3.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  50 TKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKtklKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQE 129
Cdd:cd14178   2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK---RDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYL-VME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR--ECRRVKLADFGMTRRVGCR--- 204
Cdd:cd14178  78 LMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgNPESIRICDFGFAKQLRAEngl 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWeaASGADAFFEEFV-RWQRGRLPGLPSQWRR 283
Cdd:cd14178 158 LMTPCYTANFVAPEVLKRQ-----GYDAACDIWSLGILLYTMLAGFTPF--ANGPDDTPEEILaRIGSGKYALSGGNWDS 230
                       250       260
                ....*....|....*....|....*...
gi 66773086 284 FTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14178 231 ISDAAKDIVSKMLHVDPHQRLTAPQVLR 258
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
59-309 3.33e-23

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: 99.35  E-value: 3.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSlSSSPFIIKVfDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05571   3 LGKGTFGKVILCREKATGELYAIKILKKEviiaKDEVAHTLTENRVLQN-TRHPFLTSL-KYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR---RVGCRVKRVSGT 211
Cdd:cd05571  81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL-DKD-GHIKITDFGLCKeeiSYGATTKTFCGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPglpsqwRRFTEPA 288
Cdd:cd05571 159 PEYLAPEVLEDndyGRA--------VDWWGLGVVMYEMMCGRLPFYNRDHEVLF--ELILMEEVRFP------STLSPEA 222
                       250       260
                ....*....|....*....|....*.
gi 66773086 289 LRMFQRLLALEPERR---GP--AKEV 309
Cdd:cd05571 223 KSLLAGLLKKDPKKRlggGPrdAKEI 248
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
53-253 3.40e-23

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: 98.15  E-value: 3.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLR-EVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYA 131
Cdd:cd14191   4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRqEISIMNCLHH-PKLVQCVDA-FEEKANIVMVLEMV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFD-IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRV--GCRVKRV 208
Cdd:cd14191  82 SGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLenAGSLKVL 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 66773086 209 SGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14191 162 FGTPEFVAPEVINYE-----PIGYATDMWSIGVICYILVSGLSPF 201
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
56-326 3.72e-23

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: 98.65  E-value: 3.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL--KNFLREVSITNSLSSsPFIIKVFDVVFETEDCYV-FAQEYAP 132
Cdd:cd06621   6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDvqKQILRELEINKSCAS-PYIVKYYGAFLDEQDSSIgIAMEYCE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLfDIIPPQVG-----LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdreCRR--VKLADFGMTRRVGCRV 205
Cdd:cd06621  85 GGSL-DSIYKKVKkkggrIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILL----TRKgqVKLCDFGVSGELVNSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 -KRVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAasgadaffeefvrwqRGRLPGLPSQwrrF 284
Cdd:cd06621 160 aGTFTGTSYYMAPE-----RIQGGPYSITSDVWSLGLTLLEVAQNRFPFPP---------------EGEPPLGPIE---L 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 285 TEPALRMFQRLLALEPERRGPAKEVFR-FLKHELTSELRRRPS 326
Cdd:cd06621 217 LSYIVNMPNPELKDEPENGIKWSESFKdFIEKCLEKDGTRRPG 259
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
51-253 4.24e-23

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: 97.81  E-value: 4.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN--KSKTKLKNFLREVSiTNSLSSSPFIIKVFDVVFETEDCYVfAQ 128
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDleKCQTSMDELRKEIQ-AMSQCNHPNVVSYYTSFVVGDELWL-VM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIP---PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFG--------M 197
Cdd:cd06610  79 PLLSGGSLLDIMKssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL--GEDGSVKIADFGvsaslatgG 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 198 TRRVGCRvKRVSGTIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd06610 157 DRTRKVR-KTFVGTPCWMAPEVMEQVR----GYDFKADIWSFGITAIELATGAAPY 207
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
53-311 5.15e-23

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: 99.39  E-value: 5.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSlSSSPFIIKVfDVVFETEDCYVFAQ 128
Cdd:cd05593  17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKeviiAKDEVAHTLTESRVLKN-TRHPFLTSL-KYSFQTKDRLCFVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV---GCRV 205
Cdd:cd05593  95 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKD-GHIKITDFGLCKEGitdAATM 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQ---AGRAdglavdtgVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPglpsqwR 282
Cdd:cd05593 173 KTFCGTPEYLAPEVLEdndYGRA--------VDWWGLGVVMYEMMCGRLPFYNQDHEKLF--ELILMEDIKFP------R 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 66773086 283 RFTEPALRMFQRLLALEPERR---GP--AKEVFR 311
Cdd:cd05593 237 TLSADAKSLLSGLLIKDPNKRlggGPddAKEIMR 270
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
51-303 5.45e-23

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: 99.34  E-value: 5.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVF 126
Cdd:cd05618  20 QDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKElvndDEDIDWVQTEKHVFEQASNHPFLVGLHSC-FQTESRLFF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR---RVGC 203
Cdd:cd05618  99 VIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLL-DSE-GHIKLTDYGMCKeglRPGD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQaGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWEAASGADA-------FFEEFVRWQRGRLPg 276
Cdd:cd05618 177 TTSTFCGTPNYIAPEILR-GEDYGFSVDW----WALGVLMFEMMAGRSPFDIVGSSDNpdqntedYLFQVILEKQIRIP- 250
                       250       260
                ....*....|....*....|....*..
gi 66773086 277 lpsqwRRFTEPALRMFQRLLALEPERR 303
Cdd:cd05618 251 -----RSLSVKAASVLKSFLNKDPKER 272
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
53-253 6.52e-23

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: 97.35  E-value: 6.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAP 132
Cdd:cd14113   9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQH-PQLVGLLDT-FETPTSYILVLEMAD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRR--VKLADFGMTRRVGCR--VKRV 208
Cdd:cd14113  87 QGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILV-DQSLSKptIKLADFGDAVQLNTTyyIHQL 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 66773086 209 SGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14113 166 LGSPEFAAPEIIL-----GNPVSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
51-303 7.29e-23

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 98.19  E-value: 7.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYEL-VRE--LGKGTYGKVDLVVYKGTGTKMALKFVnkSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfA 127
Cdd:cd14179   4 QHYELdLKDkpLGEGSFSICRKCLHKKTNQEYAVKIV--SKRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFL-V 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR-ECRRVKLADFGMTRRV---GC 203
Cdd:cd14179  81 MELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsDNSEIKIIDFGFARLKppdNQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCqagRADGLavDTGVDVWAFGVLIFCVLTGNFPWEAASGA---DAFFEEFVRWQRGRLPGLPSQ 280
Cdd:cd14179 161 PLKTPCFTLHYAAPELL---NYNGY--DESCDLWSLGVILYTMLSGQVPFQCHDKSltcTSAEEIMKKIKQGDFSFEGEA 235
                       250       260
                ....*....|....*....|...
gi 66773086 281 WRRFTEPALRMFQRLLALEPERR 303
Cdd:cd14179 236 WKNVSQEAKDLIQGLLTVDPNKR 258
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
48-241 8.37e-23

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: 97.51  E-value: 8.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSItnsLSS--SPFIIKVFDVVFETEDCY 124
Cdd:cd06611   2 NPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQiESEEELEDFMVEIDI---LSEckHPNIVGLYEAYFYENKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAqEYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGMTRRVG 202
Cdd:cd06611  79 ILI-EFCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLtLDGD---VKLADFGVSAKNK 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 66773086 203 CRVKRVS---GTIPYTAPEV--CQAGRADglAVDTGVDVWAFGV 241
Cdd:cd06611 155 STLQKRDtfiGTPYWMAPEVvaCETFKDN--PYDYKADIWSLGI 196
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
53-331 8.43e-23

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: 97.61  E-value: 8.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK------LKNFLREVSITNSLSSsPFIIKVFDVVFETEDCY-V 125
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTsspglsTEDLKREASICHMLKH-PHIVELLETYSSDGMLYmV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FaqEYAPAGDL-FDIIPPQVG---LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRR-VKLADFGMTRR 200
Cdd:cd14094  84 F--EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQ 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VG----CRVKRVsGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWeAASGADaFFEEFVrwqRGRLPG 276
Cdd:cd14094 162 LGesglVAGGRV-GTPHFMAPEVVKREP-----YGKPVDVWGCGVILFILLSGCLPF-YGTKER-LFEGII---KGKYKM 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 277 LPSQWRRFTEPALRMFQRLLALEPERRGPAKEVF-------------RFLKHELTSELRRRPSHRARK 331
Cdd:cd14094 231 NPRQWSHISESAKDLVRRMLMLDPAERITVYEALnhpwikerdryayRIHLPETVEQLRKFNARRKLK 298
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
53-311 8.90e-23

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 97.34  E-value: 8.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK--NFLREVSITNSLSSSPFIIKVFDVVFE-TEDCYVFAQE 129
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEqvNNLREIQALRRLSPHPNILRLIEVLFDrKTGRLALVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPaGDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrrVKLADFGMTRRVGCRVkrv 208
Cdd:cd07831  81 LMD-MNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDI--LKLADFGSCRGIYSKP--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 sgtiPYT---------APEvCQAgrADGLaVDTGVDVWAFGVLIFCVLTGN--FPWE------------AASGADAFFEE 265
Cdd:cd07831 154 ----PYTeyistrwyrAPE-CLL--TDGY-YGPKMDIWAVGCVFFEILSLFplFPGTneldqiakihdvLGTPDAEVLKK 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 266 FVRW---------QRGRlpGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd07831 226 FRKSrhmnynfpsKKGT--GLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALR 278
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
57-314 9.50e-23

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: 96.84  E-value: 9.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVdlvvYKGT-------GTKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVVFETEDCY-VF 126
Cdd:cd00192   1 KKLGEGAFGEV----YKGKlkggdgkTVDVAVKTLKEDASEseRKDFLKEARVMKKLGH-PNVVRLLGVCTEEEPLYlVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aqEYAPAGDLFDII---PPQVGLPEDTVKRCVQQLGLALD------FMHGRQLVHRDIKPENVLLFDRecRRVKLADFGM 197
Cdd:cd00192  76 --EYMEGGDLLDFLrksRPVFPSPEPSTLSLKDLLSFAIQiakgmeYLASKKFVHRDLAARNCLVGED--LVVKISDFGL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRV---GCRVKRVSGTIP--YTAPEvcqagradglAVDTGV-----DVWAFGVLIFCVLT-GNFPWEAASGADAFfeEF 266
Cdd:cd00192 152 SRDIyddDYYRKKTGGKLPirWMAPE----------SLKDGIftsksDVWSFGVLLWEIFTlGATPYPGLSNEEVL--EY 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 267 VRwQRGRLP---GLPSQWRRFtepalrMfQRLLALEPERRGPAKEVFRFLK 314
Cdd:cd00192 220 LR-KGYRLPkpeNCPDELYEL------M-LSCWQLDPEDRPTFSELVERLE 262
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
53-311 1.00e-22

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: 97.17  E-value: 1.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKFVN--KSKTKLKNFLREVSITNSLSSsPFIIKVFDVVfETEDCYVF 126
Cdd:cd07836   2 FKQLEKLGEGTYA----TVYKGrnrtTGEIVALKEIHldAEEGTPSTAIREISLMKELKH-ENIVRLHDVI-HTENKLML 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPaGDL---FDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGC 203
Cdd:cd07836  76 VFEYMD-KDLkkyMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRG--ELKLADFGLARAFGI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFvrwqrgRLPGLPSQ 280
Cdd:cd07836 153 PVNTFSNevvTLWYRAPDVLLGSR----TYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIF------RIMGTPTE 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 281 --WRRFTE-P------------------------ALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd07836 223 stWPGISQlPeykptfpryppqdlqqlfphadplGIDLLHRLLQLNPELRISAHDALQ 280
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
59-303 1.71e-22

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: 97.32  E-value: 1.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSSPFIIKVFdVVFETEDCYVFAQEYAPAG 134
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDdvecTMVEKRVLALAWENPFLTHLY-CTFQTKEHLFFVMEFLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR--VG-CRVKRVSGT 211
Cdd:cd05620  82 DLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML-DRD-GHIKIADFGMCKEnvFGdNRASTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEaASGADAFFEEFvrwqRGRLPGLPsqwRRFTEPALRM 291
Cdd:cd05620 160 PDYIAPEILQ-----GLKYTFSVDWWSFGVLLYEMLIGQSPFH-GDDEDELFESI----RVDTPHYP---RWITKESKDI 226
                       250
                ....*....|..
gi 66773086 292 FQRLLALEPERR 303
Cdd:cd05620 227 LEKLFERDPTRR 238
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
53-311 1.88e-22

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: 96.01  E-value: 1.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGT-----GTKMALKFVNKSK----TKLKNFLREVSITNSLSSsPFIIKVFDVVfETEDC 123
Cdd:cd14076   3 YILGRTLGEGEFGKVKLGWPLPKanhrsGVQVAIKLIRRDTqqenCQTSKIMREINILKGLTH-PNIVRLLDVL-KTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVGC 203
Cdd:cd14076  81 IGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL-DKN-RNLVITDFGFANTFDH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 R----VKRVSGTIPYTAPEVCQagrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEaASGADAFFEEFVRWQRgRLPGLPS 279
Cdd:cd14076 159 FngdlMSTSCGSPCYAAPELVV---SDSMYAGRKADIWSCGVILYAMLAGYLPFD-DDPHNPNGDNVPRLYR-YICNTPL 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 280 QWRRFTEPALR-MFQRLLALEPERRGPAKEVFR 311
Cdd:cd14076 234 IFPEYVTPKARdLLRRILVPNPRKRIRLSAIMR 266
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
53-283 3.05e-22

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: 95.80  E-value: 3.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKFV----NKSKTKLKNfLREVSITNSLSS--SPFIIKVFDVVF---- 118
Cdd:cd07863   2 YEPVAEIGVGAYG----TVYKArdphSGHFVALKSVrvqtNEDGLPLST-VREVALLKRLEAfdHPNIVRLMDVCAtsrt 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 --ETEDCYVFAQEYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFG 196
Cdd:cd07863  77 drETKVTLVFEHVDQDLRTYLDKVPPP-GLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGG--QVKLADFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCR--VKRVSGTIPYTAPEV-CQAGRAdglavdTGVDVWAFGVL---------IFCvltGNfpweaaSGADAFFE 264
Cdd:cd07863 154 LARIYSCQmaLTPVVVTLWYRAPEVlLQSTYA------TPVDMWSVGCIfaemfrrkpLFC---GN------SEADQLGK 218
                       250       260
                ....*....|....*....|.
gi 66773086 265 EFvrwqrgRLPGLPS--QWRR 283
Cdd:cd07863 219 IF------DLIGLPPedDWPR 233
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
51-257 3.13e-22

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 97.06  E-value: 3.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITnSLSSSPFIIKVFdVVFETEDCYVF 126
Cdd:cd05596  26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKfemiKRSDSAFFWEERDIM-AHANSEWIVQLH-YAFQDDKYLYM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVG---- 202
Cdd:cd05596 104 VMDYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASG--HLKLADFGTCMKMDkdgl 180
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 203 CRVKRVSGTIPYTAPEVCQAGRADGLaVDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd05596 181 VRSDTAVGTPDYISPEVLKSQGGDGV-YGRECDWWSVGVFLYEMLVGDTPFYADS 234
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-281 4.59e-22

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: 94.88  E-value: 4.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN---FLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQE 129
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEreeSRKEVAVLSKMKH-PNIVQYQES-FEENGNLYIVMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGL--PEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRV-- 205
Cdd:cd08218  80 YCDGGDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGI--IKLGDFGIARVLNSTVel 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 206 -KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFvrwqRGRLPGLPSQW 281
Cdd:cd08218 158 aRTCIGTPYYLSPEICE-----NKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKII----RGSYPPVPSRY 225
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
53-253 4.95e-22

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 95.17  E-value: 4.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITN---SLSSSPFIIKVFdVVFETEDCYVFAQE 129
Cdd:cd05609   2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERdilTFAENPFVVSMY-CSFETKRHLCMVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTrRVG------- 202
Cdd:cd05609  81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI--TSMGHIKLTDFGLS-KIGlmslttn 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 203 ---------CRV---KRVSGTIPYTAPEVC--QA-GRAdglavdtgVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd05609 158 lyeghiekdTREfldKQVCGTPEYIAPEVIlrQGyGKP--------VDWWAMGIILYEFLVGCVPF 215
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
59-303 5.22e-22

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: 94.83  E-value: 5.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL---KNFLREVSITNSLSSSpFIIKVFDVVFETEDCYVfAQEYAPAGD 135
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIeerKALLKEAEKMERARHS-YVLPLLGVCVERRSLGL-VMEYMENGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 L---FDIIPPQVGLPedtVK-RCVQQLGLALDFMHG--RQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVG------- 202
Cdd:cd13978  79 LkslLEREIQDVPWS---LRfRIIHEIALGMNFLHNmdPPLLHHDLKPENILL-DNHF-HVKISDFGLSKLGMksisanr 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 -CRVKRVSGTIPYTAPEVCQAGRAdglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLP--GLPS 279
Cdd:cd13978 154 rRGTENLGGTPIYMAPEAFDDFNK---KPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPSLDdiGRLK 230
                       250       260
                ....*....|....*....|....
gi 66773086 280 QWRRFTEpALRMFQRLLALEPERR 303
Cdd:cd13978 231 QIENVQE-LISLMIRCWDGNPDAR 253
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
53-254 6.10e-22

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: 96.24  E-value: 6.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd05617  17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKElvhdDEDIDWVQTEKHVFEQASSNPFLVGLHSC-FQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR---RVGCRV 205
Cdd:cd05617  96 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL-DAD-GHIKLTDYGMCKeglGPGDTT 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66773086 206 KRVSGTIPYTAPEVCQaGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWE 254
Cdd:cd05617 174 STFCGTPNYIAPEILR-GEEYGFSVDW----WALGVLMFEMMAGRSPFD 217
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
53-309 6.27e-22

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: 96.20  E-value: 6.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFdVVFETEDCYVFAQE 129
Cdd:cd05573   3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDIladADSPWIVRLH-YAFQDEDHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDL------FDIippqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVG- 202
Cdd:cd05573  82 YMPGGDLmnllikYDV------FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL-DAD-GHIKLADFGLCTKMNk 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 -------------------------------CRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGnF 251
Cdd:cd05573 154 sgdresylndsvntlfqdnvlarrrphkqrrVRAYSAVGTPDYIAPEVLR-----GTGYGPECDWWSLGVILYEMLYG-F 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 252 PWEAASGADAFFEEFVRWQRgRLpGLPSQwRRFTEPALRMFQRLLAlEPERR-GPAKEV 309
Cdd:cd05573 228 PPFYSDSLVETYSKIMNWKE-SL-VFPDD-PDVSPEAIDLIRRLLC-DPEDRlGSAEEI 282
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
53-241 9.11e-22

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: 93.87  E-value: 9.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNkSKTKLKNFLREVSITNSlSSSPFIIKVFDVVFETEDCYVFaQEYAP 132
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVP-VEEDLQEIIKEISILKQ-CDSPYIVKYYGSYFKNTDLWIV-MEYCG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGM-TRRVGCRVKR--V 208
Cdd:cd06612  82 AGSVSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL-NEEG-QAKLADFGVsGQLTDTMAKRntV 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 66773086 209 SGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGV 241
Cdd:cd06612 160 IGTPFWMAPEVIQEIGYNNKA-----DIWSLGI 187
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
53-244 9.88e-22

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: 94.92  E-value: 9.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKfVNKsKTKLKNFLREVSITNSLSSSPFIIKVFDVVF-ETEDCYVFAQEYA 131
Cdd:cd14132  20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIK-VLK-PVKKKKIKREIKILQNLRGGPNIVKLLDVVKdPQSKTPSLIFEYV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDlFDIIPPQVGLPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVlLFDRECRRVKLADFGMT------RRVGCRV 205
Cdd:cd14132  98 NNTD-FKTLYPTLTDYD--IRYYMYELLKALDYCHSKGIMHRDVKPHNI-MIDHEKRKLRLIDWGLAefyhpgQEYNVRV 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 206 krvsGTIPYTAPEvcqagradgLAV-----DTGVDVWAFGV----LIF 244
Cdd:cd14132 174 ----ASRYYKGPE---------LLVdyqyyDYSLDMWSLGCmlasMIF 208
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
59-330 1.06e-21

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: 94.72  E-value: 1.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLknflREVSITNSLSSSPFIIKVFDV---VFETEDCYVFAQEYAPAGD 135
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKMLQDCPKAR----REVELHWRASQCPHIVRIVDVyenLYAGRKCLLIVMECLDGGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADFGMTRRVGCRVKRVSG-- 210
Cdd:cd14170  86 LFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIlKLTDFGFAKETTSHNSLTTPcy 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAASG--ADAFFEEFVRWQRGRLPGlpSQWRRFTEPA 288
Cdd:cd14170 166 TPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGYPPFYSNHGlaISPGMKTRIRMGQYEFPN--PEWSEVSEEV 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 66773086 289 LRMFQRLLALEPERRGPAKEvfrFLKHEL---TSELRRRPSHRAR 330
Cdd:cd14170 239 KMLIRNLLKTEPTQRMTITE---FMNHPWimqSTKVPQTPLHTSR 280
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
54-303 1.12e-21

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: 94.15  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS--KTKLKNFLREVSITNSlSSSPFIIKvFDVVFETEDCYVFAQEYA 131
Cdd:cd06622   4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLEldESKFNQIIMELDILHK-AVSPYIVD-FYGAFFIEGAVYMCMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGD---LFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDREcrRVKLADFGMTrrvGCRVKR 207
Cdd:cd06622  82 DAGSldkLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNG--QVKLCDFGVS---GNLVAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VS----GTIPYTAPEVCQAGRADGLAVDT-GVDVWAFGVLIFCVLTGNFPWEAASgADAFFEEFVRWQRGRLPGLPSQwr 282
Cdd:cd06622 157 LAktniGCQSYMAPERIKSGGPNQNPTYTvQSDVWSLGLSILEMALGRYPYPPET-YANIFAQLSAIVDGDPPTLPSG-- 233
                       250       260
                ....*....|....*....|.
gi 66773086 283 rFTEPALRMFQRLLALEPERR 303
Cdd:cd06622 234 -YSDDAQDFVAKCLNKIPNRR 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
52-316 1.25e-21

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: 93.44  E-value: 1.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGkvdlVVYKG----TGTKMALKFV---NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCY 124
Cdd:cd06627   1 NYQLGDLIGRGAFG----SVYKGlnlnTGEFVAIKQIsleKIPKSDLKSVMGEIDLLKKLNH-PNIVKYIGS-VKTKDSL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCR 204
Cdd:cd06627  75 YIILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG--LVKLADFGVATKLNEV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKR---VSGTiPY-TAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFeEFVRWQRGRLP-GLPS 279
Cdd:cd06627 153 EKDensVVGT-PYwMAPEVIE-----MSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALF-RIVQDDHPPLPeNISP 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 66773086 280 QWRRFTepaLRMFQRllalEPERRGPAKEVfrfLKHE 316
Cdd:cd06627 226 ELRDFL---LQCFQK----DPTLRPSAKEL---LKHP 252
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-251 1.29e-21

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: 93.72  E-value: 1.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYK-GTGTKMALKFVN-----------KSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFET 120
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKsNGQTLLALKEINmtnpafgrteqERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFAQ--EYAPAGDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHG-RQLVHRDIKPENVLLFDREcrRVKLADFG 196
Cdd:cd08528  82 DRLYIVMEliEGAPLGEHFSSLKEKNEhFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDD--KVTITDFG 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVG---CRVKRVSGTIPYTAPEVCQAgradgLAVDTGVDVWAFGVLIF--CVLTGNF 251
Cdd:cd08528 160 LAKQKGpesSKMTSVVGTILYSCPEIVQN-----EPYGEKADIWALGCILYqmCTLQPPF 214
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
53-268 1.44e-21

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: 93.51  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKGTGTK----MALKFVNKSK-TKLKNflrEVSITNSLSSsPFIIKVFDVvFETEDCYVFA 127
Cdd:cd14010   2 YVLYDEIGRGKHS----VVYKGRRKGtiefVAIKCVDKSKrPEVLN---EVRLTHELKH-PNVLKFYEW-YETSNHLWLV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVG----- 202
Cdd:cd14010  73 VEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL--DGNGTLKLSDFGLARREGeilke 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 --------------CRVKRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASgadafFEEFVR 268
Cdd:cd14010 151 lfgqfsdegnvnkvSKKQAKRGTPYYMAPELFQGG-----VHSFASDLWALGCVLYEMFTGKPPFVAES-----FTELVE 220
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
53-254 1.72e-21

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: 93.00  E-value: 1.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---LKNFL-REVSITNSLSSsPFIIKVFDVvFETEDCYVFAQ 128
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASpdfVQKFLpRELSILRRVNH-PNIVQMFEC-IEVANGRLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcRRVKLADFGMTRRVGCRVK-- 206
Cdd:cd14164  80 MEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADD-RKIKIADFGFARFVEDYPEls 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66773086 207 -RVSGTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14164 159 tTFCGSRAYTPPEVILGTPYDP----KKYDVWSLGVVLYVMVTGTMPFD 203
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
53-352 1.86e-21

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: 93.93  E-value: 1.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKtklKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQEYAP 132
Cdd:cd14177   6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK---RDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYL-VTELMK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECR--RVKLADFGMTRrvgcRVKRVSG 210
Cdd:cd14177  82 GGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANadSIRICDFGFAK----QLRGENG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 -------TIPYTAPEVC-QAGradglaVDTGVDVWAFGVLIFCVLTGNFPWeaASGADAFFEE-FVRWQRGRLPGLPSQW 281
Cdd:cd14177 158 llltpcyTANFVAPEVLmRQG------YDAACDIWSLGVLLYTMLAGYTPF--ANGPNDTPEEiLLRIGSGKFSLSGGNW 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 282 RRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHELTselrrrpSHRarkppgDRPPAAGPLRLEAPGPLK 352
Cdd:cd14177 230 DTVSDAAKDLLSHMLHVDPHQRYTAEQV---LKHSWI-------ACR------DQLPHYQLNRQDAPHLVK 284
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
53-315 2.62e-21

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: 95.08  E-value: 2.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITnsLSSSPFIIKVFDVVFETEDCYVFAQ 128
Cdd:cd05624  74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKwemlKRAETACFREERNVL--VNGDCQWITTLHYAFQDENYLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFG----MTRRVGC 203
Cdd:cd05624 152 DYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL-DMN-GHIRLADFGsclkMNDDGTV 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQAgRADGLA-VDTGVDVWAFGVLIFCVLTGNFPWEAASGADAF-----FEEfvRWQrgrlpgL 277
Cdd:cd05624 230 QSSVAVGTPDYISPEILQA-MEDGMGkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYgkimnHEE--RFQ------F 300
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 278 PSQWRRFTEPALRMFQRLLAlEPERRGPAKEVFRFLKH 315
Cdd:cd05624 301 PSHVTDVSEEAKDLIQRLIC-SRERRLGQNGIEDFKKH 337
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
54-306 2.64e-21

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: 93.27  E-value: 2.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALK--FVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQEYA 131
Cdd:cd06620   8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKviHIDAKSSVRKQILRELQILHECHS-PYIVSFYGAFLNENNNIIICMEYM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDREcrRVKLADFGMTRRVgcrVKRVS- 209
Cdd:cd06620  87 DCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG--QIKLCDFGVSGEL---INSIAd 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 ---GTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPW-------EAASGADAFFEEFVRWQRGRLPGLPS 279
Cdd:cd06620 162 tfvGTSTYMSPE-----RIQGGKYSVKSDVWSLGLSIIELALGEFPFagsndddDGYNGPMGILDLLQRIVNEPPPRLPK 236
                       250       260
                ....*....|....*....|....*...
gi 66773086 280 QwRRFTEPALRMFQR-LLALEPERRGPA 306
Cdd:cd06620 237 D-RIFPKDLRDFVDRcLLKDPRERPSPQ 263
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
59-254 4.11e-21

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: 91.40  E-value: 4.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTgtKMALKFVNKSK-TKLKNfLREVSitnslssSPFIIKvFDVVFETEDCYVFAQEYAPAGDLF 137
Cdd:cd14059   1 LGSGAQGAVFLGKFRGE--EVAVKKVRDEKeTDIKH-LRKLN-------HPNIIK-FKGVCTQAPCYCILMEYCPYGQLY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRVKRVS--GTIPYT 215
Cdd:cd14059  70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV--LKISDFGTSKELSEKSTKMSfaGTVAWM 147
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 66773086 216 APEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14059 148 APEVIRNE-----PCSEKVDIWSFGVVLWELLTGEIPYK 181
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
53-252 4.25e-21

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: 92.31  E-value: 4.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN--KSKTKLKNFLREVSItnsLSS--SPFIIKVFDVVFETEDCYVFaQ 128
Cdd:cd06609   3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleEAEDEIEDIQQEIQF---LSQcdSPYITKYYGSFLKGSKLWII-M 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVKRV 208
Cdd:cd06609  79 EYCGGGSVLDLLKPG-PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILL--SEEGDVKLADFGVSGQLTSTMSKR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 209 S---GTiPY-TAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd06609 156 NtfvGT-PFwMAPEVIKQS-----GYDEKADIWSLGITAIELAKGEPP 197
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
52-241 4.42e-21

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: 91.98  E-value: 4.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSITNSlSSSPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKlEPGDDFEIIQQEISMLKE-CRHPNIVAYFGSYLRRDKLWI-VMEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKR-CVQQLgLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRV-KRV 208
Cdd:cd06613  79 CGGGSLQDIYQVTGPLSELQIAYvCRETL-KGLAYLHSTGKIHRDIKGANILLTEDGD--VKLADFGVSAQLTATIaKRK 155
                       170       180       190
                ....*....|....*....|....*....|....*
gi 66773086 209 S--GTIPYTAPEVCQAGRADGLavDTGVDVWAFGV 241
Cdd:cd06613 156 SfiGTPYWMAPEVAAVERKGGY--DGKCDIWALGI 188
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
57-261 4.53e-21

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: 93.25  E-value: 4.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAP 132
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKElvndDEDIDWVQTEKHVFETASNHPFLVGLHSC-FQTESRLFFVIEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR---RVGCRVKRVS 209
Cdd:cd05588  80 GGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLL-DSE-GHIKLTDYGMCKeglRPGDTTSTFC 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 210 GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADA 261
Cdd:cd05588 158 GTPNYIAPEILR-----GEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDN 204
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
53-341 4.77e-21

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: 93.14  E-value: 4.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTkLKNFLREVSITN----SLSSSPFIIKVFDVVFETEDCYVFAQ 128
Cdd:cd05616   2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVV-IQDDDVECTMVEkrvlALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPpQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV---GCR 204
Cdd:cd05616  81 EYVNGGDLMYHIQ-QVGrFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML-DSE-GHIKIADFGMCKENiwdGVT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYTAPEVCqAGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWEAASgADAFFEEFVRWQrgrlpglPSQWRRF 284
Cdd:cd05616 158 TKTFCGTPDYIAPEII-AYQPYGKSVDW----WAFGVLLYEMLAGQAPFEGED-EDELFQSIMEHN-------VAYPKSM 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 285 TEPALRMFQRLLALEPERR---GPAKE-------VFRFLKHEltselrrRPSHRARKPPGdRPPAAG 341
Cdd:cd05616 225 SKEAVAICKGLMTKHPGKRlgcGPEGErdikehaFFRYIDWE-------KLERKEIQPPY-KPKACG 283
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
54-254 5.21e-21

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: 92.49  E-value: 5.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS--KTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYA 131
Cdd:cd06617   4 EVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATvnSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICMEVMD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLF--DIIPPQVGLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLfDREcRRVKLADFGMTrrvGCRVKRV 208
Cdd:cd06617  84 TSLDKFykKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLI-NRN-GQVKLCDFGIS---GYLVDSV 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 209 SGTI-----PYTAPE-VCQAGRADGLAVDTgvDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd06617 159 AKTIdagckPYMAPErINPELNQKGYDVKS--DVWSLGITMIELATGRFPYD 208
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
58-255 6.31e-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: 92.04  E-value: 6.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK------------------------LKNFLREVSITNSLSSsPFIIKV 113
Cdd:cd14118   1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLkqagffrrppprrkpgalgkpldpLDRVYREIAILKKLDH-PNVVKL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 114 FDVVFET-EDCYVFAQEYAPAGDLFDIiPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKL 192
Cdd:cd14118  80 VEVLDDPnEDNLYMVFELVDKGAVMEV-PTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDG--HVKI 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 193 ADFGmtrrVGCR-------VKRVSGTIPYTAPEVCQAGRAD--GLAvdtgVDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd14118 157 ADFG----VSNEfegddalLSSTAGTPAFMAPEALSESRKKfsGKA----LDIWAMGVTLYCFVFGRCPFED 220
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
53-316 6.83e-21

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: 92.25  E-value: 6.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK----NF--LREVSITNSLSSsPFIIKVFDVvFETEDCYVF 126
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdgiNFtaLREIKLLQELKH-PNIIGLLDV-FGHKSNINL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPaGDLFDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRV 205
Cdd:cd07841  80 VFEFME-TDLEKVIKdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV--LKLADFGLARSFGSPN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSG---TIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGN--FPWE----------AASGAdafFEEFVRWQ 270
Cdd:cd07841 157 RKMTHqvvTRWYRAPELLFGARHYG----VGVDMWSVGCIFAELLLRVpfLPGDsdidqlgkifEALGT---PTEENWPG 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 271 RGRLPgLPSQWRRFTEPALRM------------FQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd07841 230 VTSLP-DYVEFKPFPPTPLKQifpaasddaldlLQRLLTLNPNKRITARQA---LEHP 283
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
53-316 7.46e-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: 91.86  E-value: 7.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKfvnksKTKLKN--------FLREVSITNSLSSsPFIIKVFDVVFETEDCY 124
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALK-----KIRMENekegfpitAIREIKLLQKLDH-PNVVRLKEIVTSKGSAK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 -------VFaqEYAPAgDLFDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFG 196
Cdd:cd07840  75 ykgsiymVF--EYMDH-DLTGLLDnPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND--GVLKLADFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTR---RVGCRV--KRVSgTIPYTAPEVCQAGRADGlavdTGVDVWAFGVLIFCVLTGNFPWEAASGADAF--------- 262
Cdd:cd07840 150 LARpytKENNADytNRVI-TLWYRPPELLLGATRYG----PEVDMWSVGCILAELFTGKPIFQGKTELEQLekifelcgs 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 263 --------FEEFVRWQRGRLPglPSQWRRFTE--------PALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd07840 225 pteenwpgVSDLPWFENLKPK--KPYKRRLREvfknvidpSALDLLDKLLTLDPKKRISADQA---LQHE 289
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
59-303 7.93e-21

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: 91.82  E-value: 7.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITnSLSSSPFIIKVfDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetmALNEKIIL-EKVSSPFIVSL-AYAFETKDKLCLVLTLMNGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DL-FDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV--GCRVKRVSG 210
Cdd:cd05577  79 DLkYHIYNvGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHG--HVRISDLGLAVEFkgGKKIKGRVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEaASGADAFFEEFVRWQRGRLPGLPSqwrRFTEPALR 290
Cdd:cd05577 157 THGYMAPEVLQKEV----AYDFSVDWFALGCMLYEMIAGRSPFR-QRKEKVDKEELKRRTLEMAVEYPD---SFSPEARS 228
                       250
                ....*....|...
gi 66773086 291 MFQRLLALEPERR 303
Cdd:cd05577 229 LCEGLLQKDPERR 241
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
59-262 8.37e-21

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: 92.56  E-value: 8.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAPAG 134
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVLKKdvilQDDDVDCTMTEKRILALAAKHPFLTALHSC-FQTKDRLFFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR---VGCRVKRVSGT 211
Cdd:cd05591  82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL-DAE-GHCKLADFGMCKEgilNGKTTTTFCGT 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 212 IPYTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAF 262
Cdd:cd05591 160 PDYIAPEILQE-----LEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLF 205
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-311 1.13e-20

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: 91.59  E-value: 1.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK-TKLKNFLREVSITNSLSSSPfIIKVFDVvFETEDCYVFA 127
Cdd:cd14166   1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPlSRDSSLENEIAVLKRIKHEN-IVTLEDI-YESTTHYYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVL-LFDRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd14166  79 MQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKIMITDFGLSKMEQNGIM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVS-GTIPYTAPEVcqagradgLA---VDTGVDVWAFGVLIFCVLTGNFPweaasgadaFFEE-----FVRWQRGRLPGL 277
Cdd:cd14166 159 STAcGTPGYVAPEV--------LAqkpYSKAVDCWSIGVITYILLCGYPP---------FYEEtesrlFEKIKEGYYEFE 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 66773086 278 PSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14166 222 SPFWDDISESAKDFIRHLLEKNPSKRYTCEKALS 255
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-311 1.40e-20

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: 90.57  E-value: 1.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFV---NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVF-AQ 128
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLnlkNASKRERKAAEQEAKLLSKLKH-PNIVSYKES-FEGEDGFLYiVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd08223  80 GFCEGGDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFL--TKSNIIKVGDLGIARVLESSSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVS---GTIPYTAPEVCQagradGLAVDTGVDVWAFGvlifCVLtgnfpWEAASGADAF----FEEFV-RWQRGRLPGLP 278
Cdd:cd08223 158 MATtliGTPYYMSPELFS-----NKPYNHKSDVWALG----CCV-----YEMATLKHAFnakdMNSLVyKILEGKLPPMP 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 279 SQwrrFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd08223 224 KQ---YSPELGELIKAMLHQDPEKRPSVKRILR 253
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
59-315 1.41e-20

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: 90.57  E-value: 1.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGkvdlVVYKGT--GTKMALKFVnKSKTKLKNFLREVsitNSLS--SSPFIIKVFDVV-FETEDCYVFaqEYAPA 133
Cdd:cd14058   1 VGRGSFG----VVCKARwrNQIVAVKII-ESESEKKAFEVEV---RQLSrvDHPNIIKLYGACsNQKPVCLVM--EYAEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVGLPEDTVKRCVQ---QLGLALDFMHG---RQLVHRDIKPENVLLFdrECRRV-KLADFGMTRRVGCRVK 206
Cdd:cd14058  71 GSLYNVLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSmkpKALIHRDLKPPNLLLT--NGGTVlKICDFGTACDISTHMT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVrwQRGRLP----GLPsqwr 282
Cdd:cd14058 149 NNKGSAAWMAPEVFE-----GSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAV--HNGERPplikNCP---- 217
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 283 rftEPALRMFQRLLALEPERRGPAKEVFRFLKH 315
Cdd:cd14058 218 ---KPIESLMTRCWSKDPEKRPSMKEIVKIMSH 247
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
59-254 1.53e-20

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: 90.39  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK-----LKNFLREVSITNSLSSsPFIIKVFDVVF--ETEDCYVFaQEYA 131
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRripngEANVKREIQILRRLNH-RNVIKLVDVLYneEKQKLYMV-MEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAG--DLFDIiPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV-----GCR 204
Cdd:cd14119  79 VGGlqEMLDS-APDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL--TTDGTLKISDFGVAEALdlfaeDDT 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 205 VKRVSGTIPYTAPEVcqagrADGLAVDTG--VDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14119 156 CTTSQGSPAFQPPEI-----ANGQDSFSGfkVDIWSAGVTLYNMTTGKYPFE 202
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
42-241 1.55e-20

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: 91.25  E-value: 1.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  42 RTLAASDVtkhYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSITNSlSSSPFIIKVFDVVFET 120
Cdd:cd06644   6 RDLDPNEV---WEIIGELGDGAFGKVYKAKNKETGALAAAKVIEtKSEEELEDYMVEIEILAT-CNHPYIVKLLGAFYWD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFAqEYAPAGDLfDIIPPQV--GLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGM 197
Cdd:cd06644  82 GKLWIMI-EFCPGGAV-DAIMLELdrGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLtLDGD---IKLADFGV 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 198 T-RRVGCRVKRVS--GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGV 241
Cdd:cd06644 157 SaKNVKTLQRRDSfiGTPYWMAPEVVMCETMKDTPYDYKADIWSLGI 203
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
59-255 2.11e-20

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: 91.31  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdLVVYKGTGTK----MALKFVNKSK----------TKL-KNFLREVSitnslssSPFIIKVFdVVFETEDC 123
Cdd:cd05584   4 LGKGGYGKV-FQVRKTTGSDkgkiFAMKVLKKASivrnqkdtahTKAeRNILEAVK-------HPFIVDLH-YAFQTGGK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV-- 201
Cdd:cd05584  75 LYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL-DAQ-GHVKLTDFGLCKESih 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd05584 153 dGTVTHTFCGTIEYMAPEILTRsghGKA--------VDWWSLGALMYDMLTGAPPFTA 202
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
59-255 2.57e-20

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 91.09  E-value: 2.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL------REVSITNSLSSSPFIIKVfDVVFETEDCYVFAQEYAP 132
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVahtigeRNILVRTALDESPFIVGL-KFSFQTPTDLYLVTDYMS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR---RVGCRVKRVS 209
Cdd:cd05586  80 GGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL--DANGHIALCDFGLSKadlTDNKTTNTFC 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 GTIPYTAPEVcqagradgLAVDTG----VDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd05586 158 GTTEYLAPEV--------LLDEKGytkmVDFWSLGVLVFEMCCGWSPFYA 199
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
53-260 3.07e-20

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: 89.92  E-value: 3.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVnKSKTKLKNFLR-EVSITNSLSSSPfIIKVFDVvFETEDCYVFAQEYA 131
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFV-KVKGADQVLVKkEISILNIARHRN-ILRLHES-FESHEELVMIFEFI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDII-PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRV--GCRVKRV 208
Cdd:cd14104  79 SGVDIFERItTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLkpGDKFRLQ 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 209 SGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd14104 159 YTSAEFYAPEVHQHE-----SVSTATDMWSLGCLVYVLLSGINPFEAETNQQ 205
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
53-315 3.51e-20

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: 90.28  E-value: 3.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKfvnksKTKLK--------NFLREVSITNSLSSSPFIIKVFDVVFETED-- 122
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK-----KTRLEmeeegvpsTALREVSLLQMLSQSIYIVRLLDVEHVEENgk 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 -CYVFAQEYAPAgDLFDIIP-----PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFG 196
Cdd:cd07837  78 pLLYLVFEYLDT-DLKKFIDsygrgPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQN-LLVDKQKGLLKIADLG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCRVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVlIFCVLTGNFP-WEAASGADAFFEEFvrwqrg 272
Cdd:cd07837 156 LGRAFTIPIKSYTHeivTLWYRAPEVLLGST----HYSTPVDMWSVGC-IFAEMSRKQPlFPGDSELQQLLHIF------ 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 273 RLPGLPSQ-----------WRRF--------------TEP-ALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd07837 225 RLLGTPNEevwpgvsklrdWHEYpqwkpqdlsravpdLEPeGVDLLTKMLAYDPAKRISAKAA---LQH 290
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
74-317 3.96e-20

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: 89.41  E-value: 3.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  74 GTGTKMALK---FVNKSKTK----LKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFaQEYAPAGDLFDIIPPQVGL 146
Cdd:cd06630  23 KTGTLMAVKqvsFCRNSSSEqeevVEAIREEIRMMARLNH-PNIVRMLGATQHKSHFNIF-VEWMAGGSVASLLSKYGAF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 147 PEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFGMTRRVGCRVKRVS-------GTIPYTAPEV 219
Cdd:cd06630 101 SENVIINYTLQILRGLAYLHDNQIIHRDLKGAN-LLVDSTGQRLRIADFGAAARLASKGTGAGefqgqllGTIAFMAPEV 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 220 C---QAGRAdglavdtgVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWRrftePALRMFQ-RL 295
Cdd:cd06630 180 LrgeQYGRS--------CDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPPIPEHLS----PGLRDVTlRC 247
                       250       260
                ....*....|....*....|..
gi 66773086 296 LALEPERRGPAKEVfrfLKHEL 317
Cdd:cd06630 248 LELQPEDRPPAREL---LKHPV 266
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-311 3.97e-20

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: 90.09  E-value: 3.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRE-LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN-FLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:cd14173   3 YQLQEEvLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSrVFREVEMLYQCQGHRNVLELIEF-FEEEDKFYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADF--GMTRRVGCRVKR 207
Cdd:cd14173  82 MRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCeHPNQVSPVKICDFdlGSGIKLNSDCSP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VS--------GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEE-----------FVR 268
Cdd:cd14173 162 IStpelltpcGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDCGWDRgeacpacqnmlFES 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 269 WQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14173 242 IQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQ 284
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
59-316 4.86e-20

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: 89.36  E-value: 4.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL-KNFLREVSITNSLSSSPFIIKVFD---VV----FE-TEDCYVFAQE 129
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSdRADSRQKTVVDALKSEIDTLKDLDhpnIVqylgFEeTEDYFSIFLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECrrvKLADFGMTRRV-----GC 203
Cdd:cd06629  89 YVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVdLEGIC---KISDFGISKKSddiygNN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQagrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRgrlPGLPSQwRR 283
Cdd:cd06629 166 GATSMQGSVFWMAPEVIH---SQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSA---PPVPED-VN 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 284 FTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd06629 239 LSPEALDFLNACFAIDPRDRPTAAEL---LSHP 268
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
51-354 5.04e-20

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: 89.93  E-value: 5.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYEL-VRE--LGKGTYGKVDLVVYKGTGTKMALKFVnkSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfA 127
Cdd:cd14180   3 QCYELdLEEpaLGEGSFSVCRKCRHRQSGQEYAVKII--SRRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYL-V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR-ECRRVKLADFGMTRRvgcrvk 206
Cdd:cd14180  80 MELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsDGAVLKVIDFGFARL------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIP---------YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASG---ADAFFEEFVRWQRGRL 274
Cdd:cd14180 154 RPQGSRPlqtpcftlqYAAPELFSNQ-----GYDESCDLWSLGVILYTMLSGQVPFQSKRGkmfHNHAADIMHKIKEGDF 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 275 PGLPSQWRRFTEPALRMFQRLLALEPERRgpakevfrfLKhelTSELRRRPSHRARKPPGDrPPAAGPLRLEAPGPLKRT 354
Cdd:cd14180 229 SLEGEAWKGVSEEAKDLVRGLLTVDPAKR---------LK---LSELRESDWLQGGSALSS-TPLMTPDVLESSGPAVRT 295
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
59-316 5.12e-20

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: 88.87  E-value: 5.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNflrEVSITNSLSSSPfIIKVFDVvFETEDCYVFAQEYAPAG 134
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKvkgaKEREEVKN---EINIMNQLNHVN-LIQLYDA-FESKTNLTLIMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFD-IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVK-RVS-GT 211
Cdd:cd14192  87 ELFDrITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPREKlKVNfGT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPWEAASGADAF-FEEFVRWQRGrlpglPSQWRRFTEPALR 290
Cdd:cd14192 167 PEFLAPEVVN---YDFVSFPT--DMWSVGVITYMLLSGLSPFLGETDAETMnNIVNCKWDFD-----AEAFENLSEEAKD 236
                       250       260
                ....*....|....*....|....*.
gi 66773086 291 MFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14192 237 FISRLLVKEKSCRMSATQC---LKHE 259
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
53-307 6.13e-20

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: 89.10  E-value: 6.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKFVN---KSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCY- 124
Cdd:cd07860   2 FQKVEKIGEGTYG----VVYKArnklTGEVVALKKIRldtETEGVPSTAIREISLLKELNH-PNIVKLLDVIHTENKLYl 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDREcRRVKLADFGMTRRVGCR 204
Cdd:cd07860  77 VFEFLHQDLKKFMDASALT-GIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQN-LLINTE-GAIKLADFGLARAFGVP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEF--------VRWqrgr 273
Cdd:cd07860 154 VRTYTHevvTLWYRAPEILLGCK----YYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFrtlgtpdeVVW---- 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 274 lPGLPS---------QWRR---------FTEPALRMFQRLLALEPERRGPAK 307
Cdd:cd07860 226 -PGVTSmpdykpsfpKWARqdfskvvppLDEDGRDLLSQMLHYDPNKRISAK 276
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
52-314 6.35e-20

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: 89.28  E-value: 6.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSItNSLSSSPFIIKVFD-----VVFETEDCYV 125
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILcHSKEDVKEAMREIEN-YRLFNHPNILRLLDsqivkEAGGKKEVYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQeYAPAGDLFDIIP----PQVGLPEDTVKRCVQQLGLALDFMH---GRQLVHRDIKPENVLLFDRecRRVKLADFGMT 198
Cdd:cd13986  80 LLP-YYKRGSLQDEIErrlvKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSED--DEPILMDLGSM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRVGCRVKRVS------------GTIPYTAPEVCQAgrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAAsgadaffeef 266
Cdd:cd13986 157 NPARIEIEGRRealalqdwaaehCTMPYRAPELFDV--KSHCTIDEKTDIWSLGCTLYALMYGESPFERI---------- 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 267 vrWQRG---RLPGLPSQWR-----RFTEPALRMFQRLLALEPERRGPAKEVFRFLK 314
Cdd:cd13986 225 --FQKGdslALAVLSGNYSfpdnsRYSEELHQLVKSMLVVNPAERPSIDDLLSRVH 278
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
59-315 6.95e-20

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: 88.75  E-value: 6.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFV------NKSKTKLKNFL----REVSITNSLSSsPFIIKVFDVVFETEDCYVFAq 128
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsAENKDRKKSMLdalqREIALLRELQH-ENIVQYLGSSSDANHLNIFL- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV------- 201
Cdd:cd06628  86 EYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG--IKISDFGISKKLeanslst 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GCRVKRVS--GTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASGADAFFeefvRWQRGRLPGLPS 279
Cdd:cd06628 164 KNNGARPSlqGSVFWMAPEVVKQTSYTRKA-----DIWSLGCLVVEMLTGTHPFPDCTQMQAIF----KIGENASPTIPS 234
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 66773086 280 QwrrFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd06628 235 N---ISSEARDFLEKTFEIDHNKRPTADEL---LKH 264
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-253 7.81e-20

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: 89.04  E-value: 7.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKfvnKSKTKL----KNFLR---EVSITNSLSSsPFIIKVFDVVFETE-----DCYVF 126
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIK---KCRQELspsdKNRERwclEVQIMKKLNH-PNVVSARDVPPELEklspnDLPLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDII-PPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADFGMTRRV- 201
Cdd:cd13989  77 AMEYCSGGDLRKVLnQPEncCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGYAKELd 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd13989 157 qGSLCTSFVGTLQYLAPELFESKK-----YTCTVDYWSFGTLAFECITGYRPF 204
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
51-252 8.04e-20

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: 88.05  E-value: 8.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVdlvvYKGT-----------GTKMALK--FVNKSKTKLknfLREVSITNSLSSSPFIIKVFDVv 117
Cdd:cd14019   1 NKYRIIEKIGEGTFSSV----YKAEdklhdlydrnkGRLVALKhiYPTSSPSRI---LNELECLERLGGSNNVSGLITA- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 118 FETEDCYVFAQEYAPAGDLFDIIPpQVGLPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFGM 197
Cdd:cd14019  73 FRNEDQVVAVLPYIEHDDFRDFYR-KMSLTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGN-FLYNRETGKGVLVDFGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 198 TRRVGCRVKRVS---GTIPYTAPEV---CQAGradglavDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd14019 149 AQREEDRPEQRApraGTRGFRAPEVlfkCPHQ-------TTAIDIWSAGVILLSILSGRFP 202
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
54-275 8.23e-20

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: 88.56  E-value: 8.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCYVFAqEYAPA 133
Cdd:cd05072  10 KLVKKLGAGQFGEVWMGYYNNS-TKVAVKTLKPGTMSVQAFLEEANLMKTLQHDK-LVRLYAVVTKEEPIYIIT-EYMAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVG----LPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR---------R 200
Cdd:cd05072  87 GSLLDFLKSDEGgkvlLPK--LIDFSAQIAEGMAYIERKNYIHRDLRAANVLV--SESLMCKIADFGLARviedneytaR 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 201 VGCRVKrvsgtIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAffeeFVRWQRG-RLP 275
Cdd:cd05072 163 EGAKFP-----IKWTAPEAINFG-----SFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDV----MSALQRGyRMP 225
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
51-309 1.02e-19

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: 89.55  E-value: 1.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITN---SLSSSPFIIKVFDVVFETEDCYVfA 127
Cdd:cd05610   4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERdalALSKSPFIVHLYYSLQSANNVYL-V 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMT--------- 198
Cdd:cd05610  83 MEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEG--HIKLTDFGLSkvtlnreln 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 ---------------------------------------------RRVGCRV--KRVSGTIPYTAPEVCqAGRADGLAVD 231
Cdd:cd05610 161 mmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvRRGAARVegERILGTPDYLAPELL-LGKPHGPAVD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 232 TgvdvWAFGVLIFCVLTGNFPWEAASGADAF---FEEFVRWqrgrlpglPSQWRRFTEPALRMFQRLLALEPERRGPAKE 308
Cdd:cd05610 240 W----WALGVCLFEFLTGIPPFNDETPQQVFqniLNRDIPW--------PEGEEELSVNAQNAIEILLTMDPTKRAGLKE 307

                .
gi 66773086 309 V 309
Cdd:cd05610 308 L 308
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
51-242 1.15e-19

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: 88.55  E-value: 1.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVdlvvYKGTGTKMALKFVNKSKTKLK--------NFLREVSITNSLSS--SPFIIKVFDVVF-- 118
Cdd:cd07862   1 QQYECVAEIGEGAYGKV----FKARDLKNGGRFVALKRVRVQtgeegmplSTIREVAVLRHLETfeHPNVVRLFDVCTvs 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ----ETEDCYVFAQEYAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLAD 194
Cdd:cd07862  77 rtdrETKLTLVFEHVDQDLTTYLDKVP-EPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV--TSSGQIKLAD 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 195 FGMTRRVGCRV--KRVSGTIPYTAPEV-CQAGRAdglavdTGVDVWAFGVL 242
Cdd:cd07862 154 FGLARIYSFQMalTSVVVTLWYRAPEVlLQSSYA------TPVDLWSVGCI 198
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-257 1.16e-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: 87.72  E-value: 1.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN--KSKTKLKNFLREVSITNSLSSsPFIIkVFDVVFETEDCYVFAQEY 130
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRlpKSSSAVEDSRKEAVLLAKMKH-PNIV-AFKESFEADGHLYIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVGCRVKRV 208
Cdd:cd08219  80 CDGGDLMQKIKLQRGklFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFL-TQNG-KVKLGDFGSARLLTSPGAYA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 209 S---GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd08219 158 CtyvGTPYYVPPEIWE-----NMPYNNKSDIWSLGCILYELCTLKHPFQANS 204
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
51-244 1.26e-19

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: 88.12  E-value: 1.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFV--NKSKTKLKNFLREVsITNSLSSSPFIIKVFDVVFETEdcYVFAQ 128
Cdd:cd13996   6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIrlTEKSSASEKVLREV-KALAKLNHPNIVRYYTAWVEEP--PLYIQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 -EYAPAGDLFDIIPPQVGLP---EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGMTRRVGcR 204
Cdd:cd13996  83 mELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL-DNDDLQVKIGDFGLATSIG-N 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 205 VKRVS------------------GTIPYTAPEVCqagraDGLAVDTGVDVWAFGVLIF 244
Cdd:cd13996 161 QKRELnnlnnnnngntsnnsvgiGTPLYASPEQL-----DGENYNEKADIYSLGIILF 213
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
59-342 1.31e-19

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: 89.25  E-value: 1.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSSPFIIKVfDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKkvilNRKEQKHIMAERNVLLKNVKHPFLVGL-HYSFQTTDKLYFVLDFVNGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVkLADFGMTRRvGCRVKRVS----G 210
Cdd:cd05604  83 ELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILL-DSQGHIV-LTDFGLCKE-GISNSDTTttfcG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADaFFEEFVRWQRGRLPGLpsqwrrfTEPALR 290
Cdd:cd05604 160 TPEYLAPEVIRKQ-----PYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAE-MYENILHKPLVLRPGI-------SLTAWS 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 291 MFQRLLALEPERRGPAKEVFRFLK-HELTSELRRRPSHRARKPPGDRPPAAGP 342
Cdd:cd05604 227 ILEELLEKDRQLRLGAKEDFLEIKnHPFFESINWTDLVQKKIPPPFNPNVNGP 279
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
49-309 1.45e-19

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: 88.29  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELV--RELGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKlknflREVSITNSLSSSPFIIKVFDVV-----FET 120
Cdd:cd14171   2 ILEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKiLLDRPKAR-----TEVRLHMMCSGHPNIVQIYDVYansvqFPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDC----YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR-ECRRVKLADF 195
Cdd:cd14171  77 ESSprarLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNsEDAPIKLCDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 196 GMTRRVGCRVKRVSGTIPYTAPEVCQAGRADGL------------AVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFF 263
Cdd:cd14171 157 GFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHRKersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTIT 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 264 EEFVRWQRGRLPGLPS-QWRRFTEPALRMFQRLLALEPERRGPAKEV 309
Cdd:cd14171 237 KDMKRKIMTGSYEFPEeEWSQISEMAKDIVRKLLCVDPEERMTIEEV 283
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
52-245 1.89e-19

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: 88.74  E-value: 1.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSsPFIIKVFDVV-------FEte 121
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfdDLIDAKRILREIKILRHLKH-ENIIGLLDILrppspeeFN-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVfAQEYAPAgDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRV 201
Cdd:cd07834  78 DVYI-VTELMET-DLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILV-NSNC-DLKICDFGLARGV 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 202 GCR----------VKRVsgtipYTAPEVCqagrADGLAVDTGVDVWAFGVlIFC 245
Cdd:cd07834 154 DPDedkgflteyvVTRW-----YRAPELL----LSSKKYTKAIDIWSVGC-IFA 197
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
52-304 2.21e-19

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: 88.53  E-value: 2.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSS---SPFIIKVFdVVFETEDCYVFAQ 128
Cdd:cd05598   2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAeadNEWVVKLY-YSFQDKENLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPpQVGLPEDTVKRC-VQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTrrVGCRVKR 207
Cdd:cd05598  81 DYIPGGDLMSLLI-KKGIFEEDLARFyIAELVCAIESVHKMGFIHRDIKPDNILI-DRD-GHIKLTDFGLC--TGFRWTH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VS---------GTIPYTAPEVcqagradgLAVdTG----VDVWAFGVLIFCVLTGNFPWEAASGADAfFEEFVRWQRG-R 273
Cdd:cd05598 156 DSkyylahslvGTPNYIAPEV--------LLR-TGytqlCDWWSVGVILYEMLVGQPPFLAQTPAET-QLKVINWRTTlK 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 66773086 274 LPGLPsqwrRFTEPALRMFQRLLALEPERRG 304
Cdd:cd05598 226 IPHEA----NLSPEAKDLILRLCCDAEDRLG 252
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
49-247 2.56e-19

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: 87.56  E-value: 2.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGkvdlVVYKG----TGTKMALKFVNKSKtKLKNflREVSITNSLSSsPFIIKVFDVVFETED-- 122
Cdd:cd14137   2 VEISYTIEKVIGSGSFG----VVYQAklleTGEVVAIKKVLQDK-RYKN--RELQIMRRLKH-PNIVKLKYFFYSSGEkk 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 ---CYVFAQEYAPaGDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADF 195
Cdd:cd14137  74 devYLNLVMEYMP-ETLYRVIrhysKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQN-LLVDPETGVLKLCDF 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 196 GmtrrvgcRVKRVSGTIP---------YTAPEV---CQagradglAVDTGVDVWAFGvlifCVL 247
Cdd:cd14137 152 G-------SAKRLVPGEPnvsyicsryYRAPELifgAT-------DYTTAIDIWSAG----CVL 197
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
52-244 2.67e-19

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: 87.34  E-value: 2.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALK--FVNkSKTKLKNFLREVSITNSLSSSPFIIKVFDV--------VFEte 121
Cdd:cd14037   4 HVTIEKYLAEGGFAHVYLVKTSNGGNRAALKrvYVN-DEHDLNVCKREIEIMKRLSGHKNIVGYIDSsanrsgngVYE-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 dCYVFaQEYAPAGDLFDIIPP--QVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLFDRecRRVKLADFGM 197
Cdd:cd14037  81 -VLLL-MEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDS--GNYKLCDFGS 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 198 TRRVGCRVKRVSG------------TIPYTAPEVCQAGRadGLAVDTGVDVWAFGVLIF 244
Cdd:cd14037 157 ATTKILPPQTKQGvtyveedikkytTLQYRAPEMIDLYR--GKPITEKSDIWALGCLLY 213
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
53-247 3.18e-19

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: 87.38  E-value: 3.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFV---NKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQE 129
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDRETGETVALKKValrKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVL-VFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPaGDLFDIIPPQV-GLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRVKRV 208
Cdd:cd07832  81 YML-SSLSEVLRDEErPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG--VLKIADFGLARLFSEEDPRL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 66773086 209 S----GTIPYTAPEVCQAGRadglAVDTGVDVWAFGvlifCVL 247
Cdd:cd07832 158 YshqvATRWYRAPELLYGSR----KYDEGVDLWAVG----CIF 192
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
53-315 3.58e-19

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: 86.56  E-value: 3.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKFVN-------KSKTKLknfLREVSITNSLSSsPFIIKVFDVVFETE 121
Cdd:cd08224   2 YEIEKKIGKGQFS----VVYRArcllDGRLVALKKVQifemmdaKARQDC---LKEIDLLQQLNH-PNIIKYLASFIENN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVfAQEYAPAGDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVllFDRECRRVKLADFGM 197
Cdd:cd08224  74 ELNI-VLELADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANV--FITANGVVKLGDLGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCR---VKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGvlifCVLtgnfpWEAASGADAFFEE-------FV 267
Cdd:cd08224 151 GRFFSSKttaAHSLVGTPYYMSPERIR-----EQGYDFKSDIWSLG----CLL-----YEMAALQSPFYGEkmnlyslCK 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 268 RWQRGRLPGLPSQwrRFTEPALRMFQRLLALEPERRGPAKEVFRFLKH 315
Cdd:cd08224 217 KIEKCEYPPLPAD--LYSQELRDLVAACIQPDPEKRPDISYVLDVAKR 262
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
53-315 3.93e-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: 87.79  E-value: 3.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK------SKTKLKNFLREVSITnslSSSPFIIKVFdVVFETEDCYVF 126
Cdd:cd05597   3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKwemlkrAETACFREERDVLVN---GDRRWITKLH-YAFQDENYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDReCRRVKLADFGMTRRV---G 202
Cdd:cd05597  79 VMDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL-DR-NGHIRLADFGSCLKLredG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVS-GTIPYTAPEVCQAgRADGLAV-DTGVDVWAFGVLIFCVLTGNFPWEAASGADAF-----FEEFVRwqrgrlp 275
Cdd:cd05597 157 TVQSSVAvGTPDYISPEILQA-MEDGKGRyGPECDWWSLGVCMYEMLYGETPFYAESLVETYgkimnHKEHFS------- 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 276 gLPSQWRRFTEPALRMFQRLLAlEPERRGPAKEVFRFLKH 315
Cdd:cd05597 229 -FPDDEDDVSEEAKDLIRRLIC-SRERRLGQNGIDDFKKH 266
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
53-315 6.13e-19

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: 86.32  E-value: 6.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKfvnksKTKLKN--------FLREVSITNSLSSsPFIIKVFDVVFET 120
Cdd:cd07861   2 YTKIEKIGEGTYG----VVYKGrnkkTGQIVAMK-----KIRLESeeegvpstAIREISLLKELQH-PNIVCLEDVLMQE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCY-VFaqEYAPAgDL---FDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFG 196
Cdd:cd07861  72 NRLYlVF--EFLSM-DLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV--IKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCRVkRVSG----TIPYTAPEVCQAGRadglAVDTGVDVWAFGVL----------------------IFCVL--T 248
Cdd:cd07861 147 LARAFGIPV-RVYThevvTLWYRAPEVLLGSP----RYSTPVDIWSIGTIfaematkkplfhgdseidqlfrIFRILgtP 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 249 GNFPWEAASGADAFFEEFVRWQRGrlpGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd07861 222 TEDIWPGVTSLPDYKNTFPKWKKG---SLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKA---LVH 282
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
53-247 6.29e-19

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: 85.78  E-value: 6.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSP-----FIIKVFDVVFETED-CYVF 126
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDkadkyHIVRLKDVFYFKNHlCIVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 A-QEYapagDLFDIIP--PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFG----MTR 199
Cdd:cd14133  81 ElLSQ----NLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGsscfLTQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 200 RVGCRVKRVSgtipYTAPEVCQagradGLAVDTGVDVWAFGvlifCVL 247
Cdd:cd14133 157 RLYSYIQSRY----YRAPEVIL-----GLPYDEKIDMWSLG----CIL 191
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
53-311 6.99e-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: 85.94  E-value: 6.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYK-GTGTKMALKFVNKSKTKLKNFLR---EVSITNSLSS--SPFIIKVFDVvFETEDCYVF 126
Cdd:cd14052   2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRrleEVSILRELTLdgHDNIVQLIDS-WEYHGHLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLfDIIPPQVG----LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGMTRRV 201
Cdd:cd14052  81 QTELCENGSL-DVFLSELGllgrLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLItFEGT---LKIGDFGMATVW 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GC-RVKRVSGTIPYTAPEVCqagrADGLaVDTGVDVWAFGVLIF-----CVLTGN-FPWEAASGADafFEEFVRWQRGRL 274
Cdd:cd14052 157 PLiRGIEREGDREYIAPEIL----SEHM-YDKPADIFSLGLILLeaaanVVLPDNgDAWQKLRSGD--LSDAPRLSSTDL 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 275 PGLPSQWR----------RFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14052 230 HSASSPSSnpppdppnmpILSGSLDRVVRWMLSPEPDRRPTADDVLA 276
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-303 7.15e-19

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: 85.85  E-value: 7.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKnflrEVSITNSLS-----SSPFIIKVFDVvFETEDC 123
Cdd:cd14167   1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGK----ETSIENEIAvlhkiKHPNIVALDDI-YESGGH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD-RECRRVKLADFGMTR--R 200
Cdd:cd14167  76 LYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSlDEDSKIMISDFGLSKieG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCRVKRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADaFFEEFVrwqRGRLPGLPSQ 280
Cdd:cd14167 156 SGSVMSTACGTPGYVAPEVLAQK-----PYSKAVDCWSIGVIAYILLCGYPPFYDENDAK-LFEQIL---KAEYEFDSPY 226
                       250       260
                ....*....|....*....|...
gi 66773086 281 WRRFTEPALRMFQRLLALEPERR 303
Cdd:cd14167 227 WDDISDSAKDFIQHLMEKDPEKR 249
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-249 1.22e-18

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: 86.06  E-value: 1.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL-----SSSPFIIKVFD---------VVF 118
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLndndpDDKHNIVRYKDsfifrghlcIVF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCyvfaqeyapagDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFG 196
Cdd:cd14210  95 ELLSI-----------NLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFG 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 197 MtrrvGCRVkrvsGTIPYT--------APEVCQagradGLAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd14210 164 S----SCFE----GEKVYTyiqsrfyrAPEVIL-----GLPYDTAIDMWSLGCILAELYTG 211
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-257 1.53e-18

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: 84.62  E-value: 1.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNflREVS----ITNSLSSSPFIIKVFDVVFETEDCYVfAQ 128
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKE--KEASkkevILLAKMKHPNIVTFFASFQENGRLFI-VM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGL--PEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGMTRRVGCRV- 205
Cdd:cd08225  79 EYCDGGDLMKRINRQRGVlfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFL-SKNGMVAKLGDFGIARQLNDSMe 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 206 --KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd08225 158 laYTCVGTPYYLSPEICQ-----NRPYNNKTDIWSLGCVLYELCTLKHPFEGNN 206
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-303 1.56e-18

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: 84.94  E-value: 1.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL--REVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEY 130
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMveNEIAVLRRINH-ENIVSLEDI-YESPTHLYLAMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDR--ECRRVKLADFGMTR-RVGCRVKR 207
Cdd:cd14169  83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPEN-LLYATpfEDSKIMISDFGLSKiEAQGMLST 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 VSGTIPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTGNFPWEAASGAdaffEEFVRWQRGRLPGLPSQWRRF 284
Cdd:cd14169 162 ACGTPGYVAPELLEQkpyGKA--------VDVWAIGVISYILLCGYPPFYDENDS----ELFNQILKAEYEFDSPYWDDI 229
                       250
                ....*....|....*....
gi 66773086 285 TEPALRMFQRLLALEPERR 303
Cdd:cd14169 230 SESAKDFIRHLLERDPEKR 248
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
58-316 1.94e-18

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: 84.42  E-value: 1.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL-REVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEYAPAGDL 136
Cdd:cd06648  14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLfNEVVIMRDYQH-PNIVEMYSSYLVGDELWV-VMEFLEGGAL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRV-KRVS--GTIP 213
Cdd:cd06648  92 TDIVT-HTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILL--TSDGRVKLSDFGFCAQVSKEVpRRKSlvGTPY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 214 YTAPEVCQAgradgLAVDTGVDVWAFGVLIFcvltgnfpwEAASGADAFFEE--FVRWQRGRLPGLP-SQWRRFTEPALR 290
Cdd:cd06648 169 WMAPEVISR-----LPYGTEVDIWSLGIMVI---------EMVDGEPPYFNEppLQAMKRIRDNEPPkLKNLHKVSPRLR 234
                       250       260
                ....*....|....*....|....*..
gi 66773086 291 MF-QRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd06648 235 SFlDRMLVRDPAQRATAAEL---LNHP 258
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
52-311 2.03e-18

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: 84.69  E-value: 2.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFV-----NKSKTKLKNFLR-EVSITNSLSSSPfIIKVFDVVFETED--C 123
Cdd:cd06653   3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKEVNALEcEIQLLKNLRHDR-IVQYYGCLRDPEEkkL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAqEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLlfdRECR-RVKLADFGMTRRV- 201
Cdd:cd06653  82 SIFV-EYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL---RDSAgNVKLGDFGASKRIq 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -----GCRVKRVSGTIPYTAPEVCqagraDGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPG 276
Cdd:cd06653 158 ticmsGTGIKSVTGTPYWMSPEVI-----SGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPQLPD 232
                       250       260       270
                ....*....|....*....|....*....|....*
gi 66773086 277 LPSQwrrftepALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd06653 233 GVSD-------ACRDFLRQIFVEEKRRPTAEFLLR 260
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
59-372 2.26e-18

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: 85.41  E-value: 2.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVfDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtilkKKEQNHIMAERNVLLKNLKHPFLVGL-HYSFQTSEKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdrECR-RVKLADFGMTRRvGCRVKRVS---- 209
Cdd:cd05603  82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL---DCQgHVVLTDFGLCKE-GMEPEETTstfc 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 210 GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRLPGLPsqwrrfTEPAL 289
Cdd:cd05603 158 GTPEYLAPEVLRKE-----PYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMY--DNILHKPLHLPGGK------TVAAC 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 290 RMFQRLLALEPERRGPAKEVFRFLK-HELTSELRRRPSHRARKPPGDRPPAAGP--LRLEAPGPLKRTVLTESGSGSRPA 366
Cdd:cd05603 225 DLLQGLLHKDQRRRLGAKADFLEIKnHVFFSPINWDDLYHKRITPPYNPNVAGPadLRHFDPEFTQEAVPHSVGRTPDLT 304

                ....*.
gi 66773086 367 PPAVGS 372
Cdd:cd05603 305 ASSSSS 310
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
59-311 2.54e-18

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: 84.48  E-value: 2.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKfvnksKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFaQEYAPAGDLFD 138
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVK-----KVRLEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIF-MDLKEGGSLGQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDrECRRVKLADFGMTRRV-----GCRVKR---VSG 210
Cdd:cd13991  88 LIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSS-DGSDAFLCDFGHAECLdpdglGKSLFTgdyIPG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVcqagrADGLAVDTGVDVWAFGVLIFCVLTGNFPWeaasgadaffeefVRWQRGRL--------PGL---PS 279
Cdd:cd13991 167 TETHMAPEV-----VLGKPCDAKVDVWSSCCMMLHMLNGCHPW-------------TQYYSGPLclkianepPPLreiPP 228
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 280 QWRRFTEPALRMFqrlLALEPERRGPAKEVFR 311
Cdd:cd13991 229 SCAPLTAQAIQAG---LRKEPVHRASAAELRR 257
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
53-304 2.58e-18

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 86.22  E-value: 2.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSSpfIIKVFDVVFETEDCYVFAQ 128
Cdd:cd05623  74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKwemlKRAETACFREERDVLVNGDSQ--WITTLHYAFQDDNNLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV---GCR 204
Cdd:cd05623 152 DYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM-DMN-GHIRLADFGSCLKLmedGTV 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVS-GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRlpgLPSQWRR 283
Cdd:cd05623 230 QSSVAvGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQ---FPTQVTD 306
                       250       260
                ....*....|....*....|.
gi 66773086 284 FTEPALRMFQRLLALEPERRG 304
Cdd:cd05623 307 VSENAKDLIRRLICSREHRLG 327
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
49-315 2.69e-18

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: 84.10  E-value: 2.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRE-LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTklknFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFA 127
Cdd:cd14109   1 VRELYEIGEEdEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF----LMREVDIHNSLDH-PNIVQMHDAYDDEKLAVTVI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLF-DIIPPQVGL-PEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecrRVKLADFGMTRRVgcrV 205
Cdd:cd14109  76 DNLASTIELVrDNLLPGKDYyTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD---KLKLADFGQSRRL---L 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEaasgADAFFEEFVRWQRGRLPGLPSQWRRFT 285
Cdd:cd14109 150 RGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFL----GDNDRETLTNVRSGKWSFDSSPLGNIS 225
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 286 EPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd14109 226 DDARDFIKKLLVYIPESRLTVDEA---LNH 252
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
128-268 2.91e-18

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: 83.95  E-value: 2.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLF-DRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd14012  83 TEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDrDAGTGIVKLTDYSLGKTLLDMCS 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 207 RVSGTI----PYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASGADAF---------FEEFVR 268
Cdd:cd14012 163 RGSLDEfkqtYWLPPELAQGSKSPTRK----TDVWDLGLLFLQMLFGLDVLEKYTSPNPVlvsldlsasLQDFLS 233
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
52-243 2.99e-18

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: 84.31  E-value: 2.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSITNSlSSSPFIIKVFDVVFETEDCYVFAqEY 130
Cdd:cd06643   6 FWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDtKSEEELEDYMVEIDILAS-CDHPNIVKLLDAFYYENNLWILI-EF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 ApAGDLFDIIPPQVGLP--EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGMTRRVGCRVKR 207
Cdd:cd06643  84 C-AGGAVDAVMLELERPltEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFtLDGD---IKLADFGVSAKNTRTLQR 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 66773086 208 VS---GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLI 243
Cdd:cd06643 160 RDsfiGTPYWMAPEVVMCETSKDRPYDYKADVWSLGVTL 198
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
59-253 3.21e-18

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: 83.47  E-value: 3.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAPAGDLFD 138
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQH-PQYITLHDT-YESPTSYILVLELMDDGRLLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADFGMTRRVGC--RVKRVSGTIPYT 215
Cdd:cd14115  79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGhrHVHHLLGNPEFA 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 66773086 216 APEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14115 159 APEVIQ-----GTPVSLATDIWSIGVLTYVMLSGVSPF 191
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
46-311 3.23e-18

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 84.71  E-value: 3.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  46 ASDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKnflrEVSITNSLSSSPFI----IKVFDVVFETE 121
Cdd:cd14168   5 VEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGK----ESSIENEIAVLRKIkhenIVALEDIYESP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD-RECRRVKLADFGMTRR 200
Cdd:cd14168  81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSqDEESKIMISDFGLSKM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCR--VKRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADaFFEEFVrwqRGRLPGLP 278
Cdd:cd14168 161 EGKGdvMSTACGTPGYVAPEVLAQK-----PYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQIL---KADYEFDS 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 279 SQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14168 232 PYWDDISDSAKDFIRNLMEKDPNKRYTCEQALR 264
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
51-311 3.37e-18

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: 84.06  E-value: 3.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVrelGKGTYGkvdlVVYKG----TGTKMALKFVN--KSKTKLKNFLREVSITNSL--SSSPFIIKVFDVVFETED 122
Cdd:cd06917   4 RRLELV---GRGSYG----AVYRGyhvkTGRVVALKVLNldTDDDDVSDIQKEVALLSQLklGQPKNIIKYYGSYLKGPS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVfAQEYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVG 202
Cdd:cd06917  77 LWI-IMDYCEGGSIRTLMRAG-PIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILV--TNTGNVKLCDFGVAASLN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 C-RVKRVS--GTIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWeaaSGADAF--FEEFVRWQRGRLPGl 277
Cdd:cd06917 153 QnSSKRSTfvGTPYWMAPEVITEGK----YYDTKADIWSLGITTYEMATGNPPY---SDVDALraVMLIPKSKPPRLEG- 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 66773086 278 psqwrRFTEPALRMFQRL-LALEPERRGPAKEVFR 311
Cdd:cd06917 225 -----NGYSPLLKEFVAAcLDEEPKDRLSADELLK 254
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
53-316 3.59e-18

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: 84.20  E-value: 3.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKfvnksktKLKNF----------LREVSITNSLSSsPFIIKVFDVVF 118
Cdd:cd07843   7 YEKLNRIEEGTYG----VVYRArdkkTGEIVALK-------KLKMEkekegfpitsLREINILLKLQH-PNIVTVKEVVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVF-AQEYAP--AGDLFDIIPPQVGLPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADF 195
Cdd:cd07843  75 GSNLDKIYmVMEYVEhdLKSLMETMKQPFLQSE--VKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRG--ILKICDF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 196 GMTRRVGCRVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWA----FGVL------------------IFCVLTG- 249
Cdd:cd07843 151 GLAREYGSPLKPYTQlvvTLWYRAPELLLGAK----EYSTAIDMWSvgciFAELltkkplfpgkseidqlnkIFKLLGTp 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086 250 ---NFP-WEAASGADAF-FEEFVRWQ-RGRLPGLpsqwrRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd07843 227 tekIWPgFSELPGAKKKtFTKYPYNQlRKKFPAL-----SLSDNGFDLLNRLLTYDPAKRISAEDA---LKHP 291
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
48-314 4.96e-18

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: 83.44  E-value: 4.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfA 127
Cdd:cd06647   4 DPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWV-V 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPP---QVGLPEDTVKRCVQqlglALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGMTRRVGC 203
Cdd:cd06647  83 MEYLAGGSLTDVVTEtcmDEGQIAAVCRECLQ----ALEFLHSNQVIHRDIKSDNILLgMDGS---VKLTDFGFCAQITP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVS---GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeeFVRWQRGRlPGLPSq 280
Cdd:cd06647 156 EQSKRStmvGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL---YLIATNGT-PELQN- 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 66773086 281 wRRFTEPALRMF-QRLLALEPERRGPAKEVFR--FLK 314
Cdd:cd06647 226 -PEKLSAIFRDFlNRCLEMDVEKRGSAKELLQhpFLK 261
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-253 5.12e-18

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: 83.86  E-value: 5.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVnKSKTKLKNFLR---EVSITNSLSSsPFIIKVFDVV-----FETEDCYVFAQEY 130
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQC-RQELSPKNRERwclEIQIMKRLNH-PNVVAARDVPeglqkLAPNDLPLLAMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDL---FDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADFGMTRRV--GCR 204
Cdd:cd14038  80 CQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKIIDLGYAKELdqGSL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66773086 205 VKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14038 160 CTSFVGTLQYLAPELLEQQK-----YTVTVDYWSFGTLAFECITGFRPF 203
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
82-316 5.19e-18

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: 83.54  E-value: 5.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  82 KFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLA 161
Cdd:cd14088  33 KFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDV-FETRKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 162 LDFMHGRQLVHRDIKPENVLLFDR-ECRRVKLADFGMTRRVGCRVKRVSGTIPYTAPEVC---QAGRAdglavdtgVDVW 237
Cdd:cd14088 112 VAYLHSLKIVHRNLKLENLVYYNRlKNSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVgrqRYGRP--------VDCW 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 238 AFGVLIFCVLTGNFPWEAASGADAFFEE----FVRWQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVfrfL 313
Cdd:cd14088 184 AIGVIMYILLSGNPPFYDEAEEDDYENHdknlFRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEA---I 260

                ...
gi 66773086 314 KHE 316
Cdd:cd14088 261 SHE 263
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
39-283 5.49e-18

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: 83.89  E-value: 5.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  39 LTLRTLAasDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVF 118
Cdd:cd06639  12 LGLESLA--DPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETeDCYVFAQ-----EYAPAGDLFDIIppqvglpeDTVKRCVQQLG------------LALDFMHGRQLVHRDIKPENVL 181
Cdd:cd06639  90 KA-DQYVGGQlwlvlELCNGGSVTELV--------KGLLKCGQRLDeamisyilygalLGLQHLHNNRIIHRDVKGNNIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 182 LFDREcrRVKLADFGMTRRV-GCRVKRVS--GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASG 258
Cdd:cd06639 161 LTTEG--GVKLVDFGVSAQLtSARLRRNTsvGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHP 238
                       250       260
                ....*....|....*....|....*..
gi 66773086 259 ADAFFeefvRWQRGRLPGL--PSQWRR 283
Cdd:cd06639 239 VKALF----KIPRNPPPTLlnPEKWCR 261
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
53-249 5.59e-18

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: 84.20  E-value: 5.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFdVVFETEDCYVFAQE 129
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDIlaeADNPWVVKLY-YSFQDEENLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLF------DIippqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDREcRRVKLADFGMTRRVGC 203
Cdd:cd05599  82 FLPGGDMMtllmkkDT------LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDN-LLLDAR-GHIKLSDFGLCTGLKK 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66773086 204 RVKRVS--GTIPYTAPEV-CQAGRADglavdtGVDVWAFGVLIFCVLTG 249
Cdd:cd05599 154 SHLAYStvGTPDYIAPEVfLQKGYGK------ECDWWSLGVIMYEMLIG 196
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
41-314 5.64e-18

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: 84.01  E-value: 5.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  41 LRTLAA-SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL-REVSITNSLSSsPFIIKVFDVVF 118
Cdd:cd06655   8 LRTIVSiGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIiNEILVMKELKN-PNIVNFLDSFL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVfAQEYAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMT 198
Cdd:cd06655  87 VGDELFV-VMEYLAGGSLTDVVT-ETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDG--SVKLTDFGFC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRVGCRVKRVS---GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRwqrgrlp 275
Cdd:cd06655 163 AQITPEQSKRStmvGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN------- 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 276 GLPS-QWRRFTEPALRMF-QRLLALEPERRGPAKEVFR--FLK 314
Cdd:cd06655 231 GTPElQNPEKLSPIFRDFlNRCLEMDVEKRGSAKELLQhpFLK 273
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
41-314 6.30e-18

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: 83.62  E-value: 6.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  41 LRTLAA-SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFE 119
Cdd:cd06656   8 LRSIVSvGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 TEDCYVfAQEYAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGMT 198
Cdd:cd06656  88 GDELWV-VMEYLAGGSLTDVVT-ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGS---VKLTDFGFC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRVGCRVKRVS---GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFF-------EEFVR 268
Cdd:cd06656 163 AQITPEQSKRStmvGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYliatngtPELQN 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 269 WQRgrlpgLPSQWRRFtepalrmFQRLLALEPERRGPAKEVFR--FLK 314
Cdd:cd06656 238 PER-----LSAVFRDF-------LNRCLEMDVDRRGSAKELLQhpFLK 273
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
51-333 6.77e-18

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: 84.70  E-value: 6.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREV-------SITNslssSPFIIKVFDVVFETEDC 123
Cdd:cd05600  11 SDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVlterdilTTTN----SPWLVKLLYAFQDPENV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YvFAQEYAPAGDlFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMT---- 198
Cdd:cd05600  87 Y-LAMEYVPGGD-FRTLLNNSGiLSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLI-DSS-GHIKLTDFGLAsgtl 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 ---------------------------RRVGCR---------VKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVL 242
Cdd:cd05600 163 spkkiesmkirleevkntafleltakeRRNIYRamrkedqnyANSVVGSPDYMAPEVLR-----GEGYDLTVDYWSLGCI 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 243 IFCVLTGnFPWEAASGADAFFEEFVRWQRgrlpglPSQWRRFTEPALRM--------FQRLLALEPERRGPAKEVFR--- 311
Cdd:cd05600 238 LFECLVG-FPPFSGSTPNETWANLYHWKK------TLQRPVYTDPDLEFnlsdeawdLITKLITDPQDRLQSPEQIKnhp 310
                       330       340
                ....*....|....*....|..
gi 66773086 312 FLKHELTSELRRRPshrarKPP 333
Cdd:cd05600 311 FFKNIDWDRLREGS-----KPP 327
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
57-303 7.53e-18

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: 82.49  E-value: 7.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKF--VNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEYAPAG 134
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKTcrETLPPDLKRKFLQEARILKQYDH-PNIVKLIGVCVQKQPIMI-VMELVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVglPEDTVKrcvQQLGLALD------FMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRVKRV 208
Cdd:cd05041  79 SLLTFLRKKG--ARLTVK---QLLQMCLDaaagmeYLESKNCIHRDLAARNCLVGENNV--LKISDFGMSREEEDGEYTV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 S---GTIP--YTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLT-GNFPWEAASGADAffEEFVrwQRG-RLP---GLP 278
Cdd:cd05041 152 SdglKQIPikWTAPEALNYGRYTSES-----DVWSFGILLWEIFSlGATPYPGMSNQQT--REQI--ESGyRMPapeLCP 222
                       250       260
                ....*....|....*....|....*
gi 66773086 279 sqwrrftEPALRMFQRLLALEPERR 303
Cdd:cd05041 223 -------EAVYRLMLQCWAYDPENR 240
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
59-262 7.56e-18

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: 84.28  E-value: 7.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAPAG 134
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDELYAIKILKKdvviQDDDVECTMVEKRVLALQDKPPFLTQLHSC-FQTVDRLYFVMEYVNGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPpQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR---VGCRVKRVSG 210
Cdd:cd05615  97 DLMYHIQ-QVGkFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML-DSE-GHIKIADFGMCKEhmvEGVTTRTFCG 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 211 TIPYTAPEVCQ---AGRAdglavdtgVDVWAFGVLIFCVLTGNFPWEAASGADAF 262
Cdd:cd05615 174 TPDYIAPEIIAyqpYGRS--------VDWWAYGVLLYEMLAGQPPFDGEDEDELF 220
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
59-315 7.91e-18

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: 82.87  E-value: 7.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKG---TGTKMALKFV-------NKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCYVFaQ 128
Cdd:cd06631   9 LGKGAYGTV----YCGltsTGQLIAVKQVeldtsdkEKAEKEYEKLQEEVDLLKTLKHVN-IVGYLGTCLEDNVVSIF-M 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRVKRV 208
Cdd:cd06631  83 EFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV--IKLIDFGCAKRLCINLSSG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 S---------GTIPYTAPEVCQagradglavDTG----VDVWAFGVLIFCVLTGNFPWEAASGADAFFeeFVRWQRGRLP 275
Cdd:cd06631 161 SqsqllksmrGTPYWMAPEVIN---------ETGhgrkSDIWSIGCTVFEMATGKPPWADMNPMAAIF--AIGSGRKPVP 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 276 GLPSqwrRFTEPALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd06631 230 RLPD---KFSPEARDFVHACLTRDQDERPSAEQL---LKH 263
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
53-253 8.21e-18

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: 82.79  E-value: 8.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN------KSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVF 126
Cdd:cd06625   2 WKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEidpintEASKEVKALECEIQLLKNLQH-ERIVQYYGCLQDEKSLSIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLlfdRECR-RVKLADFGMTRRV---- 201
Cdd:cd06625  81 -MEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL---RDSNgNVKLGDFGASKRLqtic 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQA---GRAdglavdtgVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd06625 157 sSTGMKSVTGTPYWMSPEVINGegyGRK--------ADIWSVGCTVVEMLTTKPPW 204
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
52-248 8.77e-18

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: 82.48  E-value: 8.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKV---------DLVVYKGTGTKMAlkfvnkSKTKLKNFLREVSITnSLSSSPFIIKVFDVVFETED 122
Cdd:cd08221   1 HYIPVRVLGRGAFGEAvlyrktednSLVVWKEVNLSRL------SEKERRDALNEIDIL-SLLNHDNIITYYNHFLDGES 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVfAQEYAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRR 200
Cdd:cd08221  74 LFI-EMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADL--VKLGDFGISKV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 201 VGCR---VKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLT 248
Cdd:cd08221 151 LDSEssmAESIVGTPYYMSPELVQ-----GVKYNFKSDIWAVGCVLYELLT 196
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
54-328 8.97e-18

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: 83.19  E-value: 8.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS--KTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYA 131
Cdd:cd06618  18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSgnKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELMS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGD-LFDIIppQVGLPEDTVKRCVQQLGLALDFM---HGrqLVHRDIKPENVLLFDRECrrVKLADFGMT-RRVGCRVK 206
Cdd:cd06618  98 TCLDkLLKRI--QGPIPEDILGKMTVSIVKALHYLkekHG--VIHRDVKPSNILLDESGN--VKLCDFGISgRLVDSKAK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 -RVSGTIPYTAPEVCQAGRADglAVDTGVDVWAFGVLIFCVLTGNFPWEaasGADAFFEEFVRWQRGRLPGLPSQwRRFT 285
Cdd:cd06618 172 tRSAGCAAYMAPERIDPPDNP--KYDIRADVWSLGISLVELATGQFPYR---NCKTEFEVLTKILNEEPPSLPPN-EGFS 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 286 EpalrMFQrllaleperrgpakevfRFLKHELTSELRRRPSHR 328
Cdd:cd06618 246 P----DFC-----------------SFVDLCLTKDHRYRPKYR 267
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
51-308 1.02e-17

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: 83.19  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGkvdlVVYKG----TGTKMALKFV--NKSKTKLK-NFLREVSITNSLSSsPFIIKVFDVVFETEDC 123
Cdd:cd07845   7 TEFEKLNRIGEGTYG----IVYRArdttSGEIVALKKVrmDNERDGIPiSSLREITLLLNLRH-PNIVELKEVVVGKHLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVF-AQEYAPA--GDLFDIIPPQvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRR 200
Cdd:cd07845  82 SIFlVMEYCEQdlASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC--LKIADFGLART 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCRVKRVSG---TIPYTAPEVCQAGRADglavDTGVDVWAFGVLIFCVLTGNFPWEAASGADAF--------------- 262
Cdd:cd07845 158 YGLPAKPMTPkvvTLWYRAPELLLGCTTY----TTAIDMWAVGCILAELLAHKPLLPGKSEIEQLdliiqllgtpnesiw 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 263 --FEEFVRWQRGRLPGLPSQW--RRFT---EPALRMFQRLLALEPERRGPAKE 308
Cdd:cd07845 234 pgFSDLPLVGKFTLPKQPYNNlkHKFPwlsEAGLRLLNFLLMYDPKKRATAEE 286
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
59-317 1.02e-17

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: 82.46  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGTG----------TKMALKFVNKSKT--KLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVF 126
Cdd:cd05044   3 LGSGAFGEV----FEGTAkdilgdgsgeTKVAVKTLRKGATdqEKAEFLKEAHLMSNFKH-PNILKLLGVCLDNDPQYII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aQEYAPAGDLFDII---------PPQVGLPE------DTVKRCVQqlglaLDFMHgrqLVHRDIKPENVLLFDRECRR-- 189
Cdd:cd05044  78 -LELMEGGDLLSYLraarptaftPPLLTLKDllsicvDVAKGCVY-----LEDMH---FVHRDLAARNCLVSSKDYRErv 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 190 VKLADFGMTR---RVGCRVKRVSGTIP--YTAPEvcqaGRADGLaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAFf 263
Cdd:cd05044 149 VKIGDFGLARdiyKNDYYRKEGEGLLPvrWMAPE----SLVDGV-FTTQSDVWAFGVLMWEILTlGQQPYPARNNLEVL- 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 264 eEFVRwQRGRLpglpSQWRRFTEPALRMFQRLLALEPERRgPAkevFRFLKHEL 317
Cdd:cd05044 223 -HFVR-AGGRL----DQPDNCPDDLYELMLRCWSTDPEER-PS---FARILEQL 266
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
57-275 1.60e-17

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: 81.63  E-value: 1.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVY---KGTGTKMALKFV--NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfaQEYA 131
Cdd:cd05060   1 KELGHGNFGSVRKGVYlmkSGKEVEVAVKTLkqEHEKAGKKEFLREASVMAQLDH-PCIVRLIGVCKGEPLMLV--MELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGC-----RVK 206
Cdd:cd05060  78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH--QAKISDFGMSRALGAgsdyyRAT 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 207 RvSGTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAD--AFFEefvrwQRGRLP 275
Cdd:cd05060 156 T-AGRWPlkWYAPECINYGK-----FSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEviAMLE-----SGERLP 218
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
58-310 1.74e-17

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: 82.34  E-value: 1.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL-REVSITNSLSSsPFIIKVFDVVFETEDCYVFaQEYAPAGDL 136
Cdd:cd06659  28 KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLfNEVVIMRDYQH-PNVVEMYKSYLVGEELWVL-MEYLQGGAL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDrecRRVKLADFGMTRRVGCRV-KRVS--GTI 212
Cdd:cd06659 106 TDIVS-QTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLtLD---GRVKLSDFGFCAQISKDVpKRKSlvGTP 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 213 PYTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAffeeFVRWQRGRLPGLPSQWRrfTEPALRMF 292
Cdd:cd06659 182 YWMAPEVISR-----CPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQA----MKRLRDSPPPKLKNSHK--ASPVLRDF 250
                       250
                ....*....|....*....
gi 66773086 293 -QRLLALEPERRGPAKEVF 310
Cdd:cd06659 251 lERMLVRDPQERATAQELL 269
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
51-248 2.31e-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: 81.66  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYK----GTGTKMALKFVNKSK--TKLKNFLREVSITNSLSSsPFIIK---VFDVVFETE 121
Cdd:cd05038   4 RHLKFIKQLGEGHFGSVELCRYDplgdNTGEQVAVKSLQPSGeeQHMSDFKREIEILRTLDH-EYIVKykgVCESPGRRS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFaqEYAPAGDLFDIIP---PQVGLPedTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMT 198
Cdd:cd05038  83 LRLIM--EYLPSGSLRDYLQrhrDQIDLK--RLLLFASQICKGMEYLGSQRYIHRDLAARNILV-ESE-DLVKISDFGLA 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGC-----RVKRvSGTIP--YTAPEvcqAGRADGLAVDTgvDVWAFGVLIFCVLT 248
Cdd:cd05038 157 KVLPEdkeyyYVKE-PGESPifWYAPE---CLRESRFSSAS--DVWSFGVTLYELFT 207
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
50-253 2.74e-17

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: 81.10  E-value: 2.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  50 TKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfiIKVFDVVFETEDCYVFAQE 129
Cdd:cd14108   1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKS--IVRFHDAFEKRRVVIIVTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YApAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVG------C 203
Cdd:cd14108  79 LC-HEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELTpnepqyC 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVkrvsGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14108 158 KY----GTPEFVAPEIVNQS-----PVSKVTDIWPVGVIAYLCLTGISPF 198
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
53-260 3.83e-17

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: 81.85  E-value: 3.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPF-------IIKVFDVvFE------ 119
Cdd:cd14136  12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPkdpgrehVVQLLDD-FKhtgpng 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 TEDCYVFaqEYApaGD--LFDIIPPQV-GLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDRECrRVKLADF 195
Cdd:cd14136  91 THVCMVF--EVL--GPnlLKLIKRYNYrGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKI-EVKIADL 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 196 GMTrrvgCRV-KRVSGTI---PYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd14136 166 GNA----CWTdKHFTEDIqtrQYRSPEVIL-----GAGYGTPADIWSTACMAFELATGDYLFDPHSGED 225
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-304 3.97e-17

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: 81.12  E-value: 3.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVN---KSKTKlKNFLREVSITNSLSSsPFIIKVFDV----VFETEDCYVFAQEYA 131
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRlelSVKNK-DRWCHEIQIMKKLNH-PNVVKACDVpeemNFLVNDVPLLAMEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDII-PPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADFGMTRRV--GCRV 205
Cdd:cd14039  79 SGGDLRKLLnKPEncCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAKDLdqGSLC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTG---------NFPW-EAASGADA----FFEEF---VR 268
Cdd:cd14039 159 TSFVGTLQYLAPELFE-----NKSYTVTVDYWSFGTMVFECIAGfrpflhnlqPFTWhEKIKKKDPkhifAVEEMngeVR 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 66773086 269 WQRgRLPGLPSQWRRFTEPALRMFQRLLALEPERRG 304
Cdd:cd14039 234 FST-HLPQPNNLCSLIVEPMEGWLQLMLNWDPVQRG 268
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
51-303 4.56e-17

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: 81.19  E-value: 4.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYelvRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSSpFIIKVfDVVFETEDCYVF 126
Cdd:cd05631   3 RHY---RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKRILEKVNSR-FVVSL-AYAYETKDALCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDL-FDIIppQVGLPEDTVKRCV---QQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV- 201
Cdd:cd05631  78 VLTIMNGGDLkFHIY--NMGNPGFDEQRAIfyaAELCCGLEDLQRERIVYRDLKPENILLDDRG--HIRISDLGLAVQIp 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAasgadafFEEFVRWQR--GRLPGLP 278
Cdd:cd05631 154 eGETVRGRVGTVGYMAPEVINNEK-----YTFSPDWWGLGCLIYEMIQGQSPFRK-------RKERVKREEvdRRVKEDQ 221
                       250       260
                ....*....|....*....|....*.
gi 66773086 279 SQW-RRFTEPALRMFQRLLALEPERR 303
Cdd:cd05631 222 EEYsEKFSEDAKSICRMLLTKNPKER 247
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
60-314 5.87e-17

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: 80.00  E-value: 5.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  60 GKGTYGKVDLVVYKGTGTKMALKfvnksktKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDcYVFAQEYAPAGDLFDI 139
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVK-------KLLKIEKEAEILSVLSHRN-IIQFYGAILEAPN-YGIVTEYASYGSLFDY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 140 IPPQVG--LPEDTVKRCVQQLGLALDFMHGR---QLVHRDIKPENVLLFDRECrrVKLADFGMTRRVG-CRVKRVSGTIP 213
Cdd:cd14060  73 LNSNESeeMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGV--LKICDFGASRFHShTTHMSLVGTFP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 214 YTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADaffeefVRW---QRGRLPGLPSQW-RRFTEpal 289
Cdd:cd14060 151 WMAPEVIQ-----SLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQ------VAWlvvEKNERPTIPSSCpRSFAE--- 216
                       250       260
                ....*....|....*....|....*
gi 66773086 290 rMFQRLLALEPERRGPAKEVFRFLK 314
Cdd:cd14060 217 -LMRRCWEADVKERPSFKQIIGILE 240
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
53-244 6.27e-17

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: 81.18  E-value: 6.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYK--GTGTKMALKFVNKSKTKLKNF----LREVSITNSLSSsPFIIKVFDVVFETEDCYVF 126
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKFKGDKEQYTGIsqsaCREIALLRELKH-ENVVSLVEVFLEHADKSVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 -AQEYAPAgDLFDII-----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL--FDRECRRVKLADFGMT 198
Cdd:cd07842  81 lLFDYAEH-DLWQIIkfhrqAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgEGPERGVVKIGDLGLA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 199 RRVGCRVK------RVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVlIF 244
Cdd:cd07842 160 RLFNAPLKpladldPVVVTIWYRAPELLLGARHYTKA----IDIWAIGC-IF 206
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
53-316 6.79e-17

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: 80.49  E-value: 6.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFV--NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd14046   8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIklRSESKNNSRILREVMLLSRLNH-QHVVRYYQAWIERANLYI-QMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFG-------------- 196
Cdd:cd14046  86 CEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFL--DSNGNVKIGDFGlatsnklnvelatq 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 ---------------MTRRVgcrvkrvsGTIPYTAPEVcqAGRADGlAVDTGVDVWAFGVLIF--CvltgnFPWEAASga 259
Cdd:cd14046 164 dinkstsaalgssgdLTGNV--------GTALYVAPEV--QSGTKS-TYNEKVDMYSLGIIFFemC-----YPFSTGM-- 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 260 daffEEFV--RWQRGRLPGLPSQWRRFTEP-ALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14046 226 ----ERVQilTALRSVSIEFPPDFDDNKHSkQAKLIRWLLNHDPAKRPSAQEL---LKSE 278
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
57-309 6.98e-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: 80.45  E-value: 6.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSSpFIIKVfDVVFETEDCYVFAQEYAP 132
Cdd:cd05630   6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSR-FVVSL-AYAYETKDALCLVLTLMN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDL-FDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV--GCRVKRV 208
Cdd:cd05630  84 GGDLkFHIYHmGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHG--HIRISDLGLAVHVpeGQTIKGR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAASgadaffEEFVRWQRGRL-PGLPSQW-RRFTE 286
Cdd:cd05630 162 VGTVGYMAPEVVKNER-----YTFSPDWWALGCLLYEMIAGQSPFQQRK------KKIKREEVERLvKEVPEEYsEKFSP 230
                       250       260
                ....*....|....*....|....*...
gi 66773086 287 PALRMFQRLLALEPERR-----GPAKEV 309
Cdd:cd05630 231 QARSLCSMLLCKDPAERlgcrgGGAREV 258
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
52-311 7.52e-17

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: 80.09  E-value: 7.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFV-----NKSKTKLKNFLR-EVSITNSLSSSPfIIKVFDVVFET-EDCY 124
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfdpeSPETSKEVNALEcEIQLLKNLLHER-IVQYYGCLRDPqERTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLlfDRECRRVKLADFGMTRRV--- 201
Cdd:cd06652  82 SIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL--RDSVGNVKLGDFGASKRLqti 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 ---GCRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLP 278
Cdd:cd06652 160 clsGTGMKSVTGTPYWMSPEVIS-----GEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPAHV 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 279 SQWrrftepaLRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd06652 235 SDH-------CRDFLKRIFVEAKLRPSADELLR 260
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
41-314 8.44e-17

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: 80.54  E-value: 8.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  41 LRTLAA-SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFE 119
Cdd:cd06654   9 LRSIVSvGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 TEDCYVfAQEYAPAGDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDREcrrVKLADFGMT 198
Cdd:cd06654  89 GDELWV-VMEYLAGGSLTDVVT-ETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMDGS---VKLTDFGFC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRVGCRVKRVS---GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFF-------EEFVR 268
Cdd:cd06654 164 AQITPEQSKRStmvGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYliatngtPELQN 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 269 WQRgrlpgLPSQWRRFtepalrmFQRLLALEPERRGPAKEVF--RFLK 314
Cdd:cd06654 239 PEK-----LSAIFRDF-------LNRCLEMDVEKRGSAKELLqhQFLK 274
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
52-253 1.04e-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: 80.01  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT---------------------------KLKNFLREVSITNSL 104
Cdd:cd14199   3 QYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprgaraapegctqprgPIERVYQEIAILKKL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 105 SSsPFIIKVFDVVFE-TEDCYVFAQEYAPAGDLFDIiPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLf 183
Cdd:cd14199  83 DH-PNVVKLVEVLDDpSEDHLYMVFELVKQGPVMEV-PTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV- 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086 184 dRECRRVKLADFGMTRRV---GCRVKRVSGTIPYTAPEVCQAGRAdgLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14199 160 -GEDGHIKIADFGVSNEFegsDALLTNTVGTPAFMAPETLSETRK--IFSGKALDVWAMGVTLYCFVFGQCPF 229
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
59-254 1.10e-16

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: 80.51  E-value: 1.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKfVNKSKTKLKNFLREVSITN----SLSSSPFIIKVFDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIK-ILKKDVIIQDDDVECTMVEkrvlALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DL-FDIipPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRR---VGCRVKRVS 209
Cdd:cd05587  83 DLmYHI--QQVGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-DAE-GHIKIADFGMCKEgifGGKTTRTFC 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 66773086 210 GTIPYTAPEVCqAGRADGLAVDTgvdvWAFGVLIFCVLTGNFPWE 254
Cdd:cd05587 159 GTPDYIAPEII-AYQPYGKSVDW----WAYGVLLYEMLAGQPPFD 198
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
51-303 1.24e-16

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: 79.95  E-value: 1.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSsPFIIKVfDVVFETEDCYVF 126
Cdd:cd05607   2 KYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSgekmALLEKEILEKVNS-PFIVSL-AYAFETKTHLCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDL-FDIIP-PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR-ECRrvkLADFGMTRRV-- 201
Cdd:cd05607  80 VMSLMNGGDLkYHIYNvGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNgNCR---LSDLGLAVEVke 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPW----EAASGADAF---FEEFVRWQRgrl 274
Cdd:cd05607 157 GKPITQRAGTNGYMAPEILKE-----ESYSYPVDWFAMGCSIYEMVAGRTPFrdhkEKVSKEELKrrtLEDEVKFEH--- 228
                       250       260
                ....*....|....*....|....*....
gi 66773086 275 pglpsqwRRFTEPALRMFQRLLALEPERR 303
Cdd:cd05607 229 -------QNFTEEAKDICRLFLAKKPENR 250
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
1-252 1.32e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 80.64  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    1 MSVGCPEPEPPRSltccgpGTAPGPGAGVPLLTEDMQALTLRTLaasdvtkhyELVRELGKGTYGKVDLVVYKGTGTKMA 80
Cdd:PLN00034  39 PSLAVPLPLPPPS------SSSSSSSSSSASGSAPSAAKSLSEL---------ERVNRIGSGAGGTVYKVIHRPTGRLYA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   81 LKFV--NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQql 158
Cdd:PLN00034 104 LKVIygNHEDTVRRQICREIEILRDVNH-PNVVKCHDM-FDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVARQILS-- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  159 GLAldFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVGCRVKRVS---GTIPYTAPEVCQA----GRADGLAvd 231
Cdd:PLN00034 180 GIA--YLHRRHIVHRDIKPSNLLINSA--KNVKIADFGVSRILAQTMDPCNssvGTIAYMSPERINTdlnhGAYDGYA-- 253
                        250       260
                 ....*....|....*....|.
gi 66773086  232 tgVDVWAFGVLIFCVLTGNFP 252
Cdd:PLN00034 254 --GDIWSLGVSILEFYLGRFP 272
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
53-309 1.35e-16

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: 79.24  E-value: 1.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKGT----GTKMALKFVNKSKT----KLKNFLR---EVSITNSLSSS-PFIIKVFDVvFET 120
Cdd:cd14100   2 YQVGPLLGSGGFGSV----YSGIrvadGAPVAIKHVEKDRVsewgELPNGTRvpmEIVLLKKVGSGfRGVIRLLDW-FER 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFAQEYA-PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGMtr 199
Cdd:cd14100  77 PDSFVLVLERPePVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI-DLNTGELKLIDFGS-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 rvGCRVKRV-----SGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAAsgadaffEEFVRWQ---R 271
Cdd:cd14100 154 --GALLKDTvytdfDGTRVYSPPEWIRFHRYHGRS----AAVWSLGILLYDMVCGDIPFEHD-------EEIIRGQvffR 220
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 272 grlpglpsqwRRFTEPALRMFQRLLALEPERRGPAKEV 309
Cdd:cd14100 221 ----------QRVSSECQHLIKWCLALRPSDRPSFEDI 248
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
55-318 1.48e-16

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: 78.84  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGkvdlVVYKG---TGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFE-TEDCYVFaqEY 130
Cdd:cd05112   8 FVQEIGSGQFG----LVHLGywlNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSH-PKLVQLYGVCLEqAPICLVF--EF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVG-LPEDTVkrcvqqLGLALDFMHG------RQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV-G 202
Cdd:cd05112  81 MEHGCLSDYLRTQRGlFSAETL------LGMCLDVCEGmayleeASVIHRDLAARNCLV--GENQVVKVSDFGMTRFVlD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSGT---IPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAfFEEFVRWQRGRLPGLP 278
Cdd:cd05112 153 DQYTSSTGTkfpVKWSSPEVFSFSR-----YSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEV-VEDINAGFRLYKPRLA 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 279 SQwrrftePALRMFQRLLALEPERRgPAkevFRFLKHELT 318
Cdd:cd05112 227 ST------HVYEIMNHCWKERPEDR-PS---FSLLLRQLA 256
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
53-260 1.83e-16

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: 79.34  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYK----GTGTKMALK-FVNKSKTKL--KNFLREVSITNSLSSSPFI--IKVF------DVV 117
Cdd:cd07847   3 YEKLSKIGEGSYG----VVFKcrnrETGQIVAIKkFVESEDDPVikKIALREIRMLKQLKHPNLVnlIEVFrrkrklHLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 118 FETEDCYVFAQ-EYAPAGdlfdiippqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFG 196
Cdd:cd07847  79 FEYCDHTVLNElEKNPRG-----------VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQG--QIKLCDFG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 197 MTRRV---GCRVKRVSGTIPYTAPEVcqagradgLAVDT----GVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd07847 146 FARILtgpGDDYTDYVATRWYRAPEL--------LVGDTqygpPVDVWAIGCVFAELLTGQPLWPGKSDVD 208
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
52-200 1.89e-16

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: 78.65  E-value: 1.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKsKTKLKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYA 131
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKK-DSKHPQLEYEAKVYKLLQGGPGIPRLYWF-GQEGDYNVMVMDLL 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 132 paG----DLFDIIPPQVGLpeDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADFGMTRR 200
Cdd:cd14016  79 --GpsleDLFNKCGRKFSL--KTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMgLGKNSNKVYLIDFGLAKK 148
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
53-250 2.47e-16

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: 79.53  E-value: 2.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFV-NKSK----TKLK-NFLREVSITNSLSSSPfIIKVFDVvFETEDCYVF 126
Cdd:cd14134  14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKyreaAKIEiDVLETLAEKDPNGKSH-CVQLRDW-FDYRGHMCI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQE-YAPAgdLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRV-- 201
Cdd:cd14134  92 VFElLGPS--LYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNPKKKRQIRVpk 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 202 GCRVKR----------------VSgTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGN 250
Cdd:cd14134 170 STDIKLidfgsatfddeyhssiVS-TRHYRAPEVIL-----GLGWSYPCDVWSIGCILVELYTGE 228
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
48-252 3.42e-16

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: 79.27  E-value: 3.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKfvnksktKLKNF---------LREVSITNSLSSSPfIIKVFDVV- 117
Cdd:cd07849   2 DVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK-------KISPFehqtyclrtLREIKILLRFKHEN-IIGILDIQr 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 118 ---FET-EDCYvFAQEYAPAgDLFDIIPPQVgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLA 193
Cdd:cd07849  74 pptFESfKDVY-IVQELMET-DLYKLIKTQH-LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL-NTNC-DLKIC 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 194 DFGMTR-------RVGCRVKRVSgTIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGN--FP 252
Cdd:cd07849 149 DFGLARiadpehdHTGFLTEYVA-TRWYRAPEIMLNSK----GYTKAIDIWSVGCILAEMLSNRplFP 211
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
53-325 3.64e-16

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 78.32  E-value: 3.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKfvnksKTKLKN--------FLREVSITNSLSSSPfIIKVFDVVFeT 120
Cdd:PLN00009   4 YEKVEKIGEGTYG----VVYKArdrvTNETIALK-----KIRLEQedegvpstAIREISLLKEMQHGN-IVRLQDVVH-S 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  121 EDCYVFAQEYApagDL-----FDIIPPQVGLPEdTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADF 195
Cdd:PLN00009  73 EKRLYLVFEYL---DLdlkkhMDSSPDFAKNPR-LIKTYLYQILRGIAYCHSHRVLHRDLKPQN-LLIDRRTNALKLADF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  196 GMTRRVGCRVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVlIFCVLTGNFP-------------------- 252
Cdd:PLN00009 148 GLARAFGIPVRTFTHevvTLWYRAPEILLGSR----HYSTPVDIWSVGC-IFAEMVNQKPlfpgdseidelfkifrilgt 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  253 -----WEAASGADAFFEEFVRWQRGRL----PGLpsqwrrftEPA-LRMFQRLLALEPERRGPAKEVfrfLKHELTSELR 322
Cdd:PLN00009 223 pneetWPGVTSLPDYKSAFPKWPPKDLatvvPTL--------EPAgVDLLSKMLRLDPSKRITARAA---LEHEYFKDLG 291

                 ...
gi 66773086  323 RRP 325
Cdd:PLN00009 292 DAP 294
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
54-327 3.89e-16

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: 78.19  E-value: 3.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVREL---GKGTYGKVDLVVYKGTGTKMALKFVN--KSKTKLKNFLREVSITnSLSSSPFIIKVFDVVFETEDCYVFaQ 128
Cdd:cd06641   4 ELFTKLekiGKGSFGEVFKGIDNRTQKVVAIKIIDleEAEDEIEDIQQEITVL-SQCDSPYVTKYYGSYLKDTKLWII-M 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV-GCRVKR 207
Cdd:cd06641  82 EYLGGGSALDLLEPG-PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL--SEHGEVKLADFGVAGQLtDTQIKR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 208 --VSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFeefvRWQRGRLPGLPSQWRRft 285
Cdd:cd06641 159 n*FVGTPFWMAPEVIKQS-----AYDSKADIWSLGITAIELARGEPPHSELHPMKVLF----LIPKNNPPTLEGNYSK-- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 286 epALRMF-QRLLALEPERRGPAKEVfrfLKHELTSELRRRPSH 327
Cdd:cd06641 228 --PLKEFvEACLNKEPSFRPTAKEL---LKHKFILRNAKKTSY 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-311 4.49e-16

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: 77.46  E-value: 4.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK-SKTKLK-----NFLREVSITNSLSSsPFIIKVFDVVFETED-CYV 125
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEiSVGELQpdetvDANREAKLLSKLDH-PAIVKFHDSFVEKESfCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 faQEYAPAGDLFDIIPP--QVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdrecRR--VKLADFGMTR 199
Cdd:cd08222  81 --TEYCEGGDLDDKISEykKSGttIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-----KNnvIKVGDFGISR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 RV--GCRVKRV-SGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIF--CVLTGNFpwEAASgadaFFEEFVRWQRGRL 274
Cdd:cd08222 154 ILmgTSDLATTfTGTPYYMSPEVLK-----HEGYNSKSDIWSLGCILYemCCLKHAF--DGQN----LLSVMYKIVEGET 222
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 66773086 275 PGLPSqwrRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd08222 223 PSLPD---KYSKELNAIYSRMLNKDPALRPSAAEILK 256
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
53-241 4.88e-16

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: 77.73  E-value: 4.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFET-----EDCYVFA 127
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKdppggDDQLWLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFD----IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGC 203
Cdd:cd06608  88 MEYCGGGSVTDlvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILL--TEEAEVKLVDFGVSAQLDS 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 66773086 204 RVKR---VSGTiPY-TAPEVCQAGRADGLAVDTGVDVWAFGV 241
Cdd:cd06608 166 TLGRrntFIGT-PYwMAPEVIACDQQPDASYDARCDVWSLGI 206
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
59-311 5.01e-16

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: 77.83  E-value: 5.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGkvdlVVYKG----TGTKMALKFV-NKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCYVFaQEYAPA 133
Cdd:cd06624  16 LGKGTFG----VVYAArdlsTQVRIAIKEIpERDSREVQPLHEEIALHSRLSHKN-IVQYLGSVSEDGFFKIF-MEQVPG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVGlP----EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGMTRRVG----CrV 205
Cdd:cd06624  90 GSLSALLRSKWG-PlkdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLV-NTYSGVVKISDFGTSKRLAginpC-T 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQAG-RADGLAvdtgVDVWAFGVLIFCVLTGNFPW------EAASGADAFFEEFvrwqrgrlPGLP 278
Cdd:cd06624 167 ETFTGTLQYMAPEVIDKGqRGYGPP----ADIWSLGCTIIEMATGKPPFielgepQAAMFKVGMFKIH--------PEIP 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 279 SQwrrFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd06624 235 ES---LSEEAKSFILRCFEPDPDKRATASDLLQ 264
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
52-303 5.11e-16

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: 78.07  E-value: 5.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSK---------------------------TKLKNFLREVSITNSL 104
Cdd:cd14200   1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygfprrppprgskaaqgeqakplAPLERVYQEIAILKKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 105 SSSPfIIKVFDVVFE-TEDCYVFAQEYAPAGDLFDIiPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLF 183
Cdd:cd14200  81 DHVN-IVKLIEVLDDpAEDNLYMVFDLLRKGPVMEV-PSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 184 DREcrRVKLADFGMTRRV---GCRVKRVSGTIPYTAPE-VCQAGRA-DGLAvdtgVDVWAFGVLIFCVLTGNFPweaasg 258
Cdd:cd14200 159 DDG--HVKIADFGVSNQFegnDALLSSTAGTPAFMAPEtLSDSGQSfSGKA----LDVWAMGVTLYCFVYGKCP------ 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 259 adaFFEEFVRWQRGRLPGLPSQW---RRFTEPALRMFQRLLALEPERR 303
Cdd:cd14200 227 ---FIDEFILALHNKIKNKPVEFpeePEISEELKDLILKMLDKNPETR 271
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
51-252 5.49e-16

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: 77.64  E-value: 5.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGtGTKMALKFVN---KSKTKLKNFLREVSITNSLSSSPFIIKVFDV-VFETEDcYVF 126
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDlegADEQTLQSYKNEIELLKKLKGSDRIIQLYDYeVTDEDD-YLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 A-QEYApAGDLFDIIPPQV--GLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDrecRRVKLADFGMTRRVG- 202
Cdd:cd14131  79 MvMECG-EIDLATILKKKRpkPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK---GRLKLIDFGIAKAIQn 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 203 --CRVKRVS--GTIPYTAPEVCQAGRADG-----LAVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd14131 155 dtTSIVRDSqvGTLNYMSPEAIKDTSASGegkpkSKIGRPSDVWSLGCILYQMVYGKTP 213
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
53-255 6.13e-16

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 78.48  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   53 YELVRELGKGTYGKVDLVVYK-GTGTKMALKFVNKSK----TKLKNFLREVSITNSLSSsPFIIKVFDVvFETEDCYVFA 127
Cdd:PTZ00426  32 FNFIRTLGTGSFGRVILATYKnEDFPPVAIKRFEKSKiikqKQVDHVFSERKILNYINH-PFCVNLYGS-FKDESYLYLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRVGCRVKR 207
Cdd:PTZ00426 110 LEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL-DKD-GFIKMTDFGFAKVVDTRTYT 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 66773086  208 VSGTIPYTAPEVCqagradgLAVDTG--VDVWAFGVLIFCVLTGNFPWEA 255
Cdd:PTZ00426 188 LCGTPEYIAPEIL-------LNVGHGkaADWWTLGIFIYEILVGCPPFYA 230
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
48-241 7.06e-16

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: 77.74  E-value: 7.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETE----DC 123
Cdd:cd06638  15 DPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYKKDvkngDQ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVG----LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTR 199
Cdd:cd06638  95 LWLVLELCNGGSVTDLVKGFLKrgerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG--GVKLVDFGVSA 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 66773086 200 RV-GCRVKRVS--GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGV 241
Cdd:cd06638 173 QLtSTRLRRNTsvGTPFWMAPEVIACEQQLDSTYDARCDVWSLGI 217
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
51-243 7.23e-16

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: 77.01  E-value: 7.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTgtKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEY 130
Cdd:cd05039   6 KDLKLGELIGKGEFGDVMLGDYRGQ--KVAVKCLKDDSTAAQAFLAEASVMTTLRH-PNLVQLLGVVLEGNGLYIVT-EY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIppqvglpeDTVKRCV----QQLGLALD------FMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRR 200
Cdd:cd05039  82 MAKGSLVDYL--------RSRGRAVitrkDQLGFALDvcegmeYLESKKFVHRDLAARNVLVSEDNV--AKVSDFGLAKE 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 66773086 201 VgcRVKRVSGTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLI 243
Cdd:cd05039 152 A--SSNQDGGKLPikWTAPEALREKK-----FSTKSDVWSFGILL 189
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
58-253 8.21e-16

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: 76.88  E-value: 8.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYgKVdlvVYKG----TGTKMA---LKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFET-EDCYVFAQE 129
Cdd:cd13983   8 VLGRGSF-KT---VYRAfdteEGIEVAwneIKLRKLPKAERQRFKQEIEILKSLKH-PNIIKFYDSWESKsKKEVIFITE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLfDRECRRVKLADFGM-TRRVGCRVK 206
Cdd:cd13983  83 LMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI-NGNTGEVKIGDLGLaTLLRQSFAK 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 207 RVSGTIPYTAPEVCQAGradglaVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd13983 162 SVIGTPEFMAPEMYEEH------YDEKVDIYAFGMCLLEMATGEYPY 202
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
94-257 8.58e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 79.45  E-value: 8.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   94 FLREV-SITnSLSSsPFIIKVFDVVfETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVH 172
Cdd:NF033483  54 FRREAqSAA-SLSH-PNIVSVYDVG-EDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  173 RDIKPENVLLfDREcRRVKLADFG---------MTRRVGcrvkrVSGTIPYTAPEvcQAgRadGLAVDTGVDVWAFGVLI 243
Cdd:NF033483 131 RDIKPQNILI-TKD-GRVKVTDFGiaralssttMTQTNS-----VLGTVHYLSPE--QA-R--GGTVDARSDIYSLGIVL 198
                        170
                 ....*....|....
gi 66773086  244 FCVLTGNFPWEAAS 257
Cdd:NF033483 199 YEMLTGRPPFDGDS 212
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
54-253 9.33e-16

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: 76.85  E-value: 9.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVfeTEDCYVFAQEYAPA 133
Cdd:cd05067  10 KLVERLGAGQFGEVWMGYYNGH-TKVAIKSLKQGSMSPDAFLAEANLMKQLQH-QRLVRLYAVV--TQEPIYIITEYMEN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTR---------RVG 202
Cdd:cd05067  86 GSLVDFLKTPSGikLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLS--CKIADFGLARliedneytaREG 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 203 CRVKrvsgtIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05067 164 AKFP-----IKWTAPEAINYG-----TFTIKSDVWSFGILLTEIVThGRIPY 205
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
48-326 1.61e-15

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: 76.25  E-value: 1.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVdlvvYKG----TGTKMALKFVN--KSKTKLKNFLREVSITnSLSSSPFIIKVFDVVFETE 121
Cdd:cd06642   1 DPEELFTKLERIGKGSFGEV----YKGidnrTKEVVAIKIIDleEAEDEIEDIQQEITVL-SQCDSPYITRYYGSYLKGT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFaQEYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV 201
Cdd:cd06642  76 KLWII-MEYLGGGSALDLLKPG-PLEETYIATILREILKGLDYLHSERKIHRDIKAANVLL--SEQGDVKLADFGVAGQL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVS--GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFeefvRWQRGRLPGLP 278
Cdd:cd06642 152 tDTQIKRNTfvGTPFWMAPEVIKQS-----AYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLF----LIPKNSPPTLE 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 279 SQwrrFTEPALRMFQRLLALEPERRGPAKEVfrfLKHELTSELRRRPS 326
Cdd:cd06642 223 GQ---HSKPFKEFVEACLNKDPRFRPTAKEL---LKHKFITRYTKKTS 264
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
59-260 1.62e-15

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: 76.00  E-value: 1.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTkMALKFVNKSKTKL---KNFLREVSITNSLSSSPfIIKVFDVVFETEDcYVFAQEYAPAGD 135
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGL-VVLKTVYTGPNCIehnEALLEEGKMMNRLRHSR-VVKLLGVILEEGK-YSLVMEYMEKGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFG---------MTRRVGCRVK 206
Cdd:cd14027  78 LMHVLK-KVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILV-DNDF-HIKIADLGlasfkmwskLTKEEHNEQR 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 207 RV-------SGTIPYTAPEVCQAGRADGLAVDtgvDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd14027 155 EVdgtakknAGTLYYMAPEHLNDVNAKPTEKS---DVYSFAIVLWAIFANKEPYENAINED 212
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
59-249 1.73e-15

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: 76.97  E-value: 1.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL------REVSITNSLSssPFIIKVfDVVFETEDCYVFAQEYAP 132
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVkhimaeRNVLLKNVKH--PFLVGL-HYSFQTKDKLYFVLDYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGM---------TRRVGC 203
Cdd:cd05575  80 GGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILL-DSQ-GHVVLTDFGLckegiepsdTTSTFC 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 204 rvkrvsGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd05575 158 ------GTPEYLAPEVLRKQ-----PYDRTVDWWCLGAVLYEMLYG 192
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
57-315 2.19e-15

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: 75.77  E-value: 2.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVdlvVYKGT--GTKMALKFVnksktkLKNF----LREVSITNSLSSSPFIIKVFDVvfETEDCYVF-AQE 129
Cdd:cd13982   7 KVLGYGSEGTI---VFRGTfdGRPVAVKRL------LPEFfdfaDREVQLLRESDEHPNVIRYFCT--EKDRQFLYiALE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAgDLFDII-PPQVGLPED----TVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL---FDRECRRVKLADFGMTRRV 201
Cdd:cd13982  76 LCAA-SLQDLVeSPRESKLFLrpglEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpNAHGNVRAMISDFGLCKKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 G------CRVKRVSGTIPYTAPEVCQAGRADGLAvdTGVDVWAFGVLIFCVLTGnfpweaasGADAFFEEFVRWQ---RG 272
Cdd:cd13982 155 DvgrssfSRRSGVAGTSGWIAPEMLSGSTKRRQT--RAVDIFSLGCVFYYVLSG--------GSHPFGDKLEREAnilKG 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 66773086 273 R--LPGLPSQWRRFTEpALRMFQRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd13982 225 KysLDKLLSLGEHGPE-AQDLIERMIDFDPEKRPSAEEV---LNH 265
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
53-240 2.41e-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: 75.93  E-value: 2.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFV---NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVF-ETEDCYVFaq 128
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVrldDDDEGVPSSALREICLLKELKH-KNIVRLYDVLHsDKKLTLVF-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAgDL---FDIIPPQVGLPedTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRV 205
Cdd:cd07839  79 EYCDQ-DLkkyFDSCNGDIDPE--IVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNG--ELKLADFGLARAFGIPV 153
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 66773086 206 KRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFG 240
Cdd:cd07839 154 RCYSAevvTLWYRPPDVLFGAK----LYSTSIDMWSAG 187
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
53-252 2.44e-15

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: 75.92  E-value: 2.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKL--KNFLREVSITNSLSSSPFI--IKVFD------VVFETE 121
Cdd:cd07846   3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKkFLESEDDKMvkKIAMREIKMLKQLRHENLVnlIEVFRrkkrwyLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFAQ-EYAPAGdlfdiippqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRR 200
Cdd:cd07846  83 DHTVLDDlEKYPNG-----------LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILV--SQSGVVKLCDFGFART 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 201 V---GCRVKRVSGTIPYTAPEV----CQAGRAdglavdtgVDVWAFGVLIFCVLTGN--FP 252
Cdd:cd07846 150 LaapGEVYTDYVATRWYRAPELlvgdTKYGKA--------VDVWAVGCLVTEMLTGEplFP 202
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
52-303 2.77e-15

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: 76.29  E-value: 2.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGT--GTKMALKFVNK--SKTKL-KNFLREVSITNSLSSSPFIIKVFDVVFETEDCY-- 124
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAETseEETVAIKKITNvfSKKILaKRALRELKLLRHFRGHKNITCLYDMDIVFPGNFne 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFGMTRRVGCR 204
Cdd:cd07857  81 LYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGN-LLVNADC-ELKICDFGLARGFSEN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSG-------TIPYTAPEVCQAGRadglAVDTGVDVWAFGV----------------------LIFCVLtGNFPWEA 255
Cdd:cd07857 159 PGENAGfmteyvaTRWYRAPEIMLSFQ----SYTKAIDVWSVGCilaellgrkpvfkgkdyvdqlnQILQVL-GTPDEET 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 256 ASG-ADAFFEEFVRwQRGRLPGLPSQWRR-FTEP-ALRMFQRLLALEPERR 303
Cdd:cd07857 234 LSRiGSPKAQNYIR-SLPNIPKKPFESIFpNANPlALDLLEKLLAFDPTKR 283
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
53-241 3.07e-15

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: 75.43  E-value: 3.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKG----TGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFET-----EDC 123
Cdd:cd06636  18 FELVEVVGNGTYGQV----YKGrhvkTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKsppghDDQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMT--- 198
Cdd:cd06636  94 LWLVMEFCGAGSVTDLVKNTKGnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLVDFGVSaql 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 66773086 199 -RRVGcRVKRVSGTIPYTAPEVCQAGRADGLAVDTGVDVWAFGV 241
Cdd:cd06636 172 dRTVG-RRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGI 214
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
59-311 3.11e-15

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: 75.50  E-value: 3.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVN------KSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYAP 132
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGRELAAKQVQfdpespETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLlfDRECRRVKLADFGMTRRV------GCRVK 206
Cdd:cd06651  95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLqticmsGTGIR 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRgrlPGLPSQwrrfTE 286
Cdd:cd06651 173 SVTGTPYWMSPEVIS-----GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTN---PQLPSH----IS 240
                       250       260
                ....*....|....*....|....*
gi 66773086 287 PALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd06651 241 EHARDFLGCIFVEARHRPSAEELLR 265
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
51-332 3.26e-15

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: 75.71  E-value: 3.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYK----GTGTKMALKFVNK--SKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCY 124
Cdd:cd05080   4 RYLKKIRDLGEGHFGKVSLYCYDptndGTGEMVAVKALKAdcGPQHRSGWKQEIDILKTLYHEN-IVKYKGCCSEQGGKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 V-FAQEYAPAGDLFDIIPP-QVGLPEDTVkrCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTRRV- 201
Cdd:cd05080  83 LqLIMEYVPLGSLRDYLPKhSIGLAQLLL--FAQQICEGMAYLHSQHYIHRDLAARNVLL-DND-RLVKIGDFGLAKAVp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVS--GTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAASgadAFFEEFVRWQRGRLPG 276
Cdd:cd05080 159 eGHEYYRVRedGDSPvfWYAPECLKEYK-----FYYASDVWSFGVTLYELLTHCDSSQSPP---TKFLEMIGIAQGQMTV 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 277 LpsqwrRFTEpALRMFQRLlalePERRGPAKEVFRFLKHELTSELRRRPSHRARKP 332
Cdd:cd05080 231 V-----RLIE-LLERGERL----PCPDKCPQEVYHLMKNCWETEASFRPTFENLIP 276
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
51-254 3.59e-15

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: 74.86  E-value: 3.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfiIKVFDVVFETEDCYVFAQEY 130
Cdd:cd14111   3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHER--IMALHEAYITPRYLVLIAEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRV----K 206
Cdd:cd14111  81 CSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA--IKIVDFGSAQSFNPLSlrqlG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 207 RVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14111 159 RRTGTLEYMAPEMVK-----GEPVGPPADIWSIGVLTYIMLSGRSPFE 201
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
53-310 4.23e-15

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: 74.61  E-value: 4.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKGT----GTKMALKFVNKSKTKLKNFLREVSITNSL-------SSSPFIIKVFDVvFETE 121
Cdd:cd14102   2 YQVGSVLGSGGFG----TVYAGSriadGLPVAVKHVVKERVTEWGTLNGVMVPLEIvllkkvgSGFRGVIKLLDW-YERP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFAQEYA-PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFGMtrr 200
Cdd:cd14102  77 DGFLIVMERPePVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDEN-LLVDLRTGELKLIDFGS--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 vGCRVKRV-----SGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAAsgadaffEEFVrwqRGRLp 275
Cdd:cd14102 153 -GALLKDTvytdfDGTRVYSPPEWIRYHRYHGRS----ATVWSLGVLLYDMVCGDIPFEQD-------EEIL---RGRL- 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 66773086 276 glpSQWRRFTEPALRMFQRLLALEPERRGPAKEVF 310
Cdd:cd14102 217 ---YFRRRVSPECQQLIKWCLSLRPSDRPTLEQIF 248
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
53-276 6.22e-15

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: 75.45  E-value: 6.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPF----IIKVFDVV-FETEDCYVFA 127
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENAdefnFVRAYECFqHRNHTCLVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEyapAGDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD--RECRRVKLADFGMTRRVGc 203
Cdd:cd14229  82 ML---EQNLYDFLKQNkfSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFGSASHVS- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 204 rvKRVSGTIP----YTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGnfpWEAASGADAFFEefVRW--QRGRLPG 276
Cdd:cd14229 158 --KTVCSTYLqsryYRAPEIIL-----GLPFCEAIDMWSLGCVIAELFLG---WPLYPGALEYDQ--IRYisQTQGLPG 224
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
52-311 6.33e-15

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: 74.84  E-value: 6.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKlKNF----LREVSITNSLSSSPfIIKVFDVVFETEDCYVFA 127
Cdd:cd07864   8 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEK-EGFpitaIREIKILRQLNHRS-VVNLKEIVTDKQDALDFK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 Q---------EYAPAgDLFDIIPPQ-VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGM 197
Cdd:cd07864  86 KdkgafylvfEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG--QIKLADFGL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCRVKRVSG----TIPYTAPEVCQAGRADGLAvdtgVDVWAFGvlifCVLTGNFPWEAASGADAFFEEFVRWQR-- 271
Cdd:cd07864 163 ARLYNSEESRPYTnkviTLWYRPPELLLGEERYGPA----IDVWSCG----CILGELFTKKPIFQANQELAQLELISRlc 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 272 -----------GRLPGLPS-----QWRR--------FTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd07864 235 gspcpavwpdvIKLPYFNTmkpkkQYRRrlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALN 298
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
51-332 7.99e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 74.54  E-value: 7.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYK----GTGTKMALKFVNKSKTK-LKNFLREVSITNSLSSSpFIIKVFDVVFET-EDCY 124
Cdd:cd05081   4 RHLKYISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDqQRDFQREIQILKALHSD-FIVKYRGVSYGPgRRSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-- 201
Cdd:cd05081  83 RLVMEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEA--HVKIADFGLAKLLpl 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 --GCRVKRVSGTIP--YTAPEvcqaGRADGLaVDTGVDVWAFGVLIfcvltgnfpweaasgadafFEEFVRWQRGRLPgl 277
Cdd:cd05081 161 dkDYYVVREPGQSPifWYAPE----SLSDNI-FSRQSDVWSFGVVL-------------------YELFTYCDKSCSP-- 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086 278 PSQWRRFTEP--ALRMFQRLLA-LEPERRGPA-----KEVFRFLKHELTSELRRRPSHRARKP 332
Cdd:cd05081 215 SAEFLRMMGCerDVPALCRLLElLEEGQRLPAppacpAEVHELMKLCWAPSPQDRPSFSALGP 277
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
59-303 8.54e-15

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: 73.72  E-value: 8.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT--GTKMALK------FVNKSKTKLknFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQEY 130
Cdd:cd14064   1 IGSGSFGKV----YKGRcrNKIVAIKryrantYCSKSDVDM--FCREVSILCRLNH-PCVIQFVGACLDDPSQFAIVTQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQvglpedtvKRCVQ---QLGLALDFMHGRQ--------LVHRDIKPENVLLFdrECRRVKLADFGMTR 199
Cdd:cd14064  74 VSGGSLFSLLHEQ--------KRVIDlqsKLIIAVDVAKGMEylhnltqpIIHRDLNSHNILLY--EDGHAVVADFGESR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 RVGCR----VKRVSGTIPYTAPEV-CQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWE----AASGADaffeefVRWQ 270
Cdd:cd14064 144 FLQSLdednMTKQPGNLRWMAPEVfTQCTR-----YSIKADVFSYALCLWELLTGEIPFAhlkpAAAAAD------MAYH 212
                       250       260       270
                ....*....|....*....|....*....|...
gi 66773086 271 RGRlPGLPSQwrrFTEPALRMFQRLLALEPERR 303
Cdd:cd14064 213 HIR-PPIGYS---IPKPISSLLMRGWNAEPESR 241
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
48-316 8.82e-15

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.80  E-value: 8.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   48 DVTKHYELV-RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLK-------------NF--LREVSITNSLSSsPFII 111
Cdd:PTZ00024   5 SISERYIQKgAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDvtkdrqlvgmcgiHFttLRELKIMNEIKH-ENIM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  112 KVFDVvFETEDCYVFAQEYApAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR-ECrrv 190
Cdd:PTZ00024  84 GLVDV-YVEGDFINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKgIC--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  191 KLADFGMTRRVGC---------------RVKRVSG--TIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGN--F 251
Cdd:PTZ00024 159 KIADFGLARRYGYppysdtlskdetmqrREEMTSKvvTLWYRAPELLMGAEKYHFA----VDMWSVGCIFAELLTGKplF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  252 PweaasGADAffeefVRwQRGR---LPGLPSQ-----------WRRFT---------------EPALRMFQRLLALEPER 302
Cdd:PTZ00024 235 P-----GENE-----ID-QLGRifeLLGTPNEdnwpqakklplYTEFTprkpkdlktifpnasDDAIDLLQSLLKLNPLE 303
                        330
                 ....*....|....
gi 66773086  303 RGPAKEVfrfLKHE 316
Cdd:PTZ00024 304 RISAKEA---LKHE 314
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
43-303 9.42e-15

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: 74.00  E-value: 9.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  43 TLAASDVTkhyeLVRELGKGTYGKVDLVVY---KGTGTKMALKF--VNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVV 117
Cdd:cd05056   2 EIQREDIT----LGRCIGEGQFGDVYQGVYmspENEKIAVAVKTckNCTSPSVREKFLQEAYIMRQFDH-PHIVKLIGVI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 118 feTEDCYVFAQEYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFG 196
Cdd:cd05056  77 --TENPVWIVMELAPLGELRSYLQVnKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC--VKLGDFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVG----CRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAffeeFVRWQR 271
Cdd:cd05056 153 LSRYMEdesyYKASKGKLPIKWMAPESINFRR-----FTSASDVWMFGVCMWEILMlGVKPFQGVKNNDV----IGRIEN 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 66773086 272 G-RLPgLPSQwrrfTEPAL-RMFQRLLALEPERR 303
Cdd:cd05056 224 GeRLP-MPPN----CPPTLySLMTKCWAYDPSKR 252
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
59-338 9.98e-15

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: 74.01  E-value: 9.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLRE---VSITNSLSSSPFIIkVFDVVFETEDCYVFAQEYA 131
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNErimLSLVSTGGDCPFIV-CMTYAFQTPDKLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVKRVS-G 210
Cdd:cd05606  81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL--DEHGHVRISDLGLACDFSKKKPHASvG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 211 TIPYTAPEVCQagraDGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAffEEFVRWQRGRLPGLPSQWrrftEPALR 290
Cdd:cd05606 159 THGYMAPEVLQ----KGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDK--HEIDRMTLTMNVELPDSF----SPELK 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 291 -MFQRLLALEPERR-----GPAKEVfrfLKHELTSELRRRPSHRARKPPGDRPP 338
Cdd:cd05606 229 sLLEGLLQRDVSKRlgclgRGATEV---KEHPFFKGVDWQQVYLQKYPPPLIPP 279
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
54-305 1.13e-14

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: 73.92  E-value: 1.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRE--LGKGTYGKVDLVVYKG--TGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETED-CYVFaq 128
Cdd:cd14145   7 ELVLEeiIGIGGFGKVYRAIWIGdeVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNlCLVM-- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLV---HRDIKPENVLLFDR------ECRRVKLADFGMTR 199
Cdd:cd14145  85 EFARGGPLNRVLSGK-RIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKvengdlSNKILKITDFGLAR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 RVGcRVKRVS--GTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEefVRWQRGRLPgL 277
Cdd:cd14145 164 EWH-RTTKMSaaGTYAWMAPEVIRSS-----MFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYG--VAMNKLSLP-I 234
                       250       260
                ....*....|....*....|....*...
gi 66773086 278 PSQWrrfTEPALRMFQRLLALEPERRGP 305
Cdd:cd14145 235 PSTC---PEPFARLMEDCWNPDPHSRPP 259
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
59-259 1.15e-14

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: 74.45  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALK------FVNKSKTKLKNF--LREVSITNslssspfIIKVFDVVFETEDCY-VFAQE 129
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKvfnnlsFMRPLDVQMREFevLKKLNHKN-------IVKLFAIEEELTTRHkVLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDII--PPQV-GLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV--KLADFGMTRRVGCR 204
Cdd:cd13988  74 LCPCGSLYTVLeePSNAyGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSvyKLTDFGAARELEDD 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVS--GTIPYTAPEVCQAG---RADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGA 259
Cdd:cd13988 154 EQFVSlyGTEEYLHPDMYERAvlrKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGP 213
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
53-371 1.17e-14

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: 74.67  E-value: 1.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS----KTKLKNFLREVSITNSLSSSPFIIKVfDVVFETEDCYVFAQ 128
Cdd:cd05602   9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKailkKKEEKHIMSERNVLLKNVKHPFLVGL-HFSFQTTDKLYFVL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVkLADFGMTR---RVGCRV 205
Cdd:cd05602  88 DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILL-DSQGHIV-LTDFGLCKeniEPNGTT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeefvrwqrGRLPGLPSQWR-RF 284
Cdd:cd05602 166 STFCGTPEYLAPEVLHKQ-----PYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMY---------DNILNKPLQLKpNI 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 285 TEPALRMFQRLLALEPERRGPAKEVFRFLK-HELTSELRRRPSHRARKPPGDRPPAAGPLRLEAPGPlkrtVLTEsgsgs 363
Cdd:cd05602 232 TNSARHLLEGLLQKDRTKRLGAKDDFTEIKnHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDP----EFTD----- 302

                ....*...
gi 66773086 364 RPAPPAVG 371
Cdd:cd05602 303 EPVPNSIG 310
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
148-313 1.28e-14

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: 73.33  E-value: 1.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 148 EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKR-VSGTIPYTAPEVCQagraD 226
Cdd:cd14112  98 EEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKLGKVpVDGDTDWASPEFHN----P 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 227 GLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQwrrFTEPALRMFQRLLALEPERRGPA 306
Cdd:cd14112 174 ETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKENVIFVKCRPNLIFVE---ATQEALRFATWALKKSPTRRMRT 250

                ....*....
gi 66773086 307 KEVF--RFL 313
Cdd:cd14112 251 DEALehRWL 259
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
53-198 1.29e-14

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: 74.89  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFDVVFETEDCYVFaQE 129
Cdd:cd05629   3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVlaeSDSPWVVSLYYSFQDAQYLYLI-ME 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMT 198
Cdd:cd05629  82 FLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI-DRG-GHIKLSDFGLS 148
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
53-254 1.50e-14

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: 72.96  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKG----TGTKMALKFVNKSK----TKLKNFL---REVSITNSLSSSPF---IIKVFDVvF 118
Cdd:cd14101   2 YTMGNLLGKGGFGTV----YAGhrisDGLQVAIKQISRNRvqqwSKLPGVNpvpNEVALLQSVGGGPGhrgVIRLLDW-F 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVFAQEYA-PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVKLADFGM 197
Cdd:cd14101  77 EIPEGFLLVLERPqHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV-DLRTGDIKLIDFGS 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 198 trrvGCRVK-----RVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14101 156 ----GATLKdsmytDFDGTRVYSPPEWILYHQYHALP----ATVWSLGILLYDMVCGDIPFE 209
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
59-319 1.54e-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: 73.12  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT---GTKMALKFVNK---SKTKLKnFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEYAP 132
Cdd:cd05085   4 LGKGNFGEV----YKGTlkdKTPVAVKTCKEdlpQELKIK-FLSEARILKQYDH-PNIVKLIGVCTQRQPIYI-VMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQvglpEDTVKrCVQQLGLALD------FMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRVK 206
Cdd:cd05085  77 GGDFLSFLRKK----KDELK-TKQLVKFSLDaaagmaYLESKNCIHRDLAARNCLVGENNA--LKISDFGMSRQEDDGVY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSG----TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAfFEEFVRWQRGRLPglpsqw 281
Cdd:cd05085 150 SSSGlkqiPIKWTAPEALNYGR-----YSSESDVWSFGILLWETFSlGVCPYPGMTNQQA-REQVEKGYRMSAP------ 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 66773086 282 RRFTEPALRMFQRLLALEPERRGPAKEvfrfLKHELTS 319
Cdd:cd05085 218 QRCPEDIYKIMQRCWDYNPENRPKFSE----LQKELAA 251
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
53-260 1.54e-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: 73.93  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSS--PFIIkVFDVVFETEDCYVF 126
Cdd:cd14223   2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTGdcPFIV-CMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd14223  81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL--DEFGHVRISDLGLACDFSKKKP 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 207 RVS-GTIPYTAPEVCQagraDGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd14223 159 HASvGTHGYMAPEVLQ----KGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 209
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
53-260 2.14e-14

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: 73.94  E-value: 2.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSS--PFIIkVFDVVFETEDCYVF 126
Cdd:cd05633   7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTGdcPFIV-CMTYAFHTPDKLCF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd05633  86 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGHVRISDLGLACDFSKKKP 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 207 RVS-GTIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd05633 164 HASvGTHGYMAPEVLQKGT----AYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 214
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
53-313 2.97e-14

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: 72.52  E-value: 2.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKnflREVSITNSLSSsPFIIKVFDVVFETEDC--------- 123
Cdd:cd14047   8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAE---REVKALAKLDH-PNIVRYNGCWDGFDYDpetsssnss 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 -----YVFAQ-EYAPAGDLFDIIPPQVGLPEDTVK--RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADF 195
Cdd:cd14047  84 rsktkCLFIQmEFCEKGTLESWIEKRNGEKLDKVLalEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDT--GKVKIGDF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 196 GMTRRVGCRVKRVS--GTIPYTAPEvcQAGRADglaVDTGVDVWAFGVLIFCVLtgnfpWEAASGadafFEEFVRWQRGR 273
Cdd:cd14047 162 GLVTSLKNDGKRTKskGTLSYMSPE--QISSQD---YGKEVDIYALGLILFELL-----HVCDSA----FEKSKFWTDLR 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 274 LPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFRFL 313
Cdd:cd14047 228 NGILPDIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
126-314 3.47e-14

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: 72.26  E-value: 3.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYAPAGDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD---RECRRVKLADFGMT 198
Cdd:cd14000  85 LVLELAPLGSLDHLLqqdsRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypNSAIIIKIADYGIS 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRVgCR--VKRVSGTIPYTAPEVcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEaasGADAFFEEFVRWQRGRLPg 276
Cdd:cd14000 165 RQC-CRmgAKGSEGTPGFRAPEI----ARGNVIYNEKVDVFSFGMLLYEILSGGAPMV---GHLKFPNEFDIHGGLRPP- 235
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 66773086 277 lpsqwrrFTEPALRMFQRLLAL-------EPERRGPAKEVFRFLK 314
Cdd:cd14000 236 -------LKQYECAPWPEVEVLmkkcwkeNPQQRPTAVTVVSILN 273
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
49-281 3.58e-14

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: 73.20  E-value: 3.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFE-----TEDC 123
Cdd:cd14227  13 MTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYEcfqhkNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEyapAGDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD--RECRRVKLADFGMTR 199
Cdd:cd14227  93 LVFEML---EQNLYDFLKQNkfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpsRQPYRVKVIDFGSAS 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 RVGcrvKRVSGTIP----YTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGnfpWEAASGADAFFEefVRWQrGRLP 275
Cdd:cd14227 170 HVS---KAVCSTYLqsryYRAPEIIL-----GLPFCEAIDMWSLGCVIAELFLG---WPLYPGASEYDQ--IRYI-SQTQ 235

                ....*.
gi 66773086 276 GLPSQW 281
Cdd:cd14227 236 GLPAEY 241
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
57-328 4.33e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 72.70  E-value: 4.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSSpFIIKVfDVVFETEDCYVFAQEYAP 132
Cdd:cd05632   8 RVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesmALNEKQILEKVNSQ-FVVNL-AYAYETKDALCLVLTIMN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDL----FDIIPPqvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV--GCRVK 206
Cdd:cd05632  86 GGDLkfhiYNMGNP--GFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYG--HIRISDLGLAVKIpeGESIR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQAGRAdGLAvdtgVDVWAFGVLIFCVLTGNFPWEAASgadaffEEFVRWQRGR--LPGLPSQWRRF 284
Cdd:cd05632 162 GRVGTVGYMAPEVLNNQRY-TLS----PDYWGLGCLIYEMIEGQSPFRGRK------EKVKREEVDRrvLETEEVYSAKF 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 66773086 285 TEPALRMFQRLLALEPERRGPAKEvfrflkhELTSELRRRPSHR 328
Cdd:cd05632 231 SEEAKSICKMLLTKDPKQRLGCQE-------EGAGEVKRHPFFR 267
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
51-310 4.81e-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: 71.89  E-value: 4.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS-------KTKLKnflREVSITNSLSSsPFIIKvFDVVFETEDC 123
Cdd:cd14187   7 RRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSlllkphqKEKMS---MEIAIHRSLAH-QHVVG-FHGFFEDNDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRV-- 201
Cdd:cd14187  82 VYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDD--MEVKIGDFGLATKVey 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 202 -GCRVKRVSGTIPYTAPEV-CQAGRAdglavdTGVDVWAFGVLIFCVLTGNFPWEAAsgadAFFEEFVRWQRGRLpGLPs 279
Cdd:cd14187 160 dGERKKTLCGTPNYIAPEVlSKKGHS------FEVDIWSIGCIMYTLLVGKPPFETS----CLKETYLRIKKNEY-SIP- 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 66773086 280 qwRRFTEPALRMFQRLLALEPERRGPAKEVF 310
Cdd:cd14187 228 --KHINPVAASLIQKMLQTDPTARPTINELL 256
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
58-260 5.64e-14

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 71.60  E-value: 5.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGkvdlVVYKGTGT-------KMALKFVNKSKTKLKN----FLREVSITNSLSSsPFIIKVFDVVFETEDCYVF 126
Cdd:cd05040   2 KLGDGSFG----VVRRGEWTtpsgkviQVAVKCLKSDVLSQPNamddFLKEVNAMHSLDH-PNLIRLYGVVLSSPLMMVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aqEYAPAGDLFDII-PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVG--- 202
Cdd:cd05040  77 --ELAPLGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKD--KVKIGDFGLMRALPqne 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 203 -CRV----KRVSgtIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAD 260
Cdd:cd05040 153 dHYVmqehRKVP--FAWCAPESLKTRK-----FSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQ 209
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
58-254 6.87e-14

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: 71.26  E-value: 6.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVdlvvYKGT--GTKMALKFVNKSKtklKNFLREVSITNSLSSS----PFIIKVFdvvfETEDCYVFAQ--- 128
Cdd:cd13979  10 PLGSGGFGSV----YKATykGETVAVKIVRRRR---KNRASRQSFWAELNAArlrhENIVRVL----AAETGTDFASlgl 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 ---EYAPAGDLFDIIppQVGLPEDTVKRCVQ---QLGLALDFMHGRQLVHRDIKPENVLLFDRE-CrrvKLADFGMTRR- 200
Cdd:cd13979  79 iimEYCGNGTLQQLI--YEGSEPLPLAHRILislDIARALRFCHSHGIVHLDVKPANILISEQGvC---KLCDFGCSVKl 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 201 -----VGCRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd13979 154 gegneVGTPRSHIGGTYTYRAPELLK-----GERVTPKADIYSFGITLWQMLTRELPYA 207
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
49-281 7.04e-14

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: 72.43  E-value: 7.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSP-----FIIKVFDVVFETEDC 123
Cdd:cd14228  13 MTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEyapAGDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD--RECRRVKLADFGMTR 199
Cdd:cd14228  93 LVFEML---EQNLYDFLKQNkfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFGSAS 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 RVGcrvKRVSGTIP----YTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGnfpWEAASGADAFFEefVRWQrGRLP 275
Cdd:cd14228 170 HVS---KAVCSTYLqsryYRAPEIIL-----GLPFCEAIDMWSLGCVIAELFLG---WPLYPGASEYDQ--IRYI-SQTQ 235

                ....*.
gi 66773086 276 GLPSQW 281
Cdd:cd14228 236 GLPAEY 241
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
54-260 7.33e-14

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: 71.61  E-value: 7.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKvdlvVYKGTG---------TKMALK--FVNKSKTKLKNFLREVSITNSLsSSPFIIKVFDVVFETED 122
Cdd:cd05032   9 TLIRELGQGSFGM----VYEGLAkgvvkgepeTRVAIKtvNENASMRERIEFLNEASVMKEF-NCHHVVRLLGVVSTGQP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVFaQEYAPAGDL----------FDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKL 192
Cdd:cd05032  84 TLVV-MELMAKGDLksylrsrrpeAENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMV--AEDLTVKI 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086 193 ADFGMTRRVGCR---VKRVSGTIP--YTAPEVCQagraDGLaVDTGVDVWAFGVLIfcvltgnfpWEAASGAD 260
Cdd:cd05032 161 GDFGMTRDIYETdyyRKGGKGLLPvrWMAPESLK----DGV-FTTKSDVWSFGVVL---------WEMATLAE 219
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
59-258 7.37e-14

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: 71.22  E-value: 7.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKG--TGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETED-CYVFaqEYAPAGD 135
Cdd:cd14146   2 IGVGGFGKVYRATWKGqeVAVKAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNlCLVM--EFARGGT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDIIPPQVGLPEDTVKRCVQ---------QLGLALDFMHGRQLV---HRDIKPENVLLF-----DRECRR-VKLADFGM 197
Cdd:cd14146  80 LNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLekiehDDICNKtLKITDFGL 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 198 TRRVGCRVK-RVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASG 258
Cdd:cd14146 160 AREWHRTTKmSAAGTYAWMAPEVIKSS-----LFSKGSDIWSYGVLLWELLTGEVPYRGIDG 216
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
59-249 8.87e-14

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 71.00  E-value: 8.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYvFAQEYAPAGDLF 137
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKeLIRFDEEAQRNFLKEVKVMRSLDH-PNVLKFIGVLYKDKKLN-LITEYIPGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DII-PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR----------------- 199
Cdd:cd14154  79 DVLkDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLV--REDKTVVVADFGLARliveerlpsgnmspset 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 200 ----RVGCRVKR--VSGTIPYTAPEVcqagrADGLAVDTGVDVWAFGVlIFCVLTG 249
Cdd:cd14154 157 lrhlKSPDRKKRytVVGNPYWMAPEM-----LNGRSYDEKVDIFSFGI-VLCEIIG 206
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
51-246 9.05e-14

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: 70.94  E-value: 9.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSsPFIIkvfdvvfETEDCYV- 125
Cdd:cd06607   1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSysgkQSTEKWQDIIKEVKFLRQLRH-PNTI-------EYKGCYLr 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 -----FAQEY--APAGDLFDIIppQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMT 198
Cdd:cd06607  73 ehtawLVMEYclGSASDIVEVH--KKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILL--TEPGTVKLADFGSA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 199 RRVgCRVKRVSGTIPYTAPEVCqagradgLAVDTG-----VDVWAFGvlIFCV 246
Cdd:cd06607 149 SLV-CPANSFVGTPYWMAPEVI-------LAMDEGqydgkVDVWSLG--ITCI 191
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
58-329 9.65e-14

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: 71.22  E-value: 9.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL-REVSITNSLSSSPfIIKVFDVVFETEDCYVfAQEYAPAGDL 136
Cdd:cd06658  29 KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLfNEVVIMRDYHHEN-VVDMYNSYLVGDELWV-VMEFLEGGAL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPPQVGLPEDTVKRCVQQLGlALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRV---KRVSGTIP 213
Cdd:cd06658 107 TDIVTHTRMNEEQIATVCLSVLR-ALSYLHNQGVIHRDIKSDSILLTSDG--RIKLSDFGFCAQVSKEVpkrKSLVGTPY 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 214 YTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPWeaasgadaffeefvrwqrgrlpglpsqwrrFTEPALRMFQ 293
Cdd:cd06658 184 WMAPEVISR-----LPYGTEVDIWSLGIMVIEMIDGEPPY------------------------------FNEPPLQAMR 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 66773086 294 RLLALEPERRGPAKEVFRFLKHELTSELRRRPSHRA 329
Cdd:cd06658 229 RIRDNLPPRVKDSHKVSSVLRGFLDLMLVREPSQRA 264
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
51-253 1.00e-13

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: 70.78  E-value: 1.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTgtKMALKFVNKSKTKlKNFLREVSITNSLSSSPfIIKVFDVVFETEDCYVFAQEY 130
Cdd:cd05082   6 KELKLLQTIGKGEFGDVMLGDYRGN--KVAVKCIKNDATA-QAFLAEASVMTQLRHSN-LVQLLGVIVEEKGGLYIVTEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVKRV 208
Cdd:cd05082  82 MAKGSLVDYLRSRgrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV--SEDNVAKVSDFGLTKEASSTQDTG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 209 SGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05082 160 KLPVKWTAPEALREKK-----FSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
59-253 1.03e-13

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: 71.45  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNK----SKTKLKNFLREVSITNSLSSsPFIIKVfDVVFETEDCYVFAQEYAPAG 134
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKahivSRSEVTHTLAERTVLAQVDC-PFIVPL-KFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR---RVGCRVKRVSGT 211
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL--DYTGHIALCDFGLCKlnmKDDDKTNTFCGT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 66773086 212 IPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd05585 158 PEYLAPELLL-----GHGYTKAVDWWTLGVLLYEMLTGLPPF 194
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
53-241 1.09e-13

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: 71.29  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKG----TGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFET-----EDC 123
Cdd:cd06637   8 FELVELVGNGTYGQV----YKGrhvkTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKnppgmDDQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV 201
Cdd:cd06637  84 LWLVMEFCGAGSVTDLIKNTKGntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQL 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 66773086 202 GCRVKRVS---GTIPYTAPEVCQAGRADGLAVDTGVDVWAFGV 241
Cdd:cd06637 162 DRTVGRRNtfiGTPYWMAPEVIACDENPDATYDFKSDLWSLGI 204
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
52-255 1.15e-13

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: 70.85  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN----FLREVSITNSLSSsPFIIKVfDVVFETEDCYVFA 127
Cdd:cd05605   1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNS-RFVVSL-AYAYETKDALCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDL----FDIIPPqvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-- 201
Cdd:cd05605  79 LTIMNGGDLkfhiYNMGNP--GFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHG--HVRISDLGLAVEIpe 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 202 GCRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd05605 155 GETIRGRVGTVGYMAPEVVKNER-----YTFSPDWWGLGCLIYEMIEGQAPFRA 203
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
51-311 1.26e-13

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: 70.43  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT----KLKNFLREVSITNSLSSSpFIIKVFDVVFETEDCYVF 126
Cdd:cd14188   1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVskphQREKIDKEIELHRILHHK-HVVQFYHYFEDKENIYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AqEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvlLFDRECRRVKLADFGMTRRV---GC 203
Cdd:cd14188  80 L-EYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN--FFINENMELKVGDFGLAARLeplEH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQagrADGLAVDTgvDVWAFGVLIFCVLTGNFPWEAASgadafFEEFVRWQRGRLPGLPSQwrr 283
Cdd:cd14188 157 RRRTICGTPNYLSPEVLN---KQGHGCES--DIWALGCVMYTMLLGRPPFETTN-----LKETYRCIREARYSLPSS--- 223
                       250       260
                ....*....|....*....|....*...
gi 66773086 284 FTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14188 224 LLAPAKHLIASMLSKNPEDRPSLDEIIR 251
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
59-257 1.38e-13

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: 70.53  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLsSSPFIIKVFDVVFETEDCYVFAqEYAPAGDLFD 138
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEI-KHPNLVQLLGVCTREPPFYIIT-EFMPYGNLLD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 II--PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR---------RVGCRVKr 207
Cdd:cd05052  92 YLreCNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLV--GENHLVKVADFGLSRlmtgdtytaHAGAKFP- 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 208 vsgtIPYTAPEvcqagradGLAVD---TGVDVWAFGVLIfcvltgnfpWEAAS 257
Cdd:cd05052 169 ----IKWTAPE--------SLAYNkfsIKSDVWAFGVLL---------WEIAT 200
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
53-270 1.39e-13

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: 71.61  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFDVVFETEDCYVFaQE 129
Cdd:cd05628   3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDIlveADSLWVVKMFYSFQDKLNLYLI-ME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGM------------ 197
Cdd:cd05628  82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKG--HVKLSDFGLctglkkahrtef 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 ------------------TRRVGCRVKR--------VSGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNF 251
Cdd:cd05628 160 yrnlnhslpsdftfqnmnSKRKAETWKRnrrqlafsTVGTPDYIAPEVFMQTGYNKLC-----DWWSLGVIMYEMLIGYP 234
                       250
                ....*....|....*....
gi 66773086 252 PWEAASGADAfFEEFVRWQ 270
Cdd:cd05628 235 PFCSETPQET-YKKVMNWK 252
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
53-197 1.42e-13

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: 71.63  E-value: 1.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFDVVFETEDCYVFaQE 129
Cdd:cd05627   4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDIlveADGAWVVKMFYSFQDKRNLYLI-ME 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGM 197
Cdd:cd05627  83 FLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKG--HVKLSDFGL 148
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
48-335 1.50e-13

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: 71.52  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCY 124
Cdd:cd07880  12 EVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfqSELFAKRAYRELRLLKHMKHEN-VIGLLDVFTPDLSLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEY--AP--AGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFGMTRR 200
Cdd:cd07880  91 RFHDFYlvMPfmGTDLGKLMKHE-KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGN-LAVNEDC-ELKILDFGLARQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCRVKRVSGTIPYTAPEVCqagrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFE----------EFV-RW 269
Cdd:cd07880 168 TDSEMTGYVVTRWYRAPEVI----LNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEimkvtgtpskEFVqKL 243
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 270 Q----RGRLPGLPSQWR-------RFTEP-ALRMFQRLLALEPERRGPAKEVfrfLKHELTSELrRRPSHRARKPPGD 335
Cdd:cd07880 244 QsedaKNYVKKLPRFRKkdfrsllPNANPlAVNVLEKMLVLDAESRITAAEA---LAHPYFEEF-HDPEDETEAPPYD 317
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
57-260 1.50e-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: 70.00  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFaQEYAPAGDL 136
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGT-TKVAVKTLKPGTMSPEAFLQEAQIMKKLRH-DKLVQLYAVCSDEEPIYIV-TELMSKGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDII--PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV--GCRVKRVSGTI 212
Cdd:cd05034  78 LDYLrtGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNV--CKVADFGLARLIedDEYTAREGAKF 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 213 P--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAD 260
Cdd:cd05034 156 PikWTAPEAALYGR-----FTIKSDVWSFGILLYEIVTyGRVPYPGMTNRE 201
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
48-247 1.65e-13

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: 71.24  E-value: 1.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL---KNFLREVSITNSLSSsPFIIKVFDVVFETE--- 121
Cdd:cd07855   2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVttaKRTLRELKILRHFKH-DNIIAIRDILRPKVpya 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 ---DCYVFA--QEyapaGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFG 196
Cdd:cd07855  81 dfkDVYVVLdlME----SDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSN-LLVNENC-ELKIGDFG 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 197 MTRRVGCRVKRVS-------GTIPYTAPEVCqagradgLAVD---TGVDVWAFGvlifCVL 247
Cdd:cd07855 155 MARGLCTSPEEHKyfmteyvATRWYRAPELM-------LSLPeytQAIDMWSVG----CIF 204
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
51-319 1.66e-13

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: 70.16  E-value: 1.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTgTKMALKFV-NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqE 129
Cdd:cd05148   6 EEFTLERKLGSGYFGEVWEGLWKNR-VRVAIKILkSDDLLKQQDFQKEVQALKRLRH-KHLISLFAVCSVGEPVYIIT-E 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIppqvGLPEDTVKRCVQQLGLA------LDFMHGRQLVHRDIKPENVLLFDR-ECrrvKLADFGMTRRVG 202
Cdd:cd05148  83 LMEKGSLLAFL----RSPEGQVLPVASLIDMAcqvaegMAYLEEQNSIHRDLAARNILVGEDlVC---KVADFGLARLIK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSGT-IPY--TAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAdaffEEFVRWQRG-RLPGL 277
Cdd:cd05148 156 EDVYLSSDKkIPYkwTAPEAASHGT-----FSTKSDVWSFGILLYEMFTyGQVPYPGMNNH----EVYDQITAGyRMPCP 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 278 PSqwrrfTEPAL-RMFQRLLALEPERRgPAkevFRFLKHELTS 319
Cdd:cd05148 227 AK-----CPQEIyKIMLECWAAEPEDR-PS---FKALREELDN 260
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
59-313 1.77e-13

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. 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 LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 69.98  E-value: 1.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTgtKMALKFVNKsKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEdcyVFAQEYAPAGDLFD 138
Cdd:cd14068   2 LGDGGFGSVYRAVYRGE--DVAVKIFNK-HTSFRLLRQELVVLSHLHH-PSLVALLAAGTAPR---MLVMELAPKGSLDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQ-VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD--RECRRV-KLADFGMTRRVgCR--VKRVSGTI 212
Cdd:cd14068  75 LLQQDnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlyPNCAIIaKIADYGIAQYC-CRmgIKTSEGTP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 213 PYTAPEVCQAgradGLAVDTGVDVWAFGVLIFCVLTGNfpwEAASGADAFFEEFVRWQ-RGRLPGLPSQWRRFTEPALR- 290
Cdd:cd14068 154 GFRAPEVARG----NVIYNQQADVYSFGLLLYDILTCG---ERIVEGLKFPNEFDELAiQGKLPDPVKEYGCAPWPGVEa 226
                       250       260
                ....*....|....*....|...
gi 66773086 291 MFQRLLALEPERRGPAKEVFRFL 313
Cdd:cd14068 227 LIKDCLKENPQCRPTSAQVFDIL 249
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
59-252 1.89e-13

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: 70.08  E-value: 1.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVN--KSKTKLKNFLREVSITnSLSSSPFIIKVFDVVFETEDCYVFaQEYAPAGDL 136
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKIIDleEAEDEIEDIQQEITVL-SQCDSPYVTKYYGSYLKGTKLWII-MEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIppQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV-GCRVKRVS--GTI 212
Cdd:cd06640  90 LDLL--RAGpFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLL--SEQGDVKLADFGVAGQLtDTQIKRNTfvGTP 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 66773086 213 PYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd06640 166 FWMAPEVIQQS-----AYDSKADIWSLGITAIELAKGEPP 200
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
53-253 2.05e-13

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: 69.98  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALK--FVNKSKTKLKNflrEVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEY 130
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKveSKSQPKQVLKM---EVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APA-GDLFDIIPPQVgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL--FDRECRRVKLADFGMTRRV------ 201
Cdd:cd14017  79 GPNlAELRRSQPRGK-FSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrGPSDERTVYILDFGLARQYtnkdge 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 202 GCRVKRVS----GTIPYTAPEV---CQAGRADglavdtgvDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14017 158 VERPPRNAagfrGTVRYASVNAhrnKEQGRRD--------DLWSWFYMLIEFVTGQLPW 208
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
59-262 2.34e-13

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: 69.68  E-value: 2.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKM--ALKFVNK--SKTKLKNFLREVSITNSLSSSPFIIKVFDVVfETEDCYVFAQEYAPAG 134
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEyaSKDDHRDFAGELEVLCKLGHHPNIINLLGAC-EHRGYLYLAIEYAPHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDII--------PPQVGLPEDTVKRCVQQ--------LGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMT 198
Cdd:cd05047  82 NLLDFLrksrvletDPAFAIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYV--AKIADFGLS 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGCRVKRVSGTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAF 262
Cdd:cd05047 160 RGQEVYVKKTMGRLPvrWMAIESLNYS-----VYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELY 221
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
53-329 2.98e-13

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: 70.08  E-value: 2.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKN-FLREVSITNSlSSSPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd06650   7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIHlEIKPAIRNqIIRELQVLHE-CNSPYIVGFYGAFYSDGEISI-CMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDREcrRVKLADFGMT-RRVGCRVKRV 208
Cdd:cd06650  85 MDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRG--EIKLCDFGVSgQLIDSMANSF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFP--------WEAASGADAFFEEFVRWQRGRLPGLP-S 279
Cdd:cd06650 163 VGTRSYMSPE-----RLQGTHYSVQSDIWSMGLSLVEMAVGRYPipppdakeLELMFGCQVEGDAAETPPRPRTPGRPlS 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 280 QWRRFTEPALRMFQRL--LALEPERRGPAKEVFRFLKHELTSELRRRPSHRA 329
Cdd:cd06650 238 SYGMDSRPPMAIFELLdyIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERA 289
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
54-271 3.66e-13

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: 69.28  E-value: 3.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKgTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIikVFDVVFETEDCYVFAqEYAPA 133
Cdd:cd05073  14 KLEKKLGAGQFGEVWMATYN-KHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLV--KLHAVVTKEPIYIIT-EFMAK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRV--GCRVKRVS 209
Cdd:cd05073  90 GSLLDFLKSDEGskQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILV--SASLVCKIADFGLARVIedNEYTAREG 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 210 GTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAF--FEEFVRWQR 271
Cdd:cd05073 168 AKFPikWTAPEAINFG-----SFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIraLERGYRMPR 229
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
53-252 4.10e-13

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: 69.27  E-value: 4.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKGTgTKMALKFVNKSKTKLKN-------FLREVSITNSLSSSPfIIKVFDVVfETEDCYV 125
Cdd:cd07871   7 YVKLDKLGEGTYA----TVFKGR-SKLTENLVALKEIRLEHeegapctAIREVSLLKNLKHAN-IVTLHDII-HTERCLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYAPA---------GDLFDIippqvglpeDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFG 196
Cdd:cd07871  80 LVFEYLDSdlkqyldncGNLMSM---------HNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKG--ELKLADFG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 197 MTRRVGCRVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGN--FP 252
Cdd:cd07871 149 LARAKSVPTKTYSNevvTLWYRPPDVLLGST----EYSTPIDMWGVGCILYEMATGRpmFP 205
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
48-252 4.56e-13

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: 70.07  E-value: 4.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPfIIKVFDV------VF 118
Cdd:cd07877  14 EVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfqSIIHAKRTYRELRLLKHMKHEN-VIGLLDVftparsLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVFAqeYAPAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFGMT 198
Cdd:cd07877  93 EFNDVYLVT--HLMGADLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN-LAVNEDC-ELKILDFGLA 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 199 RRVGCRVKRVSGTIPYTAPEVcqagRADGLAVDTGVDVWAFGVLIFCVLTGN--FP 252
Cdd:cd07877 168 RHTDDEMTGYVATRWYRAPEI----MLNWMHYNQTVDIWSVGCIMAELLTGRtlFP 219
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
53-325 5.14e-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: 69.26  E-value: 5.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKGTgTKMALKFVNKSKTKLKN-------FLREVSITNSLSSSPfIIKVFDVVfETEDCYV 125
Cdd:cd07873   4 YIKLDKLGEGTYA----TVYKGR-SKLTDNLVALKEIRLEHeegapctAIREVSLLKDLKHAN-IVTLHDII-HTEKSLT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYAPAgDL---FDIIPPQVGLpeDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVG 202
Cdd:cd07873  77 LVFEYLDK-DLkqyLDDCGNSINM--HNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERG--ELKLADFGLARAKS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVKRVSG---TIPYTAPEVCqAGRADglaVDTGVDVWAFGVLIFCVLTGN--FPWEAASGADAFF-------------- 263
Cdd:cd07873 152 IPTKTYSNevvTLWYRPPDIL-LGSTD---YSTQIDMWGVGCIFYEMSTGRplFPGSTVEEQLHFIfrilgtpteetwpg 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 264 ----EEFVRWQ--RGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFRFLK-HELTSELRRRP 325
Cdd:cd07873 228 ilsnEEFKSYNypKYRADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYfHSLGERIHKLP 296
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
110-257 6.49e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 70.05  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  110 IIKVFDVvFETEDCYVFAQEYAPAGDLFDIIPPQVG--LP--EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR 185
Cdd:PTZ00267 127 IVKHFDD-FKSDDKLLLIMEYGSGGDLNKQIKQRLKehLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPT 205
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086  186 ECrrVKLADFGMTRRVGCRV-----KRVSGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:PTZ00267 206 GI--IKLGDFGFSKQYSDSVsldvaSSFCGTPYYLAPELWERKRYSKKA-----DMWSLGVILYELLTLHRPFKGPS 275
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
54-273 6.82e-13

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror 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: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 68.56  E-value: 6.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKV---DLVVYKGTGTKM-----ALKFVNKSKTKlKNFLREVSITNSLsSSPFIIKVFDVVFETE-DCY 124
Cdd:cd05048   8 RFLEELGEGAFGKVykgELLGPSSEESAIsvaikTLKENASPKTQ-QDFRREAELMSDL-QHPNIVCLLGVCTKEQpQCM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFaqEYAPAGDLFDII----P---PQVGLPEDTVKRCVQQLGL---------ALDFMHGRQLVHRDIKPENVLLFDRecR 188
Cdd:cd05048  86 LF--EYMAHGDLHEFLvrhsPhsdVGVSSDDDGTASSLDQSDFlhiaiqiaaGMEYLSSHHYVHRDLAARNCLVGDG--L 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 189 RVKLADFGMTRRV-GCRVKRVSGT----IPYTAPEVCQAGRadgLAVDTgvDVWAFGVLIfcvltgnfpWEAAS-GADAF 262
Cdd:cd05048 162 TVKISDFGLSRDIySSDYYRVQSKsllpVRWMPPEAILYGK---FTTES--DVWSFGVVL---------WEIFSyGLQPY 227
                       250
                ....*....|....*
gi 66773086 263 F----EEFVRWQRGR 273
Cdd:cd05048 228 YgysnQEVIEMIRSR 242
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
54-303 7.66e-13

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: 68.29  E-value: 7.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLR-EVSITNSLSSSPFIIKVFDVVFEtedcYVFAQEYAP 132
Cdd:cd13975   3 KLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLAlEFHYTRSLPKHERIVSLHGSVID----YSYGGGSSI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 A---------GDLFDIIPPQVGLPEdtvkrcvqQLGLALD------FMHGRQLVHRDIKPENVLLfDREcRRVKLADFGM 197
Cdd:cd13975  79 AvllimerlhRDLYTGIKAGLSLEE--------RLQIALDvvegirFLHSQGLVHRDIKLKNVLL-DKK-NRAKITDLGF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCRVKRVSGTIPYTAPEVCQAgradglAVDTGVDVWAFGVLIFCVLTGNFPWEAAsgadafFEEFVR----WQRGR 273
Cdd:cd13975 149 CKPEAMMSGSIVGTPIHMAPELFSG------KYDNSVDVYAFGILFWYLCAGHVKLPEA------FEQCASkdhlWNNVR 216
                       250       260       270
                ....*....|....*....|....*....|
gi 66773086 274 LPGLPSQWRRFTEPALRMFQRLLALEPERR 303
Cdd:cd13975 217 KGVRPERLPVFDEECWNLMEACWSGDPSQR 246
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-244 8.47e-13

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: 68.13  E-value: 8.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKGT----GTKMALKFVN-----KSKTKlKNFLREVSITNSLSSsPFIIKVFDVVFETEDC 123
Cdd:cd08228   4 FQIEKKIGRGQFSEV----YRATclldRKPVALKKVQifemmDAKAR-QDCVKEIDLLKQLNH-PNVIKYLDSFIEDNEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVfAQEYAPAGDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVllFDRECRRVKLADFGMTR 199
Cdd:cd08228  78 NI-VLELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANV--FITATGVVKLGDLGLGR 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 66773086 200 RVGCRVK---RVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIF 244
Cdd:cd08228 155 FFSSKTTaahSLVGTPYYMSPE-----RIHENGYNFKSDIWSLGCLLY 197
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
53-308 9.00e-13

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: 69.04  E-value: 9.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN---FLREVSITNSLSSsPFIIKVFDVVF-----ETEDCY 124
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDatrILREIKLLRLLRH-PDIVEIKHIMLppsrrEFKDIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYApaGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRrvgCR 204
Cdd:cd07859  81 VVFELME--SDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILA-NADC-KLKICDFGLAR---VA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIPYT---------APEVCQAGRAdglAVDTGVDVWAFGVLIFCVLTGN--FPW-------------------E 254
Cdd:cd07859 154 FNDTPTAIFWTdyvatrwyrAPELCGSFFS---KYTPAIDIWSIGCIFAEVLTGKplFPGknvvhqldlitdllgtpspE 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 255 AASG-----ADAFFEEFvrwqRGRLPGLPSQWRRFTEP-ALRMFQRLLALEPERRGPAKE 308
Cdd:cd07859 231 TISRvrnekARRYLSSM----RKKQPVPFSQKFPNADPlALRLLERLLAFDPKDRPTAEE 286
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
58-315 9.68e-13

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: 68.51  E-value: 9.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL-REVSITNSLSSSPfIIKVFDVVFETEDCYVfAQEYAPAGDL 136
Cdd:cd06657  27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHEN-VVEMYNSYLVGDELWV-VMEFLEGGAL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPPQVGLPEDTVKRCVQQLGlALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRVKR---VSGTIP 213
Cdd:cd06657 105 TDIVTHTRMNEEQIAAVCLAVLK-ALSVLHAQGVIHRDIKSDSILLTHDG--RVKLSDFGFCAQVSKEVPRrksLVGTPY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 214 YTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTGNFPWeaasgadaFFEEFVRWQRGRLPGLPSQWRRF--TEPALRM 291
Cdd:cd06657 182 WMAPELISR-----LPYGPEVDIWSLGIMVIEMVDGEPPY--------FNEPPLKAMKMIRDNLPPKLKNLhkVSPSLKG 248
                       250       260
                ....*....|....*....|....*
gi 66773086 292 F-QRLLALEPERRGPAKEVfrfLKH 315
Cdd:cd06657 249 FlDRLLVRDPAQRATAAEL---LKH 270
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
59-249 1.00e-12

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: 68.06  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFEtEDCYVFAQEYAPAGDLF 137
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKeLIRFDEETQRTFLKEVKVMRCLEH-PNVLKFIGVLYK-DKRLNFITEYIKGGTLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DIIPPQvglpeDTVKRCVQQLGLALD------FMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR------------ 199
Cdd:cd14221  79 GIIKSM-----DSHYPWSQRVSFAKDiasgmaYLHSMNIIHRDLNSHNCLV--RENKSVVVADFGLARlmvdektqpegl 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 200 ---RVGCRVKR--VSGTIPYTAPEVCqagraDGLAVDTGVDVWAFGVLIfCVLTG 249
Cdd:cd14221 152 rslKKPDRKKRytVVGNPYWMAPEMI-----NGRSYDEKVDVFSFGIVL-CEIIG 200
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
44-241 1.12e-12

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: 67.76  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  44 LAASDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDC 123
Cdd:cd06645   4 LSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVfAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGC 203
Cdd:cd06645  84 WI-CMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNG--HVKLADFGVSAQITA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 66773086 204 RV-KRVS--GTIPYTAPEVCQAGRADGLavDTGVDVWAFGV 241
Cdd:cd06645 161 TIaKRKSfiGTPYWMAPEVAAVERKGGY--NQLCDIWAVGI 199
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
57-303 1.26e-12

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: 67.98  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSS---SPFIIKVfDVVFETEDCYVFAQEYAPA 133
Cdd:cd05608   7 RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAkvhSRFIVSL-AYAFQTKTDLCLVMTIMNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDL----FDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVG---CRVK 206
Cdd:cd05608  86 GDLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDG--NVRISDLGLAVELKdgqTKTK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEaASGADAFFEEFvrwQRGRLPGLPSQWRRFTE 286
Cdd:cd05608 164 GYAGTPGFMAPELLL-----GEEYDYSVDYFTLGVTLYEMIAARGPFR-ARGEKVENKEL---KQRILNDSVTYSEKFSP 234
                       250
                ....*....|....*..
gi 66773086 287 PALRMFQRLLALEPERR 303
Cdd:cd05608 235 ASKSICEALLAKDPEKR 251
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
53-252 1.33e-12

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: 68.23  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKN-FLREVSITNSlSSSPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd06615   3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHlEIKPAIRNqIIRELKVLHE-CNSPYIVGFYGAFYSDGEISI-CMEH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLfDIIPPQVG-LPEDTVKRCVQQLGLALDFMHG-RQLVHRDIKPENVLLFDR-ECrrvKLADFGMT-RRVGCRVK 206
Cdd:cd06615  81 MDGGSL-DQVLKKAGrIPENILGKISIAVLRGLTYLREkHKIMHRDVKPSNILVNSRgEI---KLCDFGVSgQLIDSMAN 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 207 RVSGTIPYTAPEVCQAGRadgLAVDTgvDVWAFGVLIFCVLTGNFP 252
Cdd:cd06615 157 SFVGTRSYMSPERLQGTH---YTVQS--DIWSLGLSLVEMAIGRYP 197
pknD PRK13184
serine/threonine-protein kinase PknD;
52-253 1.46e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 69.80  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK--SKTKL--KNFLREVSITNSLsSSPFIIKVFDVVFETEDCYvFA 127
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREdlSENPLlkKRFLREAKIAADL-IHPGIVPVYSICSDGDPVY-YT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  128 QEYAPAGDLFDIIPP---QVGLPED--------TVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-------------- 182
Cdd:PRK13184  81 MPYIEGYTLKSLLKSvwqKESLSKElaektsvgAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLglfgevvildwgaa 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086  183 FDRECRRVKLADFGMTRRVGCRVK-----RVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:PRK13184 161 IFKKLEEEDLLDIDVDERNICYSSmtipgKIVGTPDYMAPE-----RLLGVPASESTDIYALGVILYQMLTLSFPY 231
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
51-328 1.48e-12

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: 67.73  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYK----GTGTKMALKFVNKSKTK-LKNFLREVSITNSLSSSPfIIKVFDVVFET-EDCY 124
Cdd:cd14205   4 RHLKFLQQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQHSTEEhLRDFEREIEILKSLQHDN-IVKYKGVCYSAgRRNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPP-QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTR---- 199
Cdd:cd14205  83 RLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENEN--RVKIGDFGLTKvlpq 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 -RVGCRVKRvSGTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNfpwEAASGADAFFEEFVrwqrgrlpG 276
Cdd:cd14205 161 dKEYYKVKE-PGESPifWYAPESLTESK-----FSVASDVWSFGVVLYELFTYI---EKSKSPPAEFMRMI--------G 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 277 LPSQWRRFTEPALRMFQRLLALePERRGPAKEVFRFLKHELTSELRRRPSHR 328
Cdd:cd14205 224 NDKQGQMIVFHLIELLKNNGRL-PRPDGCPDEIYMIMTECWNNNVNQRPSFR 274
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
56-326 1.48e-12

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: 68.50  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFdVVFETEDCYVFAQEYAP 132
Cdd:cd05626   6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDIlaeADNEWVVKLY-YSFQDKDNLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR------------- 199
Cdd:cd05626  85 GGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI-DLD-GHIKLTDFGLCTgfrwthnskyyqk 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 ---------------------RVGCRVKRVS----------------GTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVL 242
Cdd:cd05626 163 gshirqdsmepsdlwddvsncRCGDRLKTLEqratkqhqrclahslvGTPNYIAPEVLLRKGYTQLC-----DWWSVGVI 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 243 IFCVLTGNFPWEAASGADAFFeEFVRWQRGRlpGLPSQwRRFTEPALRMFQRLLALEPER--RGPAKEVFR---FLKHEL 317
Cdd:cd05626 238 LFEMLVGQPPFLAPTPTETQL-KVINWENTL--HIPPQ-VKLSPEAVDLITKLCCSAEERlgRNGADDIKAhpfFSEVDF 313

                ....*....
gi 66773086 318 TSELRRRPS 326
Cdd:cd05626 314 SSDIRTQPA 322
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
59-303 1.61e-12

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: 67.36  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT--GTKMALKFVNKSKTKlknflrEVSITN----------SLSSSPFIIKVFDVVFETED-CYV 125
Cdd:cd14147  11 IGIGGFGKV----YRGSwrGELVAVKAARQDPDE------DISVTAesvrqearlfAMLAHPNIIALKAVCLEEPNlCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FaqEYAPAGDLFDIIPPQVGLPEDTVKRCVQqLGLALDFMHGRQLV---HRDIKPENVLLF------DRECRRVKLADFG 196
Cdd:cd14147  81 M--EYAAGGPLSRALAGRRVPPHVLVNWAVQ-IARGMHYLHCEALVpviHRDLKSNNILLLqpiendDMEHKTLKITDFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCRVK-RVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEefVRWQRGRLP 275
Cdd:cd14147 158 LAREWHKTTQmSAAGTYAWMAPEVIKAS-----TFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYG--VAVNKLTLP 230
                       250       260
                ....*....|....*....|....*...
gi 66773086 276 gLPSQWrrfTEPALRMFQRLLALEPERR 303
Cdd:cd14147 231 -IPSTC---PEPFAQLMADCWAQDPHRR 254
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
55-254 1.83e-12

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: 67.09  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEYAPAG 134
Cdd:cd05059   8 FLKELGSGQFGVVHLGKWRGK-IDVAIKMIKEGSMSEDDFIEEAKVMMKLSH-PKLVQLYGVCTKQRPIFI-VTEYMANG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGL--PEDTVKRCvQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV---------GC 203
Cdd:cd05059  85 CLLNYLRERRGKfqTEQLLEMC-KDVCEAMEYLESNGFIHRDLAARNCLVGEQNV--VKVSDFGLARYVlddeytssvGT 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 204 RVKrvsgtIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWE 254
Cdd:cd05059 162 KFP-----VKWSPPEVFMYSK-----FSSKSDVWSFGVLMWEVFSeGKMPYE 203
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
53-238 2.00e-12

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 67.58  E-value: 2.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKNFLREVSITNSLSSS-PFIIKVFDVVF------------ 118
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcNAPENVELALREFWALSSIQRQhPNVIQLEECVLqrdglaqrmshg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 -----------ET-----------EDCYV-FAQEYAPAGDLFDIIPPQVGLPEdTVKRCVQQLGLALDFMHGRQLVHRDI 175
Cdd:cd13977  82 ssksdlylllvETslkgercfdprSACYLwFVMEFCDGGDMNEYLLSRRPDRQ-TNTSFMLQLSSALAFLHRNQIVHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 176 KPENVLLFD-RECRRVKLADFGMTRRVG--------------CRVKRVSGTIPYTAPEVCQA---GRADGLAVdtGVDVW 237
Cdd:cd13977 161 KPDNILISHkRGEPILKVADFGLSKVCSgsglnpeepanvnkHFLSSACGSDFYMAPEVWEGhytAKADIFAL--GIIIW 238

                .
gi 66773086 238 A 238
Cdd:cd13977 239 A 239
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
57-253 2.22e-12

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: 66.48  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFEtEDCYVFAqEYAPAGDL 136
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMSPEAFLEEAQIMKKLRHDK-LVQLYAVVSE-EPIYIVT-EFMSKGSL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPPQVG----LPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR-ECrrvKLADFGMTR---------RVG 202
Cdd:cd14203  77 LDFLKDGEGkylkLPQ--LVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNlVC---KIADFGLARliedneytaRQG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 203 CRVKrvsgtIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd14203 152 AKFP-----IKWTAPEAALYGR-----FTIKSDVWSFGILLTELVTkGRVPY 193
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
53-241 2.34e-12

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: 66.98  E-value: 2.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVfAQEYAP 132
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWI-CMEYCG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRV-KRVS-- 209
Cdd:cd06646  90 GGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNG--DVKLADFGVAAKITATIaKRKSfi 167
                       170       180       190
                ....*....|....*....|....*....|..
gi 66773086 210 GTIPYTAPEVCQAGRADGLavDTGVDVWAFGV 241
Cdd:cd06646 168 GTPYWMAPEVAAVEKNGGY--NQLCDIWAVGI 197
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
58-268 2.44e-12

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: 66.89  E-value: 2.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKM--ALKF--VNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVfETEDcYVFAQEYAPA 133
Cdd:cd05115  11 ELGSGNFGCVKKGVYKMRKKQIdvAIKVlkQGNEKAVRDEMMREAQIMHQLDN-PYIVRMIGVC-EAEA-LMLVMEMASG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCR----VKRV 208
Cdd:cd05115  88 GPLNKFLSGKKDeITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQH--YAKISDFGLSKALGADdsyyKARS 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 209 SGTIP--YTAPEvCQAGRadglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAD--AFFEEFVR 268
Cdd:cd05115 166 AGKWPlkWYAPE-CINFR----KFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEvmSFIEQGKR 225
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
59-262 2.60e-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: 66.95  E-value: 2.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKM--ALKFVNK--SKTKLKNFLREVSITNSLSSSPFIIKVFDVVfETEDCYVFAQEYAPAG 134
Cdd:cd05089  10 IGEGNFGQVIKAMIKKDGLKMnaAIKMLKEfaSENDHRDFAGELEVLCKLGHHPNIINLLGAC-ENRGYLYIAIEYAPYG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVGLPED----------TVKRCVQQLGLALDFMHG------RQLVHRDIKPENVLLFDRECrrVKLADFGMT 198
Cdd:cd05089  89 NLLDFLRKSRVLETDpafakehgtaSTLTSQQLLQFASDVAKGmqylseKQFIHRDLAARNVLVGENLV--SKIADFGLS 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGCRVKRVSGTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAF 262
Cdd:cd05089 167 RGEEVYVKKTMGRLPvrWMAIESLNYS-----VYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELY 228
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
58-303 2.63e-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: 66.49  E-value: 2.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTGTKMALKFVNKS-KTKLKN-FLREVSITNSLSSsPFIIKVFDVVFETEDCYVfAQEYAPAGD 135
Cdd:cd05084   3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETlPPDLKAkFLQEARILKQYSH-PNIVRLIGVCTQKQPIYI-VMELVQGGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDIIPPQ-VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVGCRVKRVSG---T 211
Cdd:cd05084  81 FLTFLRTEgPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNV--LKISDFGMSREEEDGVYAATGgmkQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAffEEFVRwQRGRLPgLPSQWrrfTEPA 288
Cdd:cd05084 159 IPvkWTAPEALNYGR-----YSSESDVWSFGILLWETFSlGAVPYANLSNQQT--REAVE-QGVRLP-CPENC---PDEV 226
                       250
                ....*....|....*
gi 66773086 289 LRMFQRLLALEPERR 303
Cdd:cd05084 227 YRLMEQCWEYDPRKR 241
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
50-311 2.98e-12

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: 66.58  E-value: 2.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  50 TKHYELvRELGKGTYGKVDLVVYKGTGTKMALKfvnKSKTKL------KNFLREVSITNSLSSSPFIIKVFDVVFEtEDC 123
Cdd:cd14138   5 TEFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIK---RSKKPLagsvdeQNALREVYAHAVLGQHSHVVRYYSAWAE-DDH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQEYAPAGDLFDIIPPQVG----LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-------------FDRE 186
Cdd:cd14138  80 MLIQNEYCNGGSLADAISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegDEDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 187 CR--RV--KLADFGMTRRVGC-RVKRvsGTIPYTAPEVCQAGRADgLAvdtGVDVWAFGVLIFCvltgnfpweaASGADA 261
Cdd:cd14138 160 WAsnKVifKIGDLGHVTRVSSpQVEE--GDSRFLANEVLQENYTH-LP---KADIFALALTVVC----------AAGAEP 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 262 FFEEFVRW---QRGRLPGLPsqwRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14138 224 LPTNGDQWheiRQGKLPRIP---QVLSQEFLDLLKVMIHPDPERRPSAVALVK 273
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
56-248 3.55e-12

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: 66.49  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYK----GTGTKMALKFVN--KSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCYV-FAQ 128
Cdd:cd05079   9 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKpeSGGNHIADLKKEIEILRNLYHEN-IVKYKGICTEDGGNGIkLIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGC---- 203
Cdd:cd05079  88 EFLPSGSLKEYLPRNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH--QVKIGDFGLTKAIETdkey 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 -RVK-RVSGTIPYTAPEV---CQAGRADglavdtgvDVWAFGVLIFCVLT 248
Cdd:cd05079 166 yTVKdDLDSPVFWYAPECliqSKFYIAS--------DVWSFGVTLYELLT 207
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
59-252 3.75e-12

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: 65.98  E-value: 3.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKfVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYvFAQEYAPAGDLFD 138
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMK-ELKRFDEQRSFLKEVKLMRRLSH-PNILRFIGVCVKDNKLN-FITEYVNGGTLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIP-PQVGLPedtvkrCVQQLGLALD------FMHGRQLVHRDIKPENVLL--FDREcRRVKLADFGMTRRV-------G 202
Cdd:cd14065  78 LLKsMDEQLP------WSQRVSLAKDiasgmaYLHSKNIIHRDLNSKNCLVreANRG-RNAVVADFGLAREMpdektkkP 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 203 CRVKRVS--GTIPYTAPEVCQagradGLAVDTGVDVWAFGVlIFCVLTGNFP 252
Cdd:cd14065 151 DRKKRLTvvGSPYWMAPEMLR-----GESYDEKVDVFSFGI-VLCEIIGRVP 196
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
48-346 3.81e-12

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: 67.00  E-value: 3.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKL---KNFLREVSITNSLSSSPfIIKVFDVVFETEDCY 124
Cdd:cd07878  12 EVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLihaRRTYRELRLLKHMKHEN-VIGLLDVFTPATSIE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAP----AGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRR 200
Cdd:cd07878  91 NFNEVYLVtnlmGADLNNIVKCQ-KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAV-NEDC-ELRILDFGLARQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCRVKRVSGTIPYTAPEVcqagRADGLAVDTGVDVWAFGVLIFCVLTGN--FP-----------WEAASGADAFFEEFV 267
Cdd:cd07878 168 ADDEMTGYVATRWYRAPEI----MLNWMHYNQTVDIWSVGCIMAELLKGKalFPgndyidqlkriMEVVGTPSPEVLKKI 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 268 RWQRGR-----LPGLPSQ-----WRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHELTSELrRRPSHRARKPPGDRP 337
Cdd:cd07878 244 SSEHARkyiqsLPHMPQQdlkkiFRGANPLAIDLLEKMLVLDSDKRISASEA---LAHPYFSQY-HDPEDEPEAEPYDES 319

                ....*....
gi 66773086 338 PAAGPLRLE 346
Cdd:cd07878 320 PENKERTIE 328
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
56-270 3.93e-12

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: 67.38  E-value: 3.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL---SSSPFIIKVFdVVFETEDCYVFAQEYAP 132
Cdd:cd05625   6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIlaeADNEWVVRLY-YSFQDKDNLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREcRRVKLADFGMTR------------- 199
Cdd:cd05625  85 GGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI-DRD-GHIKLTDFGLCTgfrwthdskyyqs 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 ---------------------RVGCRVKRVS----------------GTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVL 242
Cdd:cd05625 163 gdhlrqdsmdfsnewgdpencRCGDRLKPLErraarqhqrclahslvGTPNYIAPEVLLRTGYTQLC-----DWWSVGVI 237
                       250       260
                ....*....|....*....|....*...
gi 66773086 243 IFCVLTGNFPWEAASGADAFFeEFVRWQ 270
Cdd:cd05625 238 LFEMLVGQPPFLAQTPLETQM-KVINWQ 264
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
55-260 4.37e-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: 66.15  E-value: 4.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGkvdlVVYKGTG---------TKMALKFVNKSKTKLK--NFLREVSITNSLSSSpFIIKVFDVVFETEDC 123
Cdd:cd05061  10 LLRELGQGSFG----MVYEGNArdiikgeaeTRVAVKTVNESASLREriEFLNEASVMKGFTCH-HVVRLLGVVSKGQPT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVfAQEYAPAGDLFDII---------PPqvGLPEDTVKRCVQQLGLALD---FMHGRQLVHRDIKPENVLLFDRECrrVK 191
Cdd:cd05061  85 LV-VMELMAHGDLKSYLrslrpeaenNP--GRPPPTLQEMIQMAAEIADgmaYLNAKKFVHRDLAARNCMVAHDFT--VK 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 192 LADFGMTRRV---GCRVKRVSGTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIfcvltgnfpWEAASGAD 260
Cdd:cd05061 160 IGDFGMTRDIyetDYYRKGGKGLLPvrWMAPESLKDG-----VFTTSSDMWSFGVVL---------WEITSLAE 219
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
53-252 4.79e-12

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: 66.25  E-value: 4.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVdlvvYKG----TGTKMALKFVNKSKTKLKNF--LREVSITNSLSSSPfIIKVFDVVfETEDCYVF 126
Cdd:cd07844   2 YKKLDKLGEGSYATV----YKGrsklTGQLVALKEIRLEHEEGAPFtaIREASLLKDLKHAN-IVTLHDII-HTKKTLTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAgDL---FDIIPPqvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGC 203
Cdd:cd07844  76 VFEYLDT-DLkqyMDDCGG--GLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLI--SERGELKLADFGLARAKSV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 204 RVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGN--FP 252
Cdd:cd07844 151 PSKTYSNevvTLWYRPPDVLLGST----EYSTSLDMWGVGCIFYEMATGRplFP 200
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
51-254 4.98e-12

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: 65.67  E-value: 4.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEY 130
Cdd:cd05113   4 KDLTFLKELGTGQFGVVKYGKWRGQ-YDVAIKMIKEGSMSEDEFIEEAKVMMNLSH-EKLVQLYGVCTKQRPIFIIT-EY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDII-PPQVGL-PEDTVKRCvQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV--GCRVK 206
Cdd:cd05113  81 MANGCLLNYLrEMRKRFqTQQLLEMC-KDVCEAMEYLESKQFLHRDLAARNCLVNDQGV--VKVSDFGLSRYVldDEYTS 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 207 RVSGTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWE 254
Cdd:cd05113 158 SVGSKFPvrWSPPEVLMYSK-----FSSKSDVWAFGVLMWEVYSlGKMPYE 203
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
55-260 5.15e-12

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: 65.65  E-value: 5.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYAPAG 134
Cdd:cd05114   8 FMKELGSGLFGVVRLGKWRAQ-YKVAIKAIREGAMSEEDFIEEAKVMMKLTH-PKLVQLYGVCTQQKPIYIVT-EFMENG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV-GCRVKRVSGT- 211
Cdd:cd05114  85 CLLNYLRQRRGkLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGV--VKVSDFGMTRYVlDDQYTSSSGAk 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 212 --IPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAD 260
Cdd:cd05114 163 fpVKWSPPEVFNYSK-----FSSKSDVWSFGVLMWEVFTeGKMPFESKSNYE 209
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
53-252 5.76e-12

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: 65.80  E-value: 5.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKV----DLVVYKGTGTKMalKFVNKSKTKLK--NF----LREVSITNSLSSsPFIIKVFDVVFETED 122
Cdd:cd13990   2 YLLLNLLGKGGFSEVykafDLVEQRYVACKI--HQLNKDWSEEKkqNYikhaLREYEIHKSLDH-PRIVKLYDVFEIDTD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFM--HGRQLVHRDIKPENVLLFDRE-CRRVKLADFGMTR 199
Cdd:cd13990  79 SFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNvSGEIKITDFGLSK 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 200 RVGCRVKRVS---------GTIPYTAPEVCQAGRADGLaVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd13990 159 IMDDESYNSDgmeltsqgaGTYWYLPPECFVVGKTPPK-ISSKVDVWSVGVIFYQMLYGRKP 219
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-250 5.92e-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: 66.57  E-value: 5.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSP-----FIIKVFD-VVFETEDCYVF 126
Cdd:cd14226  15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDtenkyYIVRLKRhFMFRNHLCLVF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQ-EYapagDLFDIIPPQ----VGLpeDTVKRCVQQLGLALDFMHGRQL--VHRDIKPENVLLFDRECRRVKLADFGMTR 199
Cdd:cd14226  95 ELlSY----NLYDLLRNTnfrgVSL--NLTRKFAQQLCTALLFLSTPELsiIHCDLKPENILLCNPKRSAIKIIDFGSSC 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 200 RVGCRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGN 250
Cdd:cd14226 169 QLGQRIYQYIQSRFYRSPEVLL-----GLPYDLAIDMWSLGCILVEMHTGE 214
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-261 6.12e-12

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: 65.51  E-value: 6.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQ----- 128
Cdd:cd05068  11 KLLRKLGSGQFGEVWEGLWNNT-TPVAVKTLKPGTMDPEDFLREAQIMKKLRH-PKLIQLYAVCTLEEPIYIITElmkhg 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 ---EY--APAGDLFdiIPPQVGLpedtvkrcVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTR---- 199
Cdd:cd05068  89 sllEYlqGKGRSLQ--LPQLIDM--------AAQVASGMAYLESQNYIHRDLAARNVLVGENNI--CKVADFGLARvikv 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 200 ------RVGCRVKrvsgtIPYTAPEvcqAGRADGLAVDTgvDVWAFGVLIFCVLT-GNFPWEAASGADA 261
Cdd:cd05068 157 edeyeaREGAKFP-----IKWTAPE---AANYNRFSIKS--DVWSFGILLTEIVTyGRIPYPGMTNAEV 215
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
57-249 6.22e-12

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: 65.98  E-value: 6.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGkvdlVVYKG--TGTKMALK----FVNKSKTKL-KNFLREVSITNSLSSSPfIIKVFDVVFETED-CYVFaq 128
Cdd:cd14158  21 NKLGEGGFG----VVFKGyiNDKNVAVKklaaMVDISTEDLtKQFEQEIQVMAKCQHEN-LVELLGYSCDGPQlCLVY-- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDIIPPQVGLPEDTVK-RCVQQLGLA--LDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVG--- 202
Cdd:cd14158  94 TYMPNGSLLDRLACLNDTPPLSWHmRCKIAQGTAngINYLHENNHIHRDIKSANILL--DETFVPKISDFGLARASEkfs 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66773086 203 --CRVKRVSGTIPYTAPEVCQAgradglAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd14158 172 qtIMTERIVGTTAYMAPEALRG------EITPKSDIFSFGVVLLEIITG 214
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
57-316 6.25e-12

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: 65.33  E-value: 6.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALKFVNKSKT----KLKNFLREVSITNSLSSSpFIIKvFDVVFE-TEDCYVFAqEYA 131
Cdd:cd14189   7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVakphQREKIVNEIELHRDLHHK-HVVK-FSHHFEdAENIYIFL-ELC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvlLFDRECRRVKLADFGMTRRVGC---RVKRV 208
Cdd:cd14189  84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN--FFINENMELKVGDFGLAARLEPpeqRKKTI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEVC-QAGRAdglavdTGVDVWAFGVLIFCVLTGNFPWEAASgadafFEEFVRWQRGRLPGLPSQwrrFTEP 287
Cdd:cd14189 162 CGTPNYLAPEVLlRQGHG------PESDVWSLGCVMYTLLCGNPPFETLD-----LKETYRCIKQVKYTLPAS---LSLP 227
                       250       260
                ....*....|....*....|....*....
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd14189 228 ARHLLAGILKRNPGDRLTLDQI---LEHE 253
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
52-315 8.29e-12

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: 65.44  E-value: 8.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-----KSKTKlKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVF 126
Cdd:cd08229  25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQifdlmDAKAR-ADCIKEIDLLKQLNH-PNVIKYYASFIEDNELNIV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AqEYAPAGDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVllFDRECRRVKLADFGMTRRVG 202
Cdd:cd08229 103 L-ELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANV--FITATGVVKLGDLGLGRFFS 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 203 CRVK---RVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFcvltgnfpwEAASGADAFFEEFV-------RWQRG 272
Cdd:cd08229 180 SKTTaahSLVGTPYYMSPE-----RIHENGYNFKSDIWSLGCLLY---------EMAALQSPFYGDKMnlyslckKIEQC 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 273 RLPGLPSQwrRFTEPALRMFQRLLALEPERRGPAKEVFRFLKH 315
Cdd:cd08229 246 DYPPLPSD--HYSEELRQLVNMCINPDPEKRPDITYVYDVAKR 286
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
53-249 8.44e-12

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: 65.48  E-value: 8.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKFVNKSKTKLKNF--LREVSITNSLSSSPfIIKVFDVVFETED-CYV 125
Cdd:cd07869   7 YEKLEKLGEGSYA----TVYKGkskvNGKLVALKVIRLQEEEGTPFtaIREASLLKGLKHAN-IVLLHDIIHTKETlTLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYAPAGDLFDIIPPqvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDreCRRVKLADFGMTRRVGCRV 205
Cdd:cd07869  82 FEYVHTDLCQYMDKHPG--GLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISD--TGELKLADFGLARAKSVPS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 206 KRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd07869 158 HTYSNevvTLWYRPPDVLLGST----EYSTCLDMWGVGCIFVEMIQG 200
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
47-201 9.46e-12

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: 65.96  E-value: 9.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  47 SDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFE-----T 120
Cdd:cd07854   1 FDLGSRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKkIVLTDPQSVKHALREIKIIRRLDHDN-IVKVYEVLGPsgsdlT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDC---------YVfAQEYAPAgDLFDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRVK 191
Cdd:cd07854  80 EDVgsltelnsvYI-VQEYMET-DLANVLE-QGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFI-NTEDLVLK 155
                       170
                ....*....|
gi 66773086 192 LADFGMTRRV 201
Cdd:cd07854 156 IGDFGLARIV 165
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
52-247 9.56e-12

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: 65.41  E-value: 9.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGKVDLVVYKGTGTKMALKfvnksKTKLKNF--------LREVSITNSLsSSPFIIKVFDVVFETEDc 123
Cdd:cd07866   9 DYEILGKLGEGTFGEVYKARQIKTGRVVALK-----KILMHNEkdgfpitaLREIKILKKL-KHPNVVPLIDMAVERPD- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 yvfaQEYAPAGDLFDIIP------------PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDREcRRVK 191
Cdd:cd07866  82 ----KSKRKRGSVYMVTPymdhdlsgllenPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAAN-ILIDNQ-GILK 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 192 LADFGMTRR-------------------VGCRVKRVsgtipYTAPEVCQAGRADGlavdTGVDVWAFGvlifCVL 247
Cdd:cd07866 156 IADFGLARPydgpppnpkggggggtrkyTNLVVTRW-----YRPPELLLGERRYT----TAVDIWGIG----CVF 217
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
53-308 9.81e-12

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: 65.37  E-value: 9.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKG----TGTKMALKFVNKSKTKLKNF--LREVSITNSLSSSPfIIKVFDVVfETEDCYVF 126
Cdd:cd07870   2 YLNLEKLGEGSYA----TVYKGisriNGQLVALKVISMKTEEGVPFtaIREASLLKGLKHAN-IVLLHDII-HTKETLTF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCRVK 206
Cdd:cd07870  76 VFEYMHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLI--SYLGELKLADFGLARAKSIPSQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSG---TIPYTAPEVCqAGRADglaVDTGVDVWAFGVLIFCVLTGN--FP-----------------------WEAASG 258
Cdd:cd07870 154 TYSSevvTLWYRPPDVL-LGATD---YSSALDIWGAGCIFIEMLQGQpaFPgvsdvfeqlekiwtvlgvptedtWPGVSK 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 259 ADAFFEEFVRWQRGRLpgLPSQWRRFTEP--ALRMFQRLLALEPERRGPAKE 308
Cdd:cd07870 230 LPNYKPEWFLPCKPQQ--LRVVWKRLSRPpkAEDLASQMLMMFPKDRISAQD 279
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
59-196 1.02e-11

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: 62.07  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFL-REVSITNSLSS-SPFIIKVFDVvFETEDCYVFAQEYAPAGDL 136
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLeSEMDILRRLKGlELNIPKVLVT-EDVDGPNILLMELVKGGTL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 FDIIPpQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFG 196
Cdd:cd13968  80 IAYTQ-EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSED--GNVKLIDFG 136
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
54-253 1.24e-11

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: 64.65  E-value: 1.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSItnsLSSSPFIIKVFDVVFETEDCYVFAQEYAPA 133
Cdd:cd14150   3 SMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQV---LRKTRHVNILLFMGFMTRPNFAIITQWCEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDiippQVGLPE---DTVKR--CVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGM----TRRVGCR 204
Cdd:cd14150  80 SSLYR----HLHVTEtrfDTMQLidVARQTAQGMDYLHAKNIIHRDLKSNNIFL--HEGLTVKIGDFGLatvkTRWSGSQ 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 -VKRVSGTIPYTAPEVCQAGRADGLAVDTgvDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14150 154 qVEQPSGSILWMAPEVIRMQDTNPYSFQS--DVYAYGVVLYELMSGTLPY 201
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
53-243 1.53e-11

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: 65.16  E-value: 1.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPF----IIKVFD---------VVFE 119
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENAdefnFVRAYEcfqhknhtcLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 T--EDCYVFAQE--YAPagdlfdiippqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD--RECRRVKLA 193
Cdd:cd14211  81 MleQNLYDFLKQnkFSP-------------LPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDpvRQPYRVKVI 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 194 DFGMTRRVGcrvKRVSGTIP----YTAPEVCQagradGLAVDTGVDVWAFGVLI 243
Cdd:cd14211 148 DFGSASHVS---KAVCSTYLqsryYRAPEIIL-----GLPFCEAIDMWSLGCVI 193
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
58-259 1.57e-11

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: 64.25  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGkvdlVVYKGTGTKMA-------LKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDV---VFETEDCYVFA 127
Cdd:cd14033   8 EIGRGSFK----TVYRGLDTETTvevawceLQTRKLSKGERQRFSEEVEMLKGLQH-PNIVRFYDSwksTVRGHKCIILV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLfDRECRRVKLADFGM-TRRVGCR 204
Cdd:cd14033  83 TELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFI-TGPTGSVKIGDLGLaTLKRASF 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 205 VKRVSGTIPYTAPEVCQAgradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGA 259
Cdd:cd14033 162 AKSVIGTPEFMAPEMYEE------KYDEAVDVYAFGMCILEMATSEYPYSECQNA 210
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
55-291 1.64e-11

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: 64.67  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSItnsLSSSPFIIKVFDVVFETEDCYVFAQEYAPAG 134
Cdd:cd14149  16 LSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAV---LRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDIIPPQvglpeDTVKRCVQQLGLA------LDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGM----TRRVGC- 203
Cdd:cd14149  93 SLYKHLHVQ-----ETKFQMFQLIDIArqtaqgMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLatvkSRWSGSq 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQAGRADGLAVDTgvDVWAFGVLIFCVLTGNFPWEAASGADAFFeeFVRWQRGRLPGLPSQWRR 283
Cdd:cd14149 166 QVEQPTGSILWMAPEVIRMQDNNPFSFQS--DVYSYGIVLYELMTGELPYSHINNRDQII--FMVGRGYASPDLSKLYKN 241

                ....*...
gi 66773086 284 FTEPALRM 291
Cdd:cd14149 242 CPKAMKRL 249
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
53-326 2.14e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 65.91  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086    53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN------KSKTKLK---NFLREVSITNslssspfIIKVFDVVFE--TE 121
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrglkeREKSQLVievNVMRELKHKN-------IVRYIDRFLNkaNQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   122 DCYVFaQEYAPAGDLFDIIPPQVGL----PEDTVKRCVQQLGLALDFMH-------GRQLVHRDIKPENVLLFD--RECR 188
Cdd:PTZ00266   88 KLYIL-MEFCDAGDLSRNIQKCYKMfgkiEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLSTgiRHIG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   189 RV-------------KLADFGMTRRVGCRVKRVS--GTIPYTAPEVCQagrADGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:PTZ00266  167 KItaqannlngrpiaKIGDFGLSKNIGIESMAHScvGTPYYWSPELLL---HETKSYDDKSDMWALGCIIYELCSGKTPF 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66773086   254 EAASGADAFFEEFvrwQRGrlPGLPSqwrrftepalrmfqrllaleperRGPAKEVFRFLKHELTSELRRRPS 326
Cdd:PTZ00266  244 HKANNFSQLISEL---KRG--PDLPI-----------------------KGKSKELNILIKNLLNLSAKERPS 288
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
59-249 2.22e-11

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: 64.19  E-value: 2.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYAPAGDLF 137
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDH-PNVLKFIGVLYKDKRLNLLT-EFIEGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTR------------------ 199
Cdd:cd14222  79 DFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI--KLDKTVVVADFGLSRliveekkkpppdkpttkk 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 200 ---RVGCRVKR--VSGTIPYTAPEVCqagraDGLAVDTGVDVWAFGVlIFCVLTG 249
Cdd:cd14222 157 rtlRKNDRKKRytVVGNPYWMAPEML-----NGKSYDEKVDIFSFGI-VLCEIIG 205
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
48-335 2.42e-11

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: 64.62  E-value: 2.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCY 124
Cdd:cd07851  12 EVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfqSAIHAKRTYRELRLLKHMKH-ENVIGLLDVFTPASSLE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEY--AP--AGDLFDIIPPQVgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRR 200
Cdd:cd07851  91 DFQDVYlvTHlmGADLNNIVKCQK-LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAV-NEDC-ELKILDFGLARH 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCRVKRVSGTIPYTAPEVC-------QAgradglavdtgVDVWAFGVLIFCVLTGN--FPweaasGADAF--------- 262
Cdd:cd07851 168 TDDEMTGYVATRWYRAPEIMlnwmhynQT-----------VDIWSVGCIMAELLTGKtlFP-----GSDHIdqlkrimnl 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 263 ----FEEFVR-----WQRGRLPGLPSQWRR-FTE-------PALRMFQRLLALEPERRGPAKEVfrfLKHELTSELrRRP 325
Cdd:cd07851 232 vgtpDEELLKkisseSARNYIQSLPQMPKKdFKEvfsganpLAIDLLEKMLVLDPDKRITAAEA---LAHPYLAEY-HDP 307
                       330
                ....*....|
gi 66773086 326 SHRARKPPGD 335
Cdd:cd07851 308 EDEPVAPPYD 317
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
49-253 2.50e-11

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: 64.31  E-value: 2.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKV--DLVVYKGTGTKMALKFVNKS--KTKLKNF----LREVSITNSLSSsPFIIKVFDVVFET 120
Cdd:cd14040   4 LNERYLLLHLLGRGGFSEVykAFDLYEQRYAAVKIHQLNKSwrDEKKENYhkhaCREYRIHKELDH-PRIVKLYDYFSLD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLFD-RECRRVKLADFGM 197
Cdd:cd14040  83 TDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDgTACGEIKITDFGL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 198 TRRVGCRVKRV---------SGTIPYTAPEVCQAGRaDGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14040 163 SKIMDDDSYGVdgmdltsqgAGTYWYLPPECFVVGK-EPPKISNKVDVWSVGVIFFQCLYGRKPF 226
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
53-329 2.59e-11

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: 64.30  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVN-KSKTKLKN-FLREVSITNSlSSSPFIIKVFDVVFETEDCYVfAQEY 130
Cdd:cd06649   7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHlEIKPAIRNqIIRELQVLHE-CNSPYIVGFYGAFYSDGEISI-CMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDREcrRVKLADFGMT-RRVGCRVKRV 208
Cdd:cd06649  85 MDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRG--EIKLCDFGVSgQLIDSMANSF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 209 SGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPWEA--ASGADAFF----------EEFVRWQRGRLPG 276
Cdd:cd06649 163 VGTRSYMSPE-----RLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPpdAKELEAIFgrpvvdgeegEPHSISPRPRPPG 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 277 LPSQWRRF-TEPALRMFQRL--LALEPERRGPAKEVFRFLKHELTSELRRRPSHRA 329
Cdd:cd06649 238 RPVSGHGMdSRPAMAIFELLdyIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERA 293
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
48-240 2.93e-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: 63.93  E-value: 2.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKhYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKlKNF----LREVSITNSLssspfiiKVFDVVFETEDC 123
Cdd:cd07865  10 EVSK-YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEK-EGFpitaLREIKILQLL-------KHENVVNLIEIC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAQ----------------EYAPAGDLFDiipPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDREc 187
Cdd:cd07865  81 RTKATpynrykgsiylvfefcEHDLAGLLSN---KNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-TKD- 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 188 RRVKLADFGMTR--------RVGCRVKRVSgTIPYTAPEVCQAGRADGlavdTGVDVWAFG 240
Cdd:cd07865 156 GVLKLADFGLARafslaknsQPNRYTNRVV-TLWYRPPELLLGERDYG----PPIDMWGAG 211
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
146-303 2.99e-11

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: 63.67  E-value: 2.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 146 LPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLFDRecRRVKLADFGMTRRVGCRVKR------VSGTIPYTAP 217
Cdd:cd14025  89 LPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAH--YHVKISDFGLAKWNGLSHSHdlsrdgLRGTIAYLPP 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 218 E-VCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWRRFTEPALRMFQRLL 296
Cdd:cd14025 167 ErFKEKNR----CPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRPSLSPIPRQRPSECQQMICLMKRCW 242

                ....*..
gi 66773086 297 ALEPERR 303
Cdd:cd14025 243 DQDPRKR 249
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
54-248 4.47e-11

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: 63.21  E-value: 4.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKM------ALKFV--NKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYV 125
Cdd:cd05053  15 TLGKPLGEGAFGQVVKAEAVGLDNKPnevvtvAVKMLkdDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAqEYAPAGDLFDII----PPQVGL-------PEDTVK-----RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrr 189
Cdd:cd05053  95 VV-EYASKGNLREFLrarrPPGEEAspddprvPEEQLTqkdlvSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV-- 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 190 VKLADFGMTRRVGCR---VKRVSGTIPY--TAPEvcqagradglAVDTGV-----DVWAFGVLIFCVLT 248
Cdd:cd05053 172 MKIADFGLARDIHHIdyyRKTTNGRLPVkwMAPE----------ALFDRVythqsDVWSFGVLLWEIFT 230
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
53-240 5.21e-11

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: 63.42  E-value: 5.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL------SSSPFIIKVFD-VVFETEDCYV 125
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLntkydpEDKHHIVRLLDhFMHHGHLCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 F---AQeyapagDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFG---M 197
Cdd:cd14212  81 FellGV------NLYELLKQNqfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFGsacF 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 198 TRRVgcrvkrVSGTIP---YTAPEVcqagrADGLAVDTGVDVWAFG 240
Cdd:cd14212 155 ENYT------LYTYIQsrfYRSPEV-----LLGLPYSTAIDMWSLG 189
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
59-257 5.54e-11

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: 62.92  E-value: 5.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGkvdlVVYKGT--GTKMALKFVnKSKTKL------KNFLREVSITNSLSSsPFIIKVFDVVFETED-CYVFAqe 129
Cdd:cd14159   1 IGEGGFG----CVYQAVmrNTEYAVKRL-KEDSELdwsvvkNSFLTEVEKLSRFRH-PNIVDLAGYSAQQGNyCLIYV-- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQL---GLALDFMHGRQ--LVHRDIKPENVLLFDRecRRVKLADFGMTR----- 199
Cdd:cd14159  73 YLPNGSLEDRLHCQVSCPCLSWSQRLHVLlgtARAIQYLHSDSpsLIHGDVKSSNILLDAA--LNPKLGDFGLARfsrrp 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 200 ------RVGCRVKRVSGTIPYTAPEVCQAGRadgLAVDTgvDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd14159 151 kqpgmsSTLARTQTVRGTLAYLPEEYVKTGT---LSVEI--DVYSFGVVLLELLTGRRAMEVDS 209
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
59-259 5.73e-11

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: 62.41  E-value: 5.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKG--TGTKMALKFVNKSKTK-LKNFLREVSITNSLSSsPFIIKVFDVVFETED-CYVFaqEYAPAG 134
Cdd:cd14061   2 IGVGGFGKVYRGIWRGeeVAVKAARQDPDEDISVtLENVRQEARLFWMLRH-PNIIALRGVCLQPPNlCLVM--EYARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLF-----DIIPPQVglpedTVKRCVQqLGLALDFMHGRQ---LVHRDIKPENVLLF------DRECRRVKLADFGMTRR 200
Cdd:cd14061  79 ALNrvlagRKIPPHV-----LVDWAIQ-IARGMNYLHNEApvpIIHRDLKSSNILILeaieneDLENKTLKITDFGLARE 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 201 VGcRVKRVS--GTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAASGA 259
Cdd:cd14061 153 WH-KTTRMSaaGTYAWMAPEVIKSST-----FSKASDVWSYGVLLWELLTGEVPYKGIDGL 207
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
59-253 7.62e-11

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: 62.31  E-value: 7.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT--GTKMALKFVNKSKTK-----LKNFLREVSITNSLSSsPFIIKVFDVVFETED-CYVFaqEY 130
Cdd:cd14148   2 IGVGGFGKV----YKGLwrGEEVAVKAARQDPDEdiavtAENVRQEARLFWMLQH-PNIIALRGVCLNPPHlCLVM--EY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDI-----IPPQVglpedTVKRCVQqLGLALDFMHGRQLV---HRDIKPENVLLFDRECRR------VKLADFG 196
Cdd:cd14148  75 ARGGALNRAlagkkVPPHV-----LVNWAVQ-IARGMNYLHNEAIVpiiHRDLKSSNILILEPIENDdlsgktLKITDFG 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 197 MTRRVGCRVK-RVSGTIPYTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14148 149 LAREWHKTTKmSAAGTYAWMAPEVIRLS-----LFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
156-264 7.99e-11

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: 62.39  E-value: 7.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 156 QQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGM----TRRVGC-RVKRVSGTIPYTAPEVCQAGRADGLAV 230
Cdd:cd14151 111 RQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLatvkSRWSGShQFEQLSGSILWMAPEVIRMQDKNPYSF 188
                        90       100       110
                ....*....|....*....|....*....|....
gi 66773086 231 DTgvDVWAFGVLIFCVLTGNFPWEAASGADAFFE 264
Cdd:cd14151 189 QS--DVYAFGIVLYELMTGQLPYSNINNRDQIIF 220
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
53-274 8.59e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 62.97  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN-FLREVSitnslssSPFIIKVFDVVFETE-DCYVFAQEY 130
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGTTLIEAmLLQNVN-------HPSVIRMKDTLVSGAiTCMVLPHYS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  131 ApagDLFDIIPPQVG-LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRrvgCRVKR-- 207
Cdd:PHA03209 141 S---DLYTYLTKRSRpLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVD--QVCIGDLGAAQ---FPVVApa 212
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  208 ---VSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTgnFPWEAASGADAFFEEFVRWQRGRL 274
Cdd:PHA03209 213 flgLAGTVETNAPEVLARDK-----YNSKADIWSAGIVLFEMLA--YPSTIFEDPPSTPEEYVKSCHSHL 275
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
53-315 9.67e-11

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: 61.56  E-value: 9.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALK---FVNKSKTKLKNFLREVSITNSLSSSPFIIKvFDVVFE--------TE 121
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKrsrSRFRGEKDRKRKLEEVERHEKLGEHPNCVR-FIKAWEekgilyiqTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 DCYVFAQEYAPAGDlfdiippqvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECrrvKLADFGMTRR 200
Cdd:cd14050  82 LCDTSLQQYCEETH---------SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLsKDGVC---KLGDFGLVVE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGcRVKRVS---GTIPYTAPEVCQaGRadglaVDTGVDVWAFGVLIFCVLTgNFpwEAASGADAffeefvrWQRGRLPGL 277
Cdd:cd14050 150 LD-KEDIHDaqeGDPRYMAPELLQ-GS-----FTKAADIFSLGITILELAC-NL--ELPSGGDG-------WHQLRQGYL 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 66773086 278 PSqwrRFTEPALRMFQRLLAL----EPERRGPAKEVfrfLKH 315
Cdd:cd14050 213 PE---EFTAGLSPELRSIIKLmmdpDPERRPTAEDL---LAL 248
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
42-290 9.95e-11

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: 62.05  E-value: 9.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  42 RTLAASDVTKHYELVRELGKGTYGkvdlVVYKGTGTKM-------ALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVF 114
Cdd:cd14031   1 KAVATSPGGRFLKFDIELGRGAFK----TVYKGLDTETwvevawcELQDRKLTKAEQQRFKEEAEMLKGLQH-PNIVRFY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 115 DV---VFETEDCYVFAQEYAPAGDL------FDIIPPQVglpedtVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLf 183
Cdd:cd14031  76 DSwesVLKGKKCIVLVTELMTSGTLktylkrFKVMKPKV------LRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 184 DRECRRVKLADFGMTRRVGCR-VKRVSGTIPYTAPEVCQAgradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAF 262
Cdd:cd14031 149 TGPTGSVKIGDLGLATLMRTSfAKSVIGTPEFMAPEMYEE------HYDESVDVYAFGMCMLEMATSEYPYSECQNAAQI 222
                       250       260
                ....*....|....*....|....*...
gi 66773086 263 FEEFVRWQRgrlpglPSQWRRFTEPALR 290
Cdd:cd14031 223 YRKVTSGIK------PASFNKVTDPEVK 244
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
55-253 1.04e-10

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: 62.29  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVdlvvYKGTGTKM---------ALKFV--NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDC 123
Cdd:cd05045   4 LGKTLGEGEFGKV----VKATAFRLkgragyttvAVKMLkeNASSSELRDLLSEFNLLKQVNH-PHVIKLYGACSQDGPL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAqEYAPAGDLFDII-------PPQVGLPED--------------TVKRCVQ---QLGLALDFMHGRQLVHRDIKPEN 179
Cdd:cd05045  79 LLIV-EYAKYGSLRSFLresrkvgPSYLGSDGNrnssyldnpderalTMGDLISfawQISRGMQYLAEMKLVHRDLAARN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 180 VLLfdRECRRVKLADFGMTRRV---GCRVKRVSGTIP--YTAPEvcqaGRADGLAVdTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05045 158 VLV--AEGRKMKISDFGLSRDVyeeDSYVKRSKGRIPvkWMAIE----SLFDHIYT-TQSDVWSFGVLLWEIVTlGGNPY 230
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
59-253 1.23e-10

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: 61.82  E-value: 1.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK--LKNFLREVSITNSlSSSPFIIKVFDVVFeTEDCYVFAQEYAPAGDL 136
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDITVelQKQIMSELEILYK-CDSPYIIGFYGAFF-VENRISICTEFMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 137 fDIIPPqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRR-VGCRVKRVSGTIPYT 215
Cdd:cd06619  87 -DVYRK---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRG--QVKLCDFGVSTQlVNSIAKTYVGTNAYM 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 66773086 216 APEvcqagRADGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd06619 161 APE-----RISGEQYGIHSDVWSLGISFMELALGRFPY 193
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
156-260 1.35e-10

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: 61.26  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 156 QQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGM----TRRVGCR-VKRVSGTIPYTAPEVCQAgrADGLAV 230
Cdd:cd14062  96 RQTAQGMDYLHAKNIIHRDLKSNNIFL--HEDLTVKIGDFGLatvkTRWSGSQqFEQPTGSILWMAPEVIRM--QDENPY 171
                        90       100       110
                ....*....|....*....|....*....|
gi 66773086 231 DTGVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd14062 172 SFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
59-329 1.35e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 61.34  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTG------TKMALKFVNKS-KTKLKNFLREVSiTNSLSSSPFIIKVFDVVFETEdcYVFAQEYA 131
Cdd:cd05037   7 LGQGTFTNIYDGILREVGdgrvqeVEVLLKVLDSDhRDISESFFETAS-LMSQISHKHLVKLYGVCVADE--NIMVQEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDIIPPQVGLPEDTVK-RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRR----VKLADFGMTRRVGCRVK 206
Cdd:cd05037  84 RYGPLDKYLRRMGNNVPLSWKlQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLDGyppfIKLSDPGVPITVLSREE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 207 RVSgTIPYTAPEVCQAGRADglaVDTGVDVWAFGVLIfcvltgnfpWEAASGADAFFEEFVrwqrgrlpglPSQWRRFTE 286
Cdd:cd05037 164 RVD-RIPWIAPECLRNLQAN---LTIAADKWSFGTTL---------WEICSGGEEPLSALS----------SQEKLQFYE 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 287 PAlrmfQRLLALEperrgpAKEVFRFLKHELTSELRRRPSHRA 329
Cdd:cd05037 221 DQ----HQLPAPD------CAELAELIMQCWTYEPTKRPSFRA 253
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
55-253 1.43e-10

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 61.71  E-value: 1.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKV---DLVVYKGTGTKM-----ALKFVNKSKTKlKNFLREVSITNSLSSSPfIIKVFDVVFETEDCY-V 125
Cdd:cd05049   9 LKRELGEGAFGKVflgECYNLEPEQDKMlvavkTLKDASSPDAR-KDFEREAELLTNLQHEN-IVKFYGVCTEGDPLLmV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FaqEYAPAGDL----------------FDIIPPQVGLPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrr 189
Cdd:cd05049  87 F--EYMEHGDLnkflrshgpdaaflasEDSAPGELTLSQ--LLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV-- 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 190 VKLADFGMTRRV-GCRVKRVSGT----IPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05049 161 VKIGDFGMSRDIySTDYYRVGGHtmlpIRWMPPESILYRK-----FTTESDVWSFGVVLWEIFTyGKQPW 225
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
48-249 1.59e-10

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: 62.23  E-value: 1.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPfIIKVFDVVFETEDCY 124
Cdd:cd07879  12 ELPERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRpfqSEIFAKRAYRELTLLKHMQHEN-VIGLLDVFTSAVSGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLP--EDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFGMTRRVG 202
Cdd:cd07879  91 EFQDFYLVMPYMQTDLQKIMGHPlsEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN-LAVNEDC-ELKILDFGLARHAD 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 203 CRVKRVSGTIPYTAPEVCqagrADGLAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd07879 169 AEMTGYVVTRWYRAPEVI----LNWMHYNQTVDIWSVGCIMAEMLTG 211
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
61-316 2.08e-10

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: 60.79  E-value: 2.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  61 KGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKnflrEVSITNSLSSSPfIIKVFDVVFETEDCYVFaQEYAPAGDLFDII 140
Cdd:cd13995  14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS----DVEIQACFRHEN-IAELYGALLWEETVHLF-MEAGEGGSVLEKL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 141 PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDrecRRVKLADFGMTRRVGCRV---KRVSGTIPYTAP 217
Cdd:cd13995  88 ESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS---TKAVLVDFGLSVQMTEDVyvpKDLRGTEIYMSP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 218 EV--CQAGradglavDTGVDVWAFGVLIFCVLTGNFPWEAASGADAF--FEEFVRWQRGRLPGLPSQwrrfTEPALR-MF 292
Cdd:cd13995 165 EVilCRGH-------NTKADIYSLGATIIHMQTGSPPWVRRYPRSAYpsYLYIIHKQAPPLEDIAQD----CSPAMReLL 233
                       250       260
                ....*....|....*....|....
gi 66773086 293 QRLLALEPERRGPAKEVfrfLKHE 316
Cdd:cd13995 234 EAALERNPNHRSSAAEL---LKHE 254
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
56-241 2.59e-10

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: 61.21  E-value: 2.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSSPFIikvfdvvfETEDCYV------ 125
Cdd:cd06633  26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSysgkQTNEKWQDIIKEVKFLQQLKHPNTI--------EYKGCYLkdhtaw 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEY--APAGDLFDIipPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGmTRRVGC 203
Cdd:cd06633  98 LVMEYclGSASDLLEV--HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILL--TEPGQVKLADFG-SASIAS 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 66773086 204 RVKRVSGTIPYTAPEVCqagradgLAVDTG-----VDVWAFGV 241
Cdd:cd06633 173 PANSFVGTPYWMAPEVI-------LAMDEGqydgkVDIWSLGI 208
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
58-319 3.77e-10

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: 60.47  E-value: 3.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFEtEDCYVfAQEYAPAGDLF 137
Cdd:cd05069  19 KLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDK-LVPLYAVVSE-EPIYI-VTEFMGKGSLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DIIPPQVG----LPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV--GCRVKRVSGT 211
Cdd:cd05069  95 DFLKEGDGkylkLPQ--LVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLV--CKIADFGLARLIedNEYTARQGAK 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAfFEEFVRWQRGRLP-GLPsqwrrftEP 287
Cdd:cd05069 171 FPikWTAPEAALYGR-----FTIKSDVWSFGILLTELVTkGRVPYPGMVNREV-LEQVERGYRMPCPqGCP-------ES 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 288 ALRMFQRLLALEPERRGPAKEVFRFLKHELTS 319
Cdd:cd05069 238 LHELMKLCWKKDPDERPTFEYIQSFLEDYFTA 269
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
54-257 4.72e-10

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: 60.91  E-value: 4.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTKMALK---FVNKSKTKLKNFLREVSI------TNSLSS----SPFIIKVFdvvfet 120
Cdd:cd07853   3 EPDRPIGYGAFGVVWSVTDPRDGKRVALKkmpNVFQNLVSCKRVFRELKMlcffkhDNVLSAldilQPPHIDPF------ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFAQEYApaGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECrRVKLADFGMTR- 199
Cdd:cd07853  77 EEIYVVTELMQ--SDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGN-LLVNSNC-VLKICDFGLARv 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 200 ---RVGCRVKRVSGTIPYTAPEVCQAGRADGLAvdtgVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd07853 153 eepDESKHMTQEVVTQYYRAPEILMGSRHYTSA----VDIWSVGCIFAELLGRRILFQAQS 209
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
45-252 4.73e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 61.01  E-value: 4.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   45 AASDVTKHYELVRELGKGTYGKVDLVVYKGTGTKMalKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCY 124
Cdd:PHA03207  86 PASVVRMQYNILSSLTPGSEGEVFVCTKHGDEQRK--KVIVKAVTGGKTPGREIDILKTISHRAIINLIHAYRWKSTVCM 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  125 VFaQEYApaGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCR 204
Cdd:PHA03207 164 VM-PKYK--CDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPE--NAVLGDFGAACKLDAH 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086  205 VKRV-----SGTIPYTAPEVcqagradgLAVD---TGVDVWAFGVLIFCVLTGNFP 252
Cdd:PHA03207 239 PDTPqcygwSGTLETNSPEL--------LALDpycAKTDIWSAGLVLFEMSVKNVT 286
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-254 5.19e-10

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: 60.49  E-value: 5.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL-----SSSPFIIKVFD-VVFETEDCYVF 126
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILDALrrkdrDNSHNVIHMKEyFYFRNHLCITF 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 aqEYAPAgDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTrrvgCR 204
Cdd:cd14225 125 --ELLGM-NLYELIKKNnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKVIDFGSS----CY 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 205 V-KRVSGTIP---YTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGN--FPWE 254
Cdd:cd14225 198 EhQRVYTYIQsrfYRSPEVIL-----GLPYSMAIDMWSLGCILAELYTGYplFPGE 248
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
58-319 5.75e-10

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: 59.70  E-value: 5.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFEtEDCYVfAQEYAPAGDLF 137
Cdd:cd05071  16 KLGQGCFGEVWMGTWNGT-TRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEK-LVQLYAVVSE-EPIYI-VTEYMSKGSLL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 138 DIIPPQVG----LPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV--GCRVKRVSGT 211
Cdd:cd05071  92 DFLKGEMGkylrLPQ--LVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLV--CKVADFGLARLIedNEYTARQGAK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 212 IP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAdaffEEFVRWQRG-RLPGLPSQWRRFTEP 287
Cdd:cd05071 168 FPikWTAPEAALYGR-----FTIKSDVWSFGILLTELTTkGRVPYPGMVNR----EVLDQVERGyRMPCPPECPESLHDL 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 66773086 288 ALRMFQRllalEPERRGPAKEVFRFLKHELTS 319
Cdd:cd05071 239 MCQCWRK----EPEERPTFEYLQAFLEDYFTS 266
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
56-257 5.76e-10

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: 59.93  E-value: 5.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSSpFIIKVFDVVFETEdCYVFAQEYA 131
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKldspVGDSERNCLLKEAEILHKARFS-YILPILGICNEPE-FLGIVTEYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDLFDI-----IPPQVGLPEDTvkRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLfDREcRRVKLADFGMTR-RV-- 201
Cdd:cd14026  80 TNGSLNELlhekdIYPDVAWPLRL--RILYEIALGVNYLHNMSppLLHHDLKTQNILL-DGE-FHVKIADFGLSKwRQls 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 202 -----GCRVKRVSGTIPYTAPEVCQAGRADGLAVDTgvDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:cd14026 156 isqsrSSKSAPEGGTIIYMPPEEYEPSQKRRASVKH--DIYSYAIIMWEVLSRKIPFEEVT 214
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
53-254 6.35e-10

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: 60.53  E-value: 6.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSL-----SSSPFIIKVFD-VVFETEDCYVF 126
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLkkqdkDNTMNVIHMLEsFTFRNHICMTF 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AqeyAPAGDLFDIIPPQ--VGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLADFGMTrrvgC- 203
Cdd:cd14224 147 E---LLSMNLYELIKKNkfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSS----Cy 219
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 204 RVKRVSGTIP---YTAPEVCQAGRAdGLAvdtgVDVWAFGVLIFCVLTGN--FPWE 254
Cdd:cd14224 220 EHQRIYTYIQsrfYRAPEVILGARY-GMP----IDMWSFGCILAELLTGYplFPGE 270
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
54-253 6.57e-10

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: 59.70  E-value: 6.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTgTKMALKFVNKSKTKLKNFLREVSITNSLSSSPfIIKVFDVVFEtEDCYVfAQEYAPA 133
Cdd:cd05070  12 QLIKRLGNGQFGEVWMGTWNGN-TKVAIKTLKPGTMSPESFLEEAQIMKKLKHDK-LVQLYAVVSE-EPIYI-VTEYMSK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV--GCRVKRVS 209
Cdd:cd05070  88 GSLLDFLKDGEGraLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLI--CKIADFGLARLIedNEYTARQG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 210 GTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05070 166 AKFPikWTAPEAALYGR-----FTIKSDVWSFGILLTELVTkGRVPY 207
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
51-253 7.01e-10

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: 59.71  E-value: 7.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKG-TGTKMALKFVNK------SKTKLKNFLREVSITnSLSSSPFIIKVFDVVFETEDC 123
Cdd:cd05036   6 KNLTLIRALGQGAFGEVYEGTVSGmPGDPSPLQVAVKtlpelcSEQDEMDFLMEALIM-SKFNHPNIVRCIGVCFQRLPR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAqEYAPAGDLFDI---IPPQVGLPEDTVKR----CVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRV-KLADF 195
Cdd:cd05036  85 FILL-ELMAGGDLKSFlreNRPRPEQPSSLTMLdllqLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVaKIGDF 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 196 GMTRRVgcrvkrvsgtipYTAPEVCQAGRA-------------DGLaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05036 164 GMARDI------------YRADYYRKGGKAmlpvkwmppeaflDGI-FTSKTDVWSFGVLLWEIFSlGYMPY 222
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
53-253 7.68e-10

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: 59.69  E-value: 7.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKV----DLVVYKGTGTKMALKFVNKSKTKLKNF----LREVSITNSLSSsPFIIKVFDVVFETEDCY 124
Cdd:cd14041   8 YLLLHLLGRGGFSEVykafDLTEQRYVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKELDH-PRIVKLYDYFSLDTDSF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLFD-RECRRVKLADFGMTRRV 201
Cdd:cd14041  87 CTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNgTACGEIKITDFGLSKIM 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 202 ---------GCRV-KRVSGTIPYTAPEVCQAGRaDGLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14041 167 dddsynsvdGMELtSQGAGTYWYLPPECFVVGK-EPPKISNKVDVWSVGVIFYQCLYGRKPF 227
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
53-252 7.73e-10

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: 59.93  E-value: 7.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKM-ALKFVNKSKTKLKNFLREVSITNSLSSSP-----FIIKVFDVvFETED--CY 124
Cdd:cd14135   2 YRVYGYLGKGVFSNVVRARDLARGNQEvAIKIIRNNELMHKAGLKELEILKKLNDADpddkkHCIRLLRH-FEHKNhlCL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFAqeyAPAGDLFDIIPP---QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRV-KLADFGMTRR 200
Cdd:cd14135  81 VFE---SLSMNLREVLKKygkNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILV--NEKKNTlKLCDFGSASD 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 201 VGCR------VKRVsgtipYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGN--FP 252
Cdd:cd14135 156 IGENeitpylVSRF-----YRAPEIIL-----GLPYDYPIDMWSVGCTLYELYTGKilFP 205
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
58-257 8.55e-10

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: 59.21  E-value: 8.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVY--KGTGTKMALKFV--NKSKTKLKN-FLREVSITNSLSSsPFIIKVFDVVfETEDcYVFAQEYAP 132
Cdd:cd05116   2 ELGSGNFGTVKKGYYqmKKVVKTVAVKILknEANDPALKDeLLREANVMQQLDN-PYIVRMIGIC-EAES-WMLVMEMAE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRVK----RV 208
Cdd:cd05116  79 LGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH--YAKISDFGLSKALRADENyykaQT 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 209 SGTIP--YTAPEvCqagrADGLAVDTGVDVWAFGVLIfcvltgnfpWEAAS 257
Cdd:cd05116 157 HGKWPvkWYAPE-C----MNYYKFSSKSDVWSFGVLM---------WEAFS 193
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
51-244 9.47e-10

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. 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 serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 59.65  E-value: 9.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKV-DLVVYKGTGTKMALKFVnKSKTKLKNFLR-EVSITNSLS-----SSPFIIKVFDVV-FETED 122
Cdd:cd14215  12 ERYEIVSTLGEGTFGRVvQCIDHRRGGARVALKII-KNVEKYKEAARlEINVLEKINekdpeNKNLCVQMFDWFdYHGHM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVFAqeyAPAGDLFDIIPPQVGLPE--DTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL--------FDRECRR--- 189
Cdd:cd14215  91 CISFE---LLGLSTFDFLKENNYLPYpiHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltYNLEKKRder 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 190 ------VKLADFGMTRRVGCRVKRVSGTIPYTAPEVCQAgradgLAVDTGVDVWAFGVLIF 244
Cdd:cd14215 168 svkstaIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILE-----LGWSQPCDVWSIGCIIF 223
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
48-241 1.01e-09

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: 59.29  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSSPFIikvfdvvfETEDC 123
Cdd:cd06635  22 DPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSysgkQSNEKWQDIIKEVKFLQRIKHPNSI--------EYKGC 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YV------FAQEY--APAGDLFDIipPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADF 195
Cdd:cd06635  94 YLrehtawLVMEYclGSASDLLEV--HKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILL--TEPGQVKLADF 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 196 GmTRRVGCRVKRVSGTIPYTAPEVCQAgrADGLAVDTGVDVWAFGV 241
Cdd:cd06635 170 G-SASIASPANSFVGTPYWMAPEVILA--MDEGQYDGKVDVWSLGI 212
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
53-280 1.10e-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: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGkvdlVVYKGTgTKMALKFVNKSKTKLKN-------FLREVSITNSLSSSPfIIKVFDVVfETEDCYV 125
Cdd:cd07872   8 YIKLEKLGEGTYA----TVFKGR-SKLTENLVALKEIRLEHeegapctAIREVSLLKDLKHAN-IVTLHDIV-HTDKSLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAQEYAP---------AGDLFDIippqvglpeDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFG 196
Cdd:cd07872  81 LVFEYLDkdlkqymddCGNIMSM---------HNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERG--ELKLADFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 197 MTRRVGCRVKRVSG---TIPYTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFvrwqrgR 273
Cdd:cd07872 150 LARAKSVPTKTYSNevvTLWYRPPDVLLGSS----EYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIF------R 219

                ....*..
gi 66773086 274 LPGLPSQ 280
Cdd:cd07872 220 LLGTPTE 226
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
55-253 1.24e-09

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: 59.26  E-value: 1.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGTG-------TKMALKFVNKSKTK--LKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYV 125
Cdd:cd05098  17 LGKPLGEGCFGQVVLAEAIGLDkdkpnrvTKVAVKMLKSDATEkdLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAqEYAPAGDLFDII----PPQVG-------LPEDTVK-----RCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRR 189
Cdd:cd05098  97 IV-EYASKGNLREYLqarrPPGMEycynpshNPEEQLSskdlvSCAYQVARGMEYLASKKCIHRDLAARNVLV--TEDNV 173
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 190 VKLADFGMTR---RVGCRVKRVSGTIP--YTAPEVCqagrADGLAVDTGvDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05098 174 MKIADFGLARdihHIDYYKKTTNGRLPvkWMAPEAL----FDRIYTHQS-DVWSFGVLLWEIFTlGGSPY 238
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
58-247 1.25e-09

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) 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 DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 59.18  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLV----------------VYKGTGTKMALKFV--NKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFE 119
Cdd:cd05096  12 KLGEGQFGEVHLCevvnpqdlptlqfpfnVRKGRPLLVAVKILrpDANKNARNDFLKEVKILSRLKD-PNIIRLLGVCVD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 120 tEDCYVFAQEYAPAGDL----------------FDIIPPQVGLPEDTVKRCVQ---QLGLALDFMHGRQLVHRDIKPENV 180
Cdd:cd05096  91 -EDPLCMITEYMENGDLnqflsshhlddkeengNDAVPPAHCLPAISYSSLLHvalQIASGMKYLSSLNFVHRDLATRNC 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 181 LLfdRECRRVKLADFGMTRRV-GCRVKRVSG----TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVL 247
Cdd:cd05096 170 LV--GENLTIKIADFGMSRNLyAGDYYRIQGravlPIRWMAWECILMGK-----FTTASDVWAFGVTLWEIL 234
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
55-275 1.32e-09

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 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: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 58.88  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVdlvvYKGT--GTK-------MALKFV-NKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETED-C 123
Cdd:cd05091  10 FMEELGEDRFGKV----YKGHlfGTApgeqtqaVAIKTLkDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPmS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAqeYAPAGDLFDII---PPQ--VGLPED--TVK---------RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRec 187
Cdd:cd05091  86 MIFS--YCSHGDLHEFLvmrSPHsdVGSTDDdkTVKstlepadflHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 188 RRVKLADFGMTRRV-GCRVKRVSGT----IPYTAPEVCQAGRadgLAVDTgvDVWAFGVLIFCVLT-GNFPWEAASGADA 261
Cdd:cd05091 162 LNVKISDLGLFREVyAADYYKLMGNsllpIRWMSPEAIMYGK---FSIDS--DIWSYGVVLWEVFSyGLQPYCGYSNQDV 236
                       250
                ....*....|....
gi 66773086 262 FfeEFVRwQRGRLP 275
Cdd:cd05091 237 I--EMIR-NRQVLP 247
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
55-253 1.43e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 58.90  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLV-VYKGTGTK----MALKFVNK-SKTKLKNFLREVSITNSLSSSpFIIKVFDVVFETeDCYVFAQ 128
Cdd:cd05093   9 LKRELGEGAFGKVFLAeCYNLCPEQdkilVAVKTLKDaSDNARKDFHREAELLTNLQHE-HIVKFYGVCVEG-DPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDII-------------PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADF 195
Cdd:cd05093  87 EYMKHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKIGDF 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086 196 GMTRRV-GCRVKRVSG----TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05093 165 GMSRDVySTDYYRVGGhtmlPIRWMPPESIMYRK-----FTTESDVWSLGVVLWEIFTyGKQPW 223
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
59-262 1.46e-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: 58.86  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKM--ALKFVNK--SKTKLKNFLREVSITNSLSSSPFIIKVFDVVfETEDCYVFAQEYAPAG 134
Cdd:cd05088  15 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEyaSKDDHRDFAGELEVLCKLGHHPNIINLLGAC-EHRGYLYLAIEYAPHG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 135 DLFDII--------PPQVGLPEDTVKRCVQQLGLA--------LDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMT 198
Cdd:cd05088  94 NLLDFLrksrvletDPAFAIANSTASTLSSQQLLHfaadvargMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGLS 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGCRVKRVSGTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADAF 262
Cdd:cd05088 172 RGQEVYVKKTMGRLPvrWMAIESLNYS-----VYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELY 233
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
59-252 1.49e-09

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: 58.26  E-value: 1.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKfVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYAPAGDLFD 138
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALK-MNTLSSNRANMLREVQLMNRLSH-PNILRFMGVCVHQGQLHALT-EYINGGNLEQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADFGMTRRV---GCRVKR--VSGTI 212
Cdd:cd14155  78 LLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkRDENGYTAVVGDFGLAEKIpdySDGKEKlaVVGSP 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 66773086 213 PYTAPEVCQagradGLAVDTGVDVWAFGVlIFCVLTGNFP 252
Cdd:cd14155 158 YWMAPEVLR-----GEPYNEKADVFSYGI-ILCEIIARIQ 191
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
53-255 1.94e-09

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: 58.47  E-value: 1.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTK---LKNFLREVSITNSLSSSPfIIKVFDVVFETEDCY-VFaq 128
Cdd:cd07848   3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENeevKETTLRELKMLRTLKQEN-IVELKEAFRRRGKLYlVF-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAG--DLFDIIPpqVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRVG---- 202
Cdd:cd07848  80 EYVEKNmlELLEEMP--NGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV--LKLCDFGFARNLSegsn 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 203 CRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGN--FPWEA 255
Cdd:cd07848 156 ANYTEYVATRWYRSPELLL-----GAPYGKAVDMWSVGCILGELSDGQplFPGES 205
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
59-252 2.20e-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: 57.91  E-value: 2.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTKMALKfVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYAPAGDLFD 138
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVK-IYKNDVDQHKIVREISLLQKLSH-PNIVRYLGICVKDEKLHPIL-EYVSGGCLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 139 IippqvgLPEDTVKRCVQQLG-LALD------FMHGRQLVHRDIKPENVLLfdRECRRVK---LADFGMTRRVGC----- 203
Cdd:cd14156  78 L------LAREELPLSWREKVeLACDisrgmvYLHSKNIYHRDLNSKNCLI--RVTPRGReavVTDFGLAREVGEmpand 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 66773086 204 --RVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIfCVLTGNFP 252
Cdd:cd14156 150 peRKLSLVGSAFWMAPEMLR-----GEPYDRKVDVFSFGIVL-CEILARIP 194
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
53-260 2.36e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 58.50  E-value: 2.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREV----SITNSLSSSP---FIIKVFDV-----VFET 120
Cdd:cd14216  12 YHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIkllkSVRNSDPNDPnreMVVQLLDDfkisgVNGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVFaqEYAPAGDLFDIIPPQV-GLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDRE--CRR------- 189
Cdd:cd14216  92 HICMVF--EVLGHHLLKWIIKSNYqGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSVNEqyIRRlaaeate 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 190 -------------------VKLADFGMTRRVGCRVKRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGN 250
Cdd:cd14216 170 wqrnflvnplepknaeklkVKIADLGNACWVHKHFTEDIQTRQYRSLEVLI-----GSGYNTPADIWSTACMAFELATGD 244
                       250
                ....*....|
gi 66773086 251 FPWEAASGAD 260
Cdd:cd14216 245 YLFEPHSGED 254
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
59-274 2.54e-09

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: 57.89  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT---GTKMALKFVNKSKTKLKN--FLREVSiTNSLSSSPFIIKVFDVVfETEDCYVFAQEYAPA 133
Cdd:cd14664   1 IGRGGAGTV----YKGVmpnGTLVAVKRLKGEGTQGGDhgFQAEIQ-TLGMIRHRNIVRLRGYC-SNPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDII----PPQVGLPEDTVKRCVQQLGLALDFMHGR---QLVHRDIKPENVLLfDRECRRVkLADFGMTRRV---GC 203
Cdd:cd14664  75 GSLGELLhsrpESQPPLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILL-DEEFEAH-VADFGLAKLMddkDS 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 204 RVKR-VSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFfeEFVRWQRGRL 274
Cdd:cd14664 153 HVMSsVAGSYGYIAPEYAYTGK-----VSEKSDVYSYGVVLLELITGKRPFDEAFLDDGV--DIVDWVRGLL 217
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
51-296 3.13e-09

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) 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 DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 57.70  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFV------------------NKSKTKLKNFLREVSITNSLSSsPFIIK 112
Cdd:cd05095   5 KLLTFKEKLGEGQFGEVHLCEAEGMEKFMDKDFAlevsenqpvlvavkmlraDANKNARNDFLKEIKIMSRLKD-PNIIR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 113 VFDVVFeTEDCYVFAQEYAPAGDLFDII-----PPQVGLPEDT-------VKRCVQQLGLALDFMHGRQLVHRDIKPENV 180
Cdd:cd05095  84 LLAVCI-TDDPLCMITEYMENGDLNQFLsrqqpEGQLALPSNAltvsysdLRFMAAQIASGMKYLSSLNFVHRDLATRNC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 181 LLFDRecRRVKLADFGMTRRV-GCRVKRVSG----TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT--GNFPW 253
Cdd:cd05095 163 LVGKN--YTIKIADFGMSRNLySGDYYRIQGravlPIRWMSWESILLGK-----FTTASDVWAFGVTLWETLTfcREQPY 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 254 EAASGADAFFE--EFVRWQrGRLPGLP--------------SQWRRFTE--PALRMFQRLL 296
Cdd:cd05095 236 SQLSDEQVIENtgEFFRDQ-GRQTYLPqpalcpdsvyklmlSCWRRDTKdrPSFQEIHTLL 295
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
58-248 3.31e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 58.15  E-value: 3.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYK-GTGTK-MALKFVNKSKTKLkNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQEYAPAGD 135
Cdd:cd07868  24 KVGRGTYGHVYKAKRKdGKDDKdYALKQIEGTGISM-SACREIALLRELKH-PNVISLQKVFLSHADRKVWLLFDYAEHD 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDIIP---------PQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR--ECRRVKLADFGMTRRVGCR 204
Cdd:cd07868 102 LWHIIKfhraskankKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgpERGRVKIADMGFARLFNSP 181
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 205 VKRVSGTIP------YTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLT 248
Cdd:cd07868 182 LKPLADLDPvvvtfwYRAPELLLGAR----HYTKAIDIWAIGCIFAELLT 227
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
108-303 3.35e-09

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: 57.72  E-value: 3.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 108 PFIIKVFDVVFETEDCYVFAQE--YAPAGDLF---DIIPPQVG------LPEDTVKRCVQQLGLALDFMHGRQ-LVHRDI 175
Cdd:cd14011  62 PRILTVQHPLEESRESLAFATEpvFASLANVLgerDNMPSPPPelqdykLYDVEIKYGLLQISEALSFLHNDVkLVHGNI 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 176 KPENVLLfdRECRRVKLADFGM-----------TRRVGCRVKRVSGTIP---YTAPEVCQAGRAdglavDTGVDVWAFGV 241
Cdd:cd14011 142 CPESVVI--NSNGEWKLAGFDFcisseqatdqfPYFREYDPNLPPLAQPnlnYLAPEYILSKTC-----DPASDMFSLGV 214
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 242 LIFCVL-TGNFPWEAASG---ADAFFEEFVRWQRGRLPGLPSQWRRFtepaLRMfqrLLALEPERR 303
Cdd:cd14011 215 LIYAIYnKGKPLFDCVNNllsYKKNSNQLRQLSLSLLEKVPEELRDH----VKT---LLNVTPEVR 273
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
156-253 3.41e-09

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: 57.36  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 156 QQLGLALDFMHGRQLVHRDIKPENVLLfdrECRRVKLADFGM--------TRRVGCRVKRVSGTIPYTAPEVCQAGRAD- 226
Cdd:cd14063 104 QQICQGMGYLHAKGIIHKDLKSKNIFL---ENGRVVITDFGLfslsgllqPGRREDTLVIPNGWLCYLAPEIIRALSPDl 180
                        90       100       110
                ....*....|....*....|....*....|.
gi 66773086 227 ----GLAVDTGVDVWAFGVLIFCVLTGNFPW 253
Cdd:cd14063 181 dfeeSLPFTKASDVYAFGTVWYELLAGRWPF 211
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
58-265 3.50e-09

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: 57.39  E-value: 3.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGkvdlVVYKGTGTKMALKFV-----NKSKTKL--KNFLREVSITNSLSSsPFIIKVFDV---VFETEDCYVFA 127
Cdd:cd14032   8 ELGRGSFK----TVYKGLDTETWVEVAwcelqDRKLTKVerQRFKEEAEMLKGLQH-PNIVRFYDFwesCAKGKRCIVLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDL------FDIIPPQVglpedtVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLfDRECRRVKLADFGM-T 198
Cdd:cd14032  83 TELMTSGTLktylkrFKVMKPKV------LRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFI-TGPTGSVKIGDLGLaT 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGCRVKRVSGTIPYTAPEVCQAgradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEE 265
Cdd:cd14032 156 LKRASFAKSVIGTPEFMAPEMYEE------HYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRK 216
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
51-303 6.04e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 57.96  E-value: 6.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   51 KHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPF--IIKVF-DVVFETEDCYVFA 127
Cdd:PTZ00283  32 KKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFfsIVKCHeDFAKKDPRNPENV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  128 Q------EYAPAGDLFDIIPPQV----GLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdreCRR--VKLADF 195
Cdd:PTZ00283 112 LmialvlDYANAGDLRQEIKSRAktnrTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL----CSNglVKLGDF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  196 GMTRRVGCRV-----KRVSGTIPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVrwq 270
Cdd:PTZ00283 188 GFSKMYAATVsddvgRTFCGTPYYVAPEIWRRKPYSKKA-----DMFSLGVLLYELLTLKRPFDGENMEEVMHKTLA--- 259
                        250       260       270
                 ....*....|....*....|....*....|....
gi 66773086  271 rGRLPGLPSQwrrfTEPALR-MFQRLLALEPERR 303
Cdd:PTZ00283 260 -GRYDPLPPS----ISPEMQeIVTALLSSDPKRR 288
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
50-249 6.36e-09

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 57.74  E-value: 6.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   50 TKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKtKLKNflREVSITNSLSSSPfIIKVFDVVFeTEdCYVFAQE 129
Cdd:PTZ00036  65 NKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDP-QYKN--RELLIMKNLNHIN-IIFLKDYYY-TE-CFKKNEK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  130 YAPAGDLFDIIPPQV------------GLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFGM 197
Cdd:PTZ00036 139 NIFLNVVMEFIPQTVhkymkhyarnnhALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQN-LLIDPNTHTLKLCDFGS 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66773086  198 TRRVGCRVKRVSGTIP--YTAPEVcQAGRADglaVDTGVDVWAFGVLIFCVLTG 249
Cdd:PTZ00036 218 AKNLLAGQRSVSYICSrfYRAPEL-MLGATN---YTTHIDLWSLGCIIAEMILG 267
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
151-249 7.58e-09

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 56.48  E-value: 7.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 151 VKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECrrVKLADFGMTRRVGCRVKRVSGTIPYTAPE------VCQAG 223
Cdd:cd14020 112 IQHCARDVLEALAFLHHEGYVHADLKPRNILWsAEDEC--FKLIDFGLSFKEGNQDVKYIQTDGYRAPEaelqncLAQAG 189
                        90       100
                ....*....|....*....|....*.
gi 66773086 224 RADGLAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd14020 190 LQSETECTSAVDLWSLGIVLLEMFSG 215
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
58-248 7.69e-09

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 56.62  E-value: 7.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYK-GTGTK-MALKFVNKSKTKLkNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQEYAPAGD 135
Cdd:cd07867   9 KVGRGTYGHVYKAKRKdGKDEKeYALKQIEGTGISM-SACREIALLRELKH-PNVIALQKVFLSHSDRKVWLLFDYAEHD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 136 LFDII-----------PPQvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDR--ECRRVKLADFGMTRRVG 202
Cdd:cd07867  87 LWHIIkfhraskankkPMQ--LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgpERGRVKIADMGFARLFN 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 66773086 203 CRVKRVSGTIP------YTAPEVCQAGRadglAVDTGVDVWAFGVLIFCVLT 248
Cdd:cd07867 165 SPLKPLADLDPvvvtfwYRAPELLLGAR----HYTKAIDIWAIGCIFAELLT 212
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
55-253 8.61e-09

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: 56.51  E-value: 8.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVdlVVYKGTG---------TKMALKFV--NKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDC 123
Cdd:cd05099  16 LGKPLGEGCFGQV--VRAEAYGidksrpdqtVTVAVKMLkdNATDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YVFAqEYAPAGDLFDII----PPQVGLPEDTVK------------RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREC 187
Cdd:cd05099  94 YVIV-EYAAKGNLREFLrarrPPGPDYTFDITKvpeeqlsfkdlvSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNV 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 188 rrVKLADFGMTRRV---GCRVKRVSGTIP--YTAPEVCqagrADGLAVDTGvDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05099 173 --MKIADFGLARGVhdiDYYKKTSNGRLPvkWMAPEAL----FDRVYTHQS-DVWSFGILMWEIFTlGGSPY 237
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
93-252 9.12e-09

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: 56.13  E-value: 9.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  93 NFLREVSITNSLSSsPFIIKVFDVVFETedcYVFAQEYAPAGDLFDIIPPQ------VGLPEDTVKRCVQQLGLALDFMH 166
Cdd:cd14067  56 EFRQEASMLHSLQH-PCIVYLIGISIHP---LCFALELAPLGSLNTVLEENhkgssfMPLGHMLTFKIAYQIAAGLAYLH 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 167 GRQLVHRDIKPENVLLFD---RECRRVKLADFGMTRRVGCR-VKRVSGTIPYTAPEVcqagrADGLAVDTGVDVWAFGVL 242
Cdd:cd14067 132 KKNIIFCDLKSDNILVWSldvQEHINIKLSDYGISRQSFHEgALGVEGTPGYQAPEI-----RPRIVYDEKVDMFSYGMV 206
                       170
                ....*....|
gi 66773086 243 IFCVLTGNFP 252
Cdd:cd14067 207 LYELLSGQRP 216
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
143-303 9.26e-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: 56.02  E-value: 9.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 143 QVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV--GCRVKRVSGTipYTAPEVc 220
Cdd:cd05576 107 RFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG--HIQLTYFSRWSEVedSCDSDAIENM--YCAPEV- 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 221 qagraDGLAVDT-GVDVWAFGVLIFCVLTGNFPWEA-ASGADAF----FEEFVrwqrgrlpglpsqwrrfTEPALRMFQR 294
Cdd:cd05576 182 -----GGISEETeACDWWSLGALLFELLTGKALVEChPAGINTHttlnIPEWV-----------------SEEARSLLQQ 239

                ....*....
gi 66773086 295 LLALEPERR 303
Cdd:cd05576 240 LLQFNPTER 248
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
1-339 9.66e-09

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: 56.94  E-value: 9.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   1 MSVGCPEPEPPRSLTCCgpgtapgPGAGVPLLTEDmqaltlrtlaasdvtkHYELVRELGKGTYGKVDLVV--YKGTGTK 78
Cdd:COG5752   5 LNPDCLNPQNSDTAKFC-------QKCGFKLLLKE----------------RYRAIKPLGQGGFGRTFLAVdeDIPSHPH 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  79 MALK-FV-----NKSKTK-LKNFLREVSITNSLSSSPFIIKVFDVvFETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTV 151
Cdd:COG5752  62 CVIKqFYfpeqgPSSFQKaVELFRQEAVRLDELGKHPQIPELLAY-FEQDQRLYLVQEFIEGQTLAQELEKKGVFSESQI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 152 KRCVQQLGLALDFMHGRQLVHRDIKPENVLlfdRECRRVK--LADFGMTRRVGCRVKRVSGTI----PYTAPEvcQA-GR 224
Cdd:COG5752 141 WQLLKDLLPVLQFIHSRNVIHRDIKPANII---RRRSDGKlvLIDFGVAKLLTITALLQTGTIigtpEYMAPE--QLrGK 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 225 adglaVDTGVDVWAFGVLIFCVLTGNFPWEAasgADAFFEEFVrWqRGRLPGLPSQWRRFTEPALRMFQRLLalePERRG 304
Cdd:COG5752 216 -----VFPASDLYSLGVTCIYLLTGVSPFDL---FDVSEDRWV-W-RDFLPPGTKVSDRLGQILDKLLQNAL---KQRYQ 282
                       330       340       350
                ....*....|....*....|....*....|....*
gi 66773086 305 PAKEVFRFLKHELTSELRRRPSHRARKPPGDRPPA 339
Cdd:COG5752 283 SATEVLQALKRQPPVSYSPIPVAPTKLPIQAQPPD 317
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
55-248 9.88e-09

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: 56.19  E-value: 9.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGT-----GTKMALKFVNKSKTKLK--NFLREVSITNSLSSSpFIIKVFDVVFETEDCYVFa 127
Cdd:cd05062  10 MSRELGQGSFGMVYEGIAKGVvkdepETRVAIKTVNEAASMREriEFLNEASVMKEFNCH-HVVRLLGVVSQGQPTLVI- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDII---------PPQVGLPedTVKRCVQQLGLALD---FMHGRQLVHRDIKPENVLLfdRECRRVKLADF 195
Cdd:cd05062  88 MELMTRGDLKSYLrslrpemenNPVQAPP--SLKKMIQMAGEIADgmaYLNANKFVHRDLAARNCMV--AEDFTVKIGDF 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 196 GMTRRV---GCRVKRVSGTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT 248
Cdd:cd05062 164 GMTRDIyetDYYRKGGKGLLPvrWMSPESLKDG-----VFTTYSDVWSFGVVLWEIAT 216
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
51-262 1.10e-08

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: 56.08  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  51 KHYELVRELGKGTYGKVDLVVYK---GTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEdcy 124
Cdd:cd05074   9 QQFTLGRMLGKGEFGSVREAQLKsedGSFQKVAVKMLKAdifSSSDIEEFLREAACMKEFDH-PNVIKLIGVSLRSR--- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 vfAQEYAPA----------GDLFD-IIPPQVG-----LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECR 188
Cdd:cd05074  85 --AKGRLPIpmvilpfmkhGDLHTfLLMSRIGeepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCML--NENM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 189 RVKLADFGMTRRV--------GCRVKRvsgTIPYTAPEvcqaGRADGLAVdTGVDVWAFGVLIFCVLT-GNFPWEAASGA 259
Cdd:cd05074 161 TVCVADFGLSKKIysgdyyrqGCASKL---PVKWLALE----SLADNVYT-THSDVWAFGVTMWEIMTrGQTPYAGVENS 232

                ...
gi 66773086 260 DAF 262
Cdd:cd05074 233 EIY 235
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
50-255 1.13e-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: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  50 TKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFeTEDCYVFAQE 129
Cdd:cd14110   2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSH-PRIAQLHSAYL-SPRHLVLIEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFG----MTRRVGCRV 205
Cdd:cd14110  80 LCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMII--TEKNLLKIVDLGnaqpFNQGKVLMT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66773086 206 KRVSGTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEA 255
Cdd:cd14110 158 DKKGDYVETMAPELLE-----GQGAGPQTDIWAIGVTAFIMLSADYPVSS 202
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
53-214 1.25e-08

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 55.59  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKVDLVVYKGTGTKMALKFVNkSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYVFAQEYAP 132
Cdd:cd14128   2 YRLVRKIGSGSFGDIYLGINITNGEEVAVKLES-QKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 A-GDLFDIIPPQVGLpeDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLL-FDRECRRVKLADFGMTRRVgcRVKRVSG 210
Cdd:cd14128  81 SlEDLFNFCSRRFTM--KTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMgIGRHCNKLFLIDFGLAKKY--RDSRTRQ 156

                ....
gi 66773086 211 TIPY 214
Cdd:cd14128 157 HIPY 160
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
55-253 1.53e-08

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: 55.79  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKGT-------GTKMALKFVNKSKTK--LKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYV 125
Cdd:cd05101  28 LGKPLGEGCFGQVVMAEAVGIdkdkpkeAVTVAVKMLKDDATEkdLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAqEYAPAGDLFDII----PPQVGLPEDTVK------------RCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRR 189
Cdd:cd05101 108 IV-EYASKGNLREYLrarrPPGMEYSYDINRvpeeqmtfkdlvSCTYQLARGMEYLASQKCIHRDLAARNVLV--TENNV 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 190 VKLADFGMTRRVG---CRVKRVSGTIP--YTAPEVCqagrADGLAVDTGvDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05101 185 MKIADFGLARDINnidYYKKTTNGRLPvkWMAPEAL----FDRVYTHQS-DVWSFGVLMWEIFTlGGSPY 249
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
165-314 1.58e-08

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 55.49  E-value: 1.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 165 MHGRQLVHRDIKPENVLLfDRECRRVKLADFGMTRRVGCR---VKRVSGTIPYTAPEVCQ----AGRADglavdtgvDVW 237
Cdd:cd13974 148 LHKKNIVHRDLKLGNMVL-NKRTRKITITNFCLGKHLVSEddlLKDQRGSPAYISPDVLSgkpyLGKPS--------DMW 218
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 238 AFGVLIFCVLTGNFPWeaasgADAFFEEFVRWQRGRLPGLPSQwRRFTEPALRMFQRLLALEPERRGPAKEVFRFLK 314
Cdd:cd13974 219 ALGVVLFTMLYGQFPF-----YDSIPQELFRKIKAAEYTIPED-GRVSENTVCLIRKLLVLNPQKRLTASEVLDSLE 289
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
58-261 1.86e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 55.36  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  58 ELGKGTYGKVDLVVYKG---TGTKM-----ALKFVNKSKTKlkNFLREVSITNSLSSSpFIIKVFDVVFETE-------- 121
Cdd:cd05092  12 ELGEGAFGKVFLAECHNllpEQDKMlvavkALKEATESARQ--DFQREAELLTVLQHQ-HIVRFYGVCTEGEplimvfey 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 122 ----DCYVFAQEYAPAGDLFD----IIPPQVGLPEdtVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLA 193
Cdd:cd05092  89 mrhgDLNRFLRSHGPDAKILDggegQAPGQLTLGQ--MLQIASQIASGMVYLASLHFVHRDLATRNCLV--GQGLVVKIG 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 194 DFGMTR--------RVGCRVKRvsgTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGADA 261
Cdd:cd05092 165 DFGMSRdiystdyyRVGGRTML---PIRWMPPESILYRK-----FTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEA 233
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
55-253 1.93e-08

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: 55.80  E-value: 1.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLVVYKG-------TGTKMALKFVNKSKTK--LKNFLREVSITNSLSSSPFIIKVFDVVFETEDCYV 125
Cdd:cd05100  16 LGKPLGEGCFGQVVMAEAIGidkdkpnKPVTVAVKMLKDDATDkdLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 126 FAqEYAPAGDLFDII----PPQVG-------LPEDTVK-----RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrr 189
Cdd:cd05100  96 LV-EYASKGNLREYLrarrPPGMDysfdtckLPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV-- 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 190 VKLADFGMTRRV---GCRVKRVSGTIP--YTAPEVCqagrADGLAVDTGvDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05100 173 MKIADFGLARDVhniDYYKKTTNGRLPvkWMAPEAL----FDRVYTHQS-DVWSFGVLLWEIFTlGGSPY 237
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
59-274 2.02e-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: 55.16  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTG-----TKMALKFVNKSKTK--LKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAqEYA 131
Cdd:cd05046  13 LGRGEFGEVFLAKAKGIEeeggeTLVLVKALQKTKDEnlQSEFRRELDMFRKLSH-KNVVRLLGLCREAEPHYMIL-EYT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 132 PAGDL--FDII----PPQVGLPEDTVKRCVQ---QLGLALDFMHGRQLVHRDIKPENVLLFDRecRRVKLADFGMTRRVG 202
Cdd:cd05046  91 DLGDLkqFLRAtkskDEKLKPPPLSTKQKVAlctQIALGMDHLSNARFVHRDLAARNCLVSSQ--REVKVSLLSLSKDVY 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 203 CR--VKRVSGTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGadaffEEFV-RWQRGRL 274
Cdd:cd05046 169 NSeyYKLRNALIPlrWLAPEAVQEDD-----FSTKSDVWSFGVLMWEVFTqGELPFYGLSD-----EEVLnRLQAGKL 236
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
49-249 2.59e-08

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. 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 serine/threonine residues. The CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 55.40  E-value: 2.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTG-TKMALKFVnKSKTKLKNFLR-EVSITNSLSSSPFIIKVFDVVFEteDCYVF 126
Cdd:cd14214  11 LQERYEIVGDLGEGTFGKVVECLDHARGkSQVALKII-RNVGKYREAARlEINVLKKIKEKDKENKFLCVLMS--DWFNF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 127 AQEYAPAGDL-----FDIIPPQVGLPEDT--VKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRE----------CRR 189
Cdd:cd14214  88 HGHMCIAFELlgkntFEFLKENNFQPYPLphIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtlynesksCEE 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 190 -------VKLADFGMTRRVGCRVKRVSGTIPYTAPEVCQAgradgLAVDTGVDVWAFGVLIFCVLTG 249
Cdd:cd14214 168 ksvkntsIRVADFGSATFDHEHHTTIVATRHYRPPEVILE-----LGWAQPCDVWSLGCILFEYYRG 229
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
59-260 2.64e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 54.57  E-value: 2.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTG-------TKMALKFVNKS-KTKLKNFLREVSITNSLSSSPFIIKvFDVVFETEDcYVFAQEY 130
Cdd:cd05078   7 LGQGTFTKIFKGIRREVGdygqlheTEVLLKVLDKAhRNYSESFFEAASMMSQLSHKHLVLN-YGVCVCGDE-NILVQEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLPEDTVKRCV-QQLGLALDFMHGRQLVHRDIKPENVLLFDRECRR------VKLADFGMTRRVGC 203
Cdd:cd05078  85 VKFGSLDTYLKKNKNCINILWKLEVaKQLAWAMHFLEEKTLVHGNVCAKNILLIREEDRKtgnppfIKLSDPGISITVLP 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 204 RvKRVSGTIPYTAPEVCQAGRADGLAVDTgvdvWAFGVLIfcvltgnfpWEAASGAD 260
Cdd:cd05078 165 K-DILLERIPWVPPECIENPKNLSLATDK----WSFGTTL---------WEICSGGD 207
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
53-247 3.14e-08

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 54.86  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYGKV-DLVVYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSS----SPF----IIKVFD------VV 117
Cdd:cd14213  14 YEIVDTLGEGAFGKVvECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTtdpnSTFrcvqMLEWFDhhghvcIV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 118 FETE--DCYVFAQEYApagdlfdIIPpqvgLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFD----------- 184
Cdd:cd14213  94 FELLglSTYDFIKENS-------FLP----FPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQsdyvvkynpkm 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 185 -RECRR-----VKLADFGMTRRVGCRVKRVSGTIPYTAPEVCQAgradgLAVDTGVDVWAFGvlifCVL 247
Cdd:cd14213 163 kRDERTlknpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-----LGWSQPCDVWSIG----CIL 222
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
57-252 3.97e-08

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: 54.02  E-value: 3.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGkvdlVVYKGT-------GTKMALKFVNK--SKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFA 127
Cdd:cd05058   1 EVIGKGHFG----CVYHGTlidsdgqKIHCAVKSLNRitDIEEVEQFLKEGIIMKDFSH-PNVLSLLGICLPSEGSPLVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVGLPedTVKRCVQ---QLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCR 204
Cdd:cd05058  76 LPYMKHGDLRNFIRSETHNP--TVKDLIGfglQVAKGMEYLASKKFVHRDLAARNCML--DESFTVKVADFGLARDIYDK 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 205 ----VKRVSGT---IPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLTGNFP 252
Cdd:cd05058 152 eyysVHNHTGAklpVKWMALESLQTQK-----FTTKSDVWSFGVLLWELMTRGAP 201
PTZ00284 PTZ00284
protein kinase; Provisional
50-311 5.20e-08

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 54.97  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   50 TKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK-------SKTKLKnFLREVSITNSLSSSPFI-IKVFdvvFETE 121
Cdd:PTZ00284 128 TQRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNvpkytrdAKIEIQ-FMEKVRQADPADRFPLMkIQRY---FQNE 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  122 D---CYVFAQeYAPAgdLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGR-QLVHRDIKPENVLLFDRE----------- 186
Cdd:PTZ00284 204 TghmCIVMPK-YGPC--LLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETSDtvvdpvtnral 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  187 ----CrRVKLADFGmtrrvGCRVKRVS-----GTIPYTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAAS 257
Cdd:PTZ00284 281 ppdpC-RVRICDLG-----GCCDERHSrtaivSTRHYRSPEVVL-----GLGWMYSTDMWSMGCIIYELYTGKLLYDTHD 349
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086  258 GAdaffeEFVRWQRGRLPGLPSQW--RRFTEPALRMFQRLLALEP----------ERRGPAKEVFR 311
Cdd:PTZ00284 350 NL-----EHLHLMEKTLGRLPSEWagRCGTEEARLLYNSAGQLRPctdpkhlariARARPVREVIR 410
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
48-241 5.39e-08

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: 54.26  E-value: 5.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVN----KSKTKLKNFLREVSITNSLSSSPFIikvfdvvfETEDC 123
Cdd:cd06634  12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSysgkQSNEKWQDIIKEVKFLQKLRHPNTI--------EYRGC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YV------FAQEY--APAGDLFDIipPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADF 195
Cdd:cd06634  84 YLrehtawLVMEYclGSASDLLEV--HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILL--TEPGLVKLGDF 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66773086 196 GmTRRVGCRVKRVSGTIPYTAPEVCQAgrADGLAVDTGVDVWAFGV 241
Cdd:cd06634 160 G-SASIMAPANSFVGTPYWMAPEVILA--MDEGQYDGKVDVWSLGI 202
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
57-309 6.15e-08

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: 53.67  E-value: 6.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  57 RELGKGTYGKVDLVVYKGTGTKMALK-FVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVF---ETEDC----YVFAQ 128
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAASigkEESDQgqaeYLLLT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAG--DLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPENVLLFDRecRRVKLADFGMT------ 198
Cdd:cd14036  86 ELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQ--GQIKLCDFGSAtteahy 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 --------RRVGCRVKRVSGTIP-YTAPEVCQAgrADGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVrw 269
Cdd:cd14036 164 pdyswsaqKRSLVEDEITRNTTPmYRTPEMIDL--YSNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYT-- 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 66773086 270 qrgrLPGLPSQWRRFTEpalrMFQRLLALEPERRGPAKEV 309
Cdd:cd14036 240 ----IPPNDTQYTVFHD----LIRSTLKVNPEERLSITEI 271
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
104-310 6.56e-08

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: 53.12  E-value: 6.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 104 LSSSPFIIKVFDVVFETEDCYVFAQEyaPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLF 183
Cdd:cd14022  41 LPAHSNINQITEIILGETKAYVFFER--SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFK 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 184 DRECRRVKLA-----------DFGMTRRVGCRVkrvsgtipYTAPEVCQA-GRADGLAVDtgvdVWAFGVLIFCVLTGNF 251
Cdd:cd14022 119 DEERTRVKLEsledayilrghDDSLSDKHGCPA--------YVSPEILNTsGSYSGKAAD----VWSLGVMLYTMLVGRY 186
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 252 PWEAASGADAffeeFVRWQRGRLpGLPSQwrrFTEPALRMFQRLLALEPERRGPAKEVF 310
Cdd:cd14022 187 PFHDIEPSSL----FSKIRRGQF-NIPET---LSPKAKCLIRSILRREPSERLTSQEIL 237
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
55-253 7.46e-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: 7.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKV---DLVVYKGTGTKMA---LKFVNKSKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQ 128
Cdd:cd05035   3 LGKILGEGEFGSVmeaQLKQDDGSQLKVAvktMKVDIHTYSEIEEFLSEAACMKDFDH-PNVMRLIGVCFTASDLNKPPS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 E-----YAPAGDLFDII------PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGM 197
Cdd:cd05035  82 PmvilpFMKHGDLHSYLlysrlgGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCML--DENMTVCVADFGL 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 198 TRRVGC----RVKRVSGT-IPYTAPEvcqaGRADGLAVDTGvDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05035 160 SRKIYSgdyyRQGRISKMpVKWIALE----SLADNVYTSKS-DVWSFGVTMWEIATrGQTPY 216
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
44-260 7.84e-08

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: 53.14  E-value: 7.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  44 LAASDVTkhyeLVRELGKGTYGKVdlvvYKGTGTKMALKFVNKSKTKLK---------NFLREVSITNSLSSsPFIIKVF 114
Cdd:cd05033   1 IDASYVT----IEKVIGGGEFGEV----CSGSLKLPGKKEIDVAIKTLKsgysdkqrlDFLTEASIMGQFDH-PNVIRLE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 115 DVVFETEDCYVFAqEYAPAGDLFDIippqvgLPEDTVKRCVQQL-----GLA--LDFMHGRQLVHRDIKPENVLLFDREc 187
Cdd:cd05033  72 GVVTKSRPVMIVT-EYMENGSLDKF------LRENDGKFTVTQLvgmlrGIAsgMKYLSEMNYVHRDLAARNILVNSDL- 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 188 rRVKLADFGMTRRVGCR---VKRVSGTIP--YTAPEVCQAGradglAVDTGVDVWAFGVLIFCVLT-GNFPWEAASGAD 260
Cdd:cd05033 144 -VCKVSDFGLSRRLEDSeatYTTKGGKIPirWTAPEAIAYR-----KFTSASDVWSFGIVMWEVMSyGERPYWDMSNQD 216
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
32-259 8.31e-08

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: 53.52  E-value: 8.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  32 LTEDMQALTLRTLAASDVTKHYELVRELGKGTYGkvdlVVYKGTGTKMALKFV-------NKSKTKLKNFLREVSITNSL 104
Cdd:cd14030   6 QQDEIEELETKAVG*SPDGRFLKFDIEIGRGSFK----TVYKGLDTETTVEVAwcelqdrKLSKSERQRFKEEAGMLKGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 105 SSsPFIIKVFDV---VFETEDCYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQ--LVHRDIKPEN 179
Cdd:cd14030  82 QH-PNIVRFYDSwesTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 180 VLLfDRECRRVKLADFGM-TRRVGCRVKRVSGTIPYTAPEVCQAgradglAVDTGVDVWAFGVLIFCVLTGNFPWEAASG 258
Cdd:cd14030 161 IFI-TGPTGSVKIGDLGLaTLKRASFAKSVIGTPEFMAPEMYEE------KYDESVDVYAFGMCMLEMATSEYPYSECQN 233

                .
gi 66773086 259 A 259
Cdd:cd14030 234 A 234
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
54-260 8.68e-08

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: 53.19  E-value: 8.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKVDLVVYKGTGTK----MALKFVNKSKTKLKN--FLREVSITNSLSSsPFIIKVFDVVFETEDCYVfa 127
Cdd:cd05057  10 EKGKVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLREETGPKANeeILDEAYVMASVDH-PHLVRLLGICLSSQVQLI-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDII-PPQVGL-PEDTVKRCVQqLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRVGCRV 205
Cdd:cd05057  87 TQLMPLGCLLDYVrNHRDNIgSQLLLNWCVQ-IAKGMSYLEEKRLVHRDLAARNVLVKTPN--HVKITDFGLAKLLDVDE 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66773086 206 KRVSGT-----IPYTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLT-GNFPWEAASGAD 260
Cdd:cd05057 164 KEYHAEggkvpIKWMALESIQYRIYTHKS-----DVWSYGVTVWELMTfGAKPYEGIPAVE 219
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
53-309 1.25e-07

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: 52.95  E-value: 1.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  53 YELVRELGKGTYG-------KVDLVVYkgTGTKMALKFVNKSKTKLknfLREVSITNSLSSsPFIIKVFDVVFET----- 120
Cdd:cd14048   8 FEPIQCLGRGGFGvvfeaknKVDDCNY--AVKRIRLPNNELAREKV---LREVRALAKLDH-PGIVRYFNAWLERppegw 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 ----EDCYVFAQ-EYAPAGDLFDIIPPQVGL---PEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVlLFDREcRRVKL 192
Cdd:cd14048  82 qekmDEVYLYIQmQLCRKENLKDWMNRRCTMesrELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNV-FFSLD-DVVKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 193 ADFGMTRRVGC----------------RVKRVsGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLIFCVLtgnFPWEAA 256
Cdd:cd14048 160 GDFGLVTAMDQgepeqtvltpmpayakHTGQV-GTRLYMSPE-----QIHGNQYSEKVDIFALGLILFELI---YSFSTQ 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 66773086 257 SGADAFFEEFvrwQRGRLPGLPSQwrrfTEPALRMF-QRLLALEPERRGPAKEV 309
Cdd:cd14048 231 MERIRTLTDV---RKLKFPALFTN----KYPEERDMvQQMLSPSPSERPEAHEV 277
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
48-340 1.41e-07

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: 52.96  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  48 DVTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNKS-KTKL--KNFLREVSITNSLSSSPfIIKVFDVVFE-TEDC 123
Cdd:cd07856   7 EITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPfSTPVlaKRTYRELKLLKHLRHEN-IISLSDIFISpLEDI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 124 YvFAQEYApAGDLFDIIPPQvGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRRVGC 203
Cdd:cd07856  86 Y-FVTELL-GTDLHRLLTSR-PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILV-NENC-DLKICDFGLARIQDP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 204 RVKRVSGTIPYTAPEVCQAGRadglAVDTGVDVWAFGVLI------------------FCVLT---GNFPWEAASGADAf 262
Cdd:cd07856 161 QMTGYVSTRYYRAPEIMLTWQ----KYDVEVDIWSAGCIFaemlegkplfpgkdhvnqFSIITellGTPPDDVINTICS- 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 263 fEEFVRW-----QRGRLPgLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVfrfLKHELTSelrrrPSHrarkPPGDRP 337
Cdd:cd07856 236 -ENTLRFvqslpKRERVP-FSEKFKNADPDAIDLLEKMLVFDPKKRISAAEA---LAHPYLA-----PYH----DPTDEP 301

                ...
gi 66773086 338 PAA 340
Cdd:cd07856 302 VAD 304
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
156-244 1.62e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 53.36  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  156 QQLGLALDFMHGRQLVHRDIKPENVLLFDREcrRVKLADFGMTRRV-GCRVKRV----SGTIPYTAPEVcqagradgLAV 230
Cdd:PHA03211 267 RQLLSAIDYIHGEGIIHRDIKTENVLVNGPE--DICLGDFGAACFArGSWSTPFhygiAGTVDTNAPEV--------LAG 336
                         90
                 ....*....|....*..
gi 66773086  231 D---TGVDVWAFGVLIF 244
Cdd:PHA03211 337 DpytPSVDIWSAGLVIF 353
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
141-196 1.77e-07

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 52.44  E-value: 1.77e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 141 PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENvLLFDRECRRVKLADFG 196
Cdd:cd14013 112 PRGPKRENVIIKSIMRQILVALRKLHSTGIVHRDVKPQN-IIVSEGDGQFKIIDLG 166
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
52-254 1.86e-07

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 52.11  E-value: 1.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  52 HYELVRELGKGTYGkvdlVVYKGT----GTKMALKFvNKSKTKLKNFLREVSITNSLSSSPFIIKVfdvvfetedcYVFA 127
Cdd:cd14127   1 HYKVGKKIGEGSFG----VIFEGTnllnGQQVAIKF-EPRKSDAPQLRDEYRTYKLLAGCPGIPNV----------YYFG 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAGDLFDIIPPQVglpED---------TVKRCVQ---QLGLALDFMHGRQLVHRDIKPENVLL---FDRECRRVKL 192
Cdd:cd14127  66 QEGLHNILVIDLLGPSL---EDlfdlcgrkfSVKTVVMvakQMLTRVQTIHEKNLIYRDIKPDNFLIgrpGTKNANVIHV 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 193 ADFGMTRRVgcRVKRVSGTIPYTAPEvCQAGRADGLAVDTGV--------DVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14127 143 VDFGMAKQY--RDPKTKQHIPYREKK-SLSGTARYMSINTHLgreqsrrdDLEALGHVFMYFLRGSLPWQ 209
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
54-243 2.46e-07

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: 51.74  E-value: 2.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVReLGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN---FLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQEY 130
Cdd:cd14049  10 EIAR-LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDcmkVLREVKVLAGLQH-PNIVGYHTAWMEHVQLMLYIQMQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLFDIIPPQVGLP-EDTVKRC-------------VQQLGLALDFMHGRQLVHRDIKPENVLLFDRECrRVKLADFG 196
Cdd:cd14049  88 LCELSLWDWIVERNKRPcEEEFKSApytpvdvdvttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDI-HVRIGDFG 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 197 ---------------MTRRVGCRVKRVSGTIPYTAPEvcqagRADGLAVDTGVDVWAFGVLI 243
Cdd:cd14049 167 lacpdilqdgndsttMSRLNGLTHTSGVGTCLYAAPE-----QLEGSHYDFKSDMYSIGVIL 223
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
68-303 2.82e-07

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: 52.29  E-value: 2.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  68 DLVVYKGTGTKM--ALKFVNKSKTKLKNFLREVSITNSLSSSPFIikvfdvvfETEDCYVFAQEYAPAGDLFDiippQVG 145
Cdd:cd05103 109 EFVPYKTKGARFrqGKDYVGDISVDLKRRLDSITSSQSSASSGFV--------EEKSLSDVEEEEAGQEDLYK----DFL 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 146 LPEDTVkrCVQ-QLGLALDFMHGRQLVHRDIKPENVLLFDRECrrVKLADFGMTRRV---GCRVKRVSGTIP--YTAPEV 219
Cdd:cd05103 177 TLEDLI--CYSfQVAKGMEFLASRKCIHRDLAARNILLSENNV--VKICDFGLARDIykdPDYVRKGDARLPlkWMAPET 252
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 220 CqagrADGLAVdTGVDVWAFGVLIFCVLT-GNFPWEAASGADAFFEEFVRWQRGRLPglpsqwrRFTEPalRMFQRLLAL 298
Cdd:cd05103 253 I----FDRVYT-IQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKEGTRMRAP-------DYTTP--EMYQTMLDC 318

                ....*...
gi 66773086 299 ---EPERR 303
Cdd:cd05103 319 whgEPSQR 326
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
55-253 2.87e-07

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 51.55  E-value: 2.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVDLV-VYKGTGTK----MALKFV-NKSKTKLKNFLREVSITNSLSSSpFIIKVFDVVFETeDCYVFAQ 128
Cdd:cd05094   9 LKRELGEGAFGKVFLAeCYNLSPTKdkmlVAVKTLkDPTLAARKDFQREAELLTNLQHD-HIVKFYGVCGDG-DPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 129 EYAPAGDLFDII----PPQVGLPEDTVKRCVQQLGLA------------LDFMHGRQLVHRDIKPENVLLFDRECrrVKL 192
Cdd:cd05094  87 EYMKHGDLNKFLrahgPDAMILVDGQPRQAKGELGLSqmlhiatqiasgMVYLASQHFVHRDLATRNCLVGANLL--VKI 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086 193 ADFGMTRRV-GCRVKRVSG----TIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPW 253
Cdd:cd05094 165 GDFGMSRDVySTDYYRVGGhtmlPIRWMPPESIMYRK-----FTTESDVWSFGVILWEIFTyGKQPW 226
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
110-254 2.95e-07

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 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 TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 51.42  E-value: 2.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 110 IIKVFDVVFETEDCYVFAQeyAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLFDREcrR 189
Cdd:cd14024  47 VCSVLEVVIGQDRAYAFFS--RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDEL--R 122
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 190 VKLA-------------DFGMTRRVGCRVkrvsgtipYTAPEVCQAGRA-DGLAvdtgVDVWAFGVLIFCVLTGNFPWE 254
Cdd:cd14024 123 TKLVlvnledscplngdDDSLTDKHGCPA--------YVGPEILSSRRSySGKA----ADVWSLGVCLYTMLLGRYPFQ 189
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
157-279 3.44e-07

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 51.73  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 157 QLGLALDFMHGRQLVHRDIKPENVLL-FD-RECRRVKLADFG---MTRRVGCRVKRVS------GTIPYTAPEVCQAGRA 225
Cdd:cd14018 146 QLLEGVDHLVRHGIAHRDLKSDNILLeLDfDGCPWLVIADFGcclADDSIGLQLPFSSwyvdrgGNACLMAPEVSTAVPG 225
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 226 DGLAVDTG-VDVWAFGVLIFCVLTGNFPWEAASGADAffeEFVRWQRGRLPGLPS 279
Cdd:cd14018 226 PGVVINYSkADAWAVGAIAYEIFGLSNPFYGLGDTML---ESRSYQESQLPALPS 277
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
50-248 3.64e-07

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They 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 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 51.57  E-value: 3.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  50 TKHYELVRELGKGTYGKV---------DLVV--YKGTGTKMALKFV-------NKSKTKLKNFLREVSITNSLSSsPFII 111
Cdd:cd05051   4 REKLEFVEKLGEGQFGEVhlceanglsDLTSddFIGNDNKDEPVLVavkmlrpDASKNAREDFLKEVKIMSQLKD-PNIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 112 KVFDVVFETEDCYVFAqEYAPAGDLFDIIppQVGLPEDTVKRCVQQLGL---ALDFM-----------HGRQLVHRDIKP 177
Cdd:cd05051  83 RLLGVCTRDEPLCMIV-EYMENGDLNQFL--QKHEAETQGASATNSKTLsygTLLYMatqiasgmkylESLNFVHRDLAT 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66773086 178 ENVLLFDRecRRVKLADFGMTR----RVGCRVK-RVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT 248
Cdd:cd05051 160 RNCLVGPN--YTIKIADFGMSRnlysGDYYRIEgRAVLPIRWMAWESILLGK-----FTTKSDVWAFGVTLWEILT 228
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
49-243 4.68e-07

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: 51.63  E-value: 4.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKV----DLVVYKGTG-TKMALKFVNKskTKLKNFLREVSITNSLSSSPFI--IKVF---DVVF 118
Cdd:cd07874  15 VLKRYQNLKPIGSGAQGIVcaayDAVLDRNVAiKKLSRPFQNQ--THAKRAYRELVLMKCVNHKNIIslLNVFtpqKSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVfAQEYAPAgDLFDIIppQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMT 198
Cdd:cd07874  93 EFQDVYL-VMELMDA-NLCQVI--QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV-KSDC-TLKILDFGLA 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGCRVKRVSGTIP--YTAPEVCQagradGLAVDTGVDVWAFGVLI 243
Cdd:cd07874 167 RTAGTSFMMTPYVVTryYRAPEVIL-----GMGYKENVDIWSVGCIM 208
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
56-311 6.64e-07

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: 50.70  E-value: 6.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKFVNKSKTKLKN---FLREVSITNSLSSSPFIIKVFDVVFEtEDCYVFAQEYAP 132
Cdd:cd14139   5 LEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNeqlALHEVYAHAVLGHHPHVVRYYSAWAE-DDHMIIQNEYCN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 133 AGDLFDIIPPQVGL----PEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdreCRRVKL-----------ADFGM 197
Cdd:cd14139  84 GGSLQDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI----CHKMQSssgvgeevsneEDEFL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 198 TRRVGCRVKRVSGTIPYTAPEVcQAGRADGLAVDT---------GVDVWAFGVLIFcvltgnfpweAASGADAFFEEFVR 268
Cdd:cd14139 160 SANVVYKIGDLGHVTSINKPQV-EEGDSRFLANEIlqedyrhlpKADIFALGLTVA----------LAAGAEPLPTNGAA 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 66773086 269 WQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14139 229 WHHIRKGNFPDVPQELPESFSSLLKNMIQPDPEQRPSATALAR 271
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
75-311 6.80e-07

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 50.12  E-value: 6.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  75 TGTKMALKFVNKS--KTKLKNFLRevsitnsLSSSPFIIKVFDVVFETEDCYVFaQEYApAGDLFDIIPPQVGLPEDTVK 152
Cdd:cd13976  17 TGEELVCKVVPVPecHAVLRAYFR-------LPSHPNISGVHEVIAGETKAYVF-FERD-HGDLHSYVRSRKRLREPEAA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 153 RCVQQLGLALDFMHGRQLVHRDIKPENVLLFDRECRRVKLA-----------DFGMTRRVGCRVkrvsgtipYTAPEVCQ 221
Cdd:cd13976  88 RLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLEsledavilegeDDSLSDKHGCPA--------YVSPEILN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 222 AGRA-DGLAVDtgvdVWAFGVLIFCVLTGNFPWEAASGADAffeeFVRWQRGRLpGLPSQwrrFTEPALRMFQRLLALEP 300
Cdd:cd13976 160 SGATySGKAAD----VWSLGVILYTMLVGRYPFHDSEPASL----FAKIRRGQF-AIPET---LSPRARCLIRSLLRREP 227
                       250
                ....*....|.
gi 66773086 301 ERRGPAKEVFR 311
Cdd:cd13976 228 SERLTAEDILL 238
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
157-275 6.88e-07

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: 50.77  E-value: 6.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 157 QLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMTRRVGCR---VKRVSGTIP--YTAPEVCqagrADGLaVD 231
Cdd:cd14207 188 QVARGMEFLSSRKCIHRDLAARNILL--SENNVVKICDFGLARDIYKNpdyVRKGDARLPlkWMAPESI----FDKI-YS 260
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 66773086 232 TGVDVWAFGVLIFCVLT-GNFPWEAASGADAFFEEFVRWQRGRLP 275
Cdd:cd14207 261 TKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMRAP 305
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
156-313 9.61e-07

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 49.91  E-value: 9.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 156 QQLGLALDFMHGRQLVHRDIKPENVLLFDRECRR-----VKLADFGMTRRVGCRVKRVSgTIPYTAPEVCQAGRadglAV 230
Cdd:cd05076 123 RQLASALSYLENKNLVHGNVCAKNILLARLGLEEgtspfIKLSDPGVGLGVLSREERVE-RIPWIAPECVPGGN----SL 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 231 DTGVDVWAFG-VLIFCVLTGNFPWEAASGADAffEEFVRwQRGRLPglpsqwrrftEPALRMFQRL----LALEPERRGP 305
Cdd:cd05076 198 STAADKWGFGaTLLEICFNGEAPLQSRTPSEK--ERFYQ-RQHRLP----------EPSCPELATLisqcLTYEPTQRPS 264

                ....*...
gi 66773086 306 AKEVFRFL 313
Cdd:cd05076 265 FRTILRDL 272
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
54-244 1.17e-06

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 49.83  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  54 ELVRELGKGTYGKV------DLVVYKgTGTKMALKFVNK--SKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETED-CY 124
Cdd:cd05050   8 EYVRDIGQGAFGRVfqarapGLLPYE-PFTMVAVKMLKEeaSADMQADFQREAALMAEFDH-PNIVKLLGVCAVGKPmCL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 125 VFaqEYAPAGDLFDII----PPQV-GLPEDTVK-----------RCVQQLGLALDFMHG------RQLVHRDIKPENVLL 182
Cdd:cd05050  86 LF--EYMAYGDLNEFLrhrsPRAQcSLSHSTSSarkcglnplplSCTEQLCIAKQVAAGmaylseRKFVHRDLATRNCLV 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66773086 183 fdRECRRVKLADFGMTRRVgcrvkrvsgtipYTApEVCQAGRADGLAV-------------DTGVDVWAFGVLIF 244
Cdd:cd05050 164 --GENMVVKIADFGLSRNI------------YSA-DYYKASENDAIPIrwmppesifynryTTESDVWAYGVVLW 223
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
123-265 1.19e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 50.38  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  123 CYVFAQEYAPAGDLFDIippqvglpEDTVKRcvqqlglALDFMHGRQLVHRDIKPENVllFDRECRRVKLADFGmtrrVG 202
Cdd:PHA03212 171 CYLAAKRNIAICDILAI--------ERSVLR-------AIQYLHENRIIHRDIKAENI--FINHPGDVCLGDFG----AA 229
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66773086  203 C--------RVKRVSGTIPYTAPEVcqagradgLAVD---TGVDVWAFGVLIFcvltgnfpwEAASGADAFFEE 265
Cdd:PHA03212 230 CfpvdinanKYYGWAGTIATNAPEL--------LARDpygPAVDIWSAGIVLF---------EMATCHDSLFEK 286
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
28-251 1.41e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 50.46  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   28 GVPLLTEDMQALTLRTLAAS------------------DVTKHYELVRELGKGTYGKV---DLVVYKGT-----GTKMAL 81
Cdd:PHA03210 107 DGPSGAEDSDASHLDFDEAPpdaagpvplaqaklkhddEFLAHFRVIDDLPAGAFGKIficALRASTEEaearrGVNSTN 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   82 KFVNKSKTKLKNFLREVS-----ITNSLSSSPF-----IIKVFDVVFETEDCYVFAQEYApaGDLFDIIPPQVGLPEDT- 150
Cdd:PHA03210 187 QGKPKCERLIAKRVKAGSraaiqLENEILALGRlnhenILKIEEILRSEANTYMITQKYD--FDLYSFMYDEAFDWKDRp 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  151 ----VKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdrECR-RVKLADFG-MTRRVGCRVKRV---SGTIPYTAPEVCq 221
Cdd:PHA03210 265 llkqTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFL---NCDgKIVLGDFGtAMPFEKEREAFDygwVGTVATNSPEIL- 340
                        250       260       270
                 ....*....|....*....|....*....|
gi 66773086  222 AGraDGLAVDTgvDVWAFGVLIFCVLTGNF 251
Cdd:PHA03210 341 AG--DGYCEIT--DIWSCGLILLDMLSHDF 366
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
55-275 1.55e-06

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 49.62  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKVdlvvYKG----TGTKMA-------LKFVNKSKtKLKNFLREVSITNSLSSsPFIIKVFDVVFETED- 122
Cdd:cd05090   9 FMEELGECAFGKI----YKGhlylPGMDHAqlvaiktLKDYNNPQ-QWNEFQQEASLMTELHH-PNIVCLLGVVTQEQPv 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 123 CYVFaqEYAPAGDLFDII---PPQ--VGLPED---TVKRCVQ---------QLGLALDFMHGRQLVHRDIKPENVLLfdR 185
Cdd:cd05090  83 CMLF--EFMNQGDLHEFLimrSPHsdVGCSSDedgTVKSSLDhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILV--G 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 186 ECRRVKLADFGMTRRV-----GCRVKRVSGTIPYTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFPWEAASGA 259
Cdd:cd05090 159 EQLHVKISDLGLSREIyssdyYRVQNKSLLPIRWMPPEAIMYGK-----FSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ 233
                       250
                ....*....|....*.
gi 66773086 260 DAFfeEFVRwQRGRLP 275
Cdd:cd05090 234 EVI--EMVR-KRQLLP 246
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
41-326 1.64e-06

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: 49.25  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  41 LRTLAASDVTKhyelVRELGKGTYGkvdlVVYKG--------TGTKMALKFV--NKSKTKLKNFLREVSITNSLSSsPFI 110
Cdd:cd05109   1 MRILKETELKK----VKVLGSGAFG----TVYKGiwipdgenVKIPVAIKVLreNTSPKANKEILDEAYVMAGVGS-PYV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 111 IKVFDVVFETEDCYVfaQEYAPAGDLFDIIPPQVGL--PEDTVKRCVQqLGLALDFMHGRQLVHRDIKPENVLLfdRECR 188
Cdd:cd05109  72 CRLLGICLTSTVQLV--TQLMPYGCLLDYVRENKDRigSQDLLNWCVQ-IAKGMSYLEEVRLVHRDLAARNVLV--KSPN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 189 RVKLADFGMTRRVGCRVKRV---SGTIP--YTAPEVCQAGRADGLAvdtgvDVWAFGVLIFCVLT-GNFPWEAASGADaf 262
Cdd:cd05109 147 HVKITDFGLARLLDIDETEYhadGGKVPikWMALESILHRRFTHQS-----DVWSYGVTVWELMTfGAKPYDGIPARE-- 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 263 feefvrwqrgrLPGLPSQWRRFTEPAL------RMFQRLLALEPERRgPAkevFRFLKHELTSeLRRRPS 326
Cdd:cd05109 220 -----------IPDLLEKGERLPQPPIctidvyMIMVKCWMIDSECR-PR---FRELVDEFSR-MARDPS 273
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
59-311 1.65e-06

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 49.13  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVdlvvYKGT----------GTKMALKFVNKS-KTKLKNFLREVSITNSLSSSPFIIkVFDVVFETEDCYVfa 127
Cdd:cd14208   7 LGKGSFTKI----YRGLrtdeeddercETEVLLKVMDPThGNCQESFLEAASIMSQISHKHLVL-LHGVCVGKDSIMV-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 128 QEYAPAG--DLFDIIPPQVGLPEDTVK-RCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRR-----VKLADFGMTR 199
Cdd:cd14208  80 QEFVCHGalDLYLKKQQQKGPVAISWKlQVVKQLAYALNYLEDKQLVHGNVSAKKVLL-SREGDKgsppfIKLSDPGVSI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 200 RVgCRVKRVSGTIPYTAPEVCQagRADGLAVDTgvDVWAFGVLIFCVLT-GNFPWEAASGADA--FFEEfvrwqRGRLPG 276
Cdd:cd14208 159 KV-LDEELLAERIPWVAPECLS--DPQNLALEA--DKWGFGATLWEIFSgGHMPLSALDPSKKlqFYND-----RKQLPA 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 66773086 277 lpsqwRRFTEPALrMFQRLLALEPERRGPAKEVFR 311
Cdd:cd14208 229 -----PHWIELAS-LIQQCMSYNPLLRPSFRAIIR 257
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
19-202 2.05e-06

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 49.79  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   19 PGTAPGpgagvpllTEDMQALT--LRTLAASDVTKHYELVRELGKGTYGkvdlVVYKGTGTKMALKFVNKSKTKLKNFLR 96
Cdd:PLN03225 106 PGVAPG--------FVDMFVLAplEGLFRPSFKKDDFVLGKKLGEGAFG----VVYKASLVNKQSKKEGKYVLKKATEYG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086   97 EVSI-TNSL-------SSSPFIIKVFDVV-FETEDCYVFAQEYAPAGDLFDII-----PPQV---------GLPEDT--- 150
Cdd:PLN03225 174 AVEIwMNERvrracpnSCADFVYGFLEPVsSKKEDEYWLVWRYEGESTLADLMqskefPYNVepyllgkvqDLPKGLere 253
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 66773086  151 ---VKRCVQQLGLALDFMHGRQLVHRDIKPENVlLFDRECRRVKLADFGMTR--RVG 202
Cdd:PLN03225 254 nkiIQTIMRQILFALDGLHSTGIVHRDVKPQNI-IFSEGSGSFKIIDLGAAAdlRVG 309
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
56-311 2.41e-06

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: 48.94  E-value: 2.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  56 VRELGKGTYGKVDLVVYKGTGTKMALKfvnKSKTKL------KNFLREVSITNSLSSSPFIIKVFDVVFEtEDCYVFAQE 129
Cdd:cd14051   5 VEKIGSGEFGSVYKCINRLDGCVYAIK---KSKKPVagsvdeQNALNEVYAHAVLGKHPHVVRYYSAWAE-DDHMIIQNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 YAPAGDLFDIIPP--QVG--LPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECRRV--------------- 190
Cdd:cd14051  81 YCNGGSLADAISEneKAGerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFI-SRTPNPVsseeeeedfegeedn 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 191 --------KLADFGmtrrvgcRVKRVS------GTIPYTAPEVCQAGRaDGLavdTGVDVWAFGVLIFCvltgnfpweaA 256
Cdd:cd14051 160 pesnevtyKIGDLG-------HVTSISnpqveeGDCRFLANEILQENY-SHL---PKADIFALALTVYE----------A 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 257 SGADAF---FEEFVRWQRGRLPGLPSQWRRFTEPALRMFQRllalEPERRGPAKEVFR 311
Cdd:cd14051 219 AGGGPLpknGDEWHEIRQGNLPPLPQCSPEFNELLRSMIHP----DPEKRPSAAALLQ 272
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
49-243 2.82e-06

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: 48.89  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKV----DLVVYKGTG-TKMALKFVNKskTKLKNFLREVSITNSLSSSPFI--IKVF---DVVF 118
Cdd:cd07875  22 VLKRYQNLKPIGSGAQGIVcaayDAILERNVAiKKLSRPFQNQ--THAKRAYRELVLMKCVNHKNIIglLNVFtpqKSLE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 119 ETEDCYVfAQEYAPAgDLFDIIppQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMT 198
Cdd:cd07875 100 EFQDVYI-VMELMDA-NLCQVI--QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV-KSDC-TLKILDFGLA 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 66773086 199 RRVGCRVKRVSGTIP--YTAPEVCQagradGLAVDTGVDVWAFGVLI 243
Cdd:cd07875 174 RTAGTSFMMTPYVVTryYRAPEVIL-----GMGYKENVDIWSVGCIM 215
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
55-325 2.86e-06

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: 48.47  E-value: 2.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  55 LVRELGKGTYGKV--DLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSsPFIIKVFDVVFETEDCYVFAQE 129
Cdd:cd05075   4 LGKTLGEGEFGSVmeGQLNQDDSVLKVAVKTMKIaicTRSEMEDFLSEAVCMKEFDH-PNVMRLIGVCLQNTESEGYPSP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 130 -----YAPAGDLFDII------PPQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfdRECRRVKLADFGMT 198
Cdd:cd05075  83 vvilpFMKHGDLHSFLlysrlgDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCML--NENMNVCVADFGLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 199 RRV----GCRVKRVSGT-IPYTAPEvcqaGRADGLAVdTGVDVWAFGVLIFCVLT-GNFPWEAASGADAFfeEFVRwqrg 272
Cdd:cd05075 161 KKIyngdYYRQGRISKMpVKWIAIE----SLADRVYT-TKSDVWSFGVTMWEIATrGQTPYPGVENSEIY--DYLR---- 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66773086 273 rlpglpsQWRRFTEPA------LRMFQRLLALEPERRgPAkevFRFLKHELTSELRRRP 325
Cdd:cd05075 230 -------QGNRLKQPPdcldglYELMSSCWLLNPKDR-PS---FETLRCELEKILKDLP 277
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
59-296 3.77e-06

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: 48.51  E-value: 3.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGkvdlVVYKGT--GTKMALK-FVNKSKtklKNFLREVSITN-SLSSSPFIIKVF----DVVFETEDCYVFAQEY 130
Cdd:cd14054   3 IGQGRYG----TVWKGSldERPVAVKvFPARHR---QNFQNEKDIYElPLMEHSNILRFIgadeRPTADGRMEYLLVLEY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 131 APAGDLfdiippQVGLPEDTVK-----RCVQQLGLALDFMHG---RQ------LVHRDIKPENVLL-FDRECrrvKLADF 195
Cdd:cd14054  76 APKGSL------CSYLRENTLDwmsscRMALSLTRGLAYLHTdlrRGdqykpaIAHRDLNSRNVLVkADGSC---VICDF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 196 GMTRRV-GCRVKRVS------------GTIPYTAPEVCqagraDGlAVD--------TGVDVWAFGVLIFCVLT------ 248
Cdd:cd14054 147 GLAMVLrGSSLVRGRpgaaenasisevGTLRYMAPEVL-----EG-AVNlrdcesalKQVDVYALGLVLWEIAMrcsdly 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66773086 249 -----GNF--PWEAASGADAFFEE---FVRWQRGRlPGLPSQWRRFTePALRMFQRLL 296
Cdd:cd14054 221 pgesvPPYqmPYEAELGNHPTFEDmqlLVSREKAR-PKFPDAWKENS-LAVRSLKETI 276
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
49-260 4.97e-06

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: 48.10  E-value: 4.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  49 VTKHYELVRELGKGTYGKVDLVVYKGTGTKMALKFVNK---SKTKLKNFLREVSITNSLSSSPFI--IKVF---DVVFET 120
Cdd:cd07876  19 VLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRpfqNQTHAKRAYRELVLLKCVNHKNIIslLNVFtpqKSLEEF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 121 EDCYVfAQEYAPAgDLFDIIppQVGLPEDTVKRCVQQLGLALDFMHGRQLVHRDIKPENVLLfDRECrRVKLADFGMTRR 200
Cdd:cd07876  99 QDVYL-VMELMDA-NLCQVI--HMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV-KSDC-TLKILDFGLART 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773086 201 VGCRVKRVSGTIP--YTAPEVCQagradGLAVDTGVDVWAFGVLIFCVLTGNFPWEAASGAD 260
Cdd:cd07876 173 ACTNFMMTPYVVTryYRAPEVIL-----GMGYKENVDIWSVGCIMGELVKGSVIFQGTDHID 229
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
59-254 5.05e-06

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: 47.66  E-value: 5.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086  59 LGKGTYGKVDLVVYKGTGTK---MALKFVNKSKTKLK--NFLREVSITNSLSSSPfIIKVFDVVFETEDCYVFAqEYAPA 133
Cdd:cd05063  13 IGAGEFGEVFRGILKMPGRKevaVAIKTLKPGYTEKQrqDFLSEASIMGQFSHHN-IIRLEGVVTKFKPAMIIT-EYMEN 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773086 134 GDLFDIIPPQVGlpEDTVKRCVQQL-GLA--LDFMHGRQLVHRDIKPENVLLFDR-ECrrvKLADFGMTRRVG----CRV 205
Cdd:cd05063  91 GALDKYLRDHDG--EFSSYQLVGMLrGIAagMKYLSDMNYVHRDLAARNILVNSNlEC---KVSDFGLSRVLEddpeGTY 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 66773086 206 KRVSGTIP--YTAPEVCQAGRadglaVDTGVDVWAFGVLIFCVLT-GNFP-WE 254
Cdd:cd05063 166 TTSGGKIPirWTAPEAIAYRK-----FTSASDVWSFGIVMWEVMSfGERPyWD 213
 
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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