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Conserved domains on  [gi|126215545|ref|NP_081156|]
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serine/threonine-protein kinase PINK1, mitochondrial precursor [Mus musculus]

Protein Classification

serine/threonine-protein kinase PINK1( domain architecture ID 10197102)

serine/threonine-protein kinase PINK1 (Pten INduced Kinase 1) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it plays an important role in maintaining mitochondrial homeostasis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
162-511 0e+00

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: 531.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 162 IGKGCNAAVYEATMptlpqhlekakhlgligkgpdvvlkgadgeqapgtptFPFAIKMMWNISAGSSSEAILSKMSQELV 241
Cdd:cd14018    1 IGKGCNAAVYEAAL-------------------------------------FPLAIKMMWNISAGSSSEAILRSMGNELV 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 242 PASRVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYP 321
Cdd:cd14018   44 PAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNYP 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 322 CTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADQHVGLRLPFNS 401
Cdd:cd14018  124 CTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVERGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEA 481
Cdd:cd14018  204 WYVDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPDV 283
                        330       340       350
                 ....*....|....*....|....*....|
gi 126215545 482 RRLVRSLLQREASKRPSARLAANVLHLSLW 511
Cdd:cd14018  284 RQVVKDLLQRDPNKRVSARVAANVLHLSLW 313
 
Name Accession Description Interval E-value
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
162-511 0e+00

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: 531.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 162 IGKGCNAAVYEATMptlpqhlekakhlgligkgpdvvlkgadgeqapgtptFPFAIKMMWNISAGSSSEAILSKMSQELV 241
Cdd:cd14018    1 IGKGCNAAVYEAAL-------------------------------------FPLAIKMMWNISAGSSSEAILRSMGNELV 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 242 PASRVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYP 321
Cdd:cd14018   44 PAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNYP 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 322 CTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADQHVGLRLPFNS 401
Cdd:cd14018  124 CTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVERGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEA 481
Cdd:cd14018  204 WYVDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPDV 283
                        330       340       350
                 ....*....|....*....|....*....|
gi 126215545 482 RRLVRSLLQREASKRPSARLAANVLHLSLW 511
Cdd:cd14018  284 RQVVKDLLQRDPNKRVSARVAANVLHLSLW 313
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
270-500 3.10e-28

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 113.39  E-value: 3.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   270 HPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYPC-TLRQYLEEQTP-SSRLATMMTLQLLE 347
Cdd:smart00220  56 HPNIVRLYDVFE---------------------------DEDKLYLVMEYCEGgDLFDLLKKRGRlSEDEARFYLRQILS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   348 GVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVGLRlpfnSSSVerggnGSL--MAPEVSTAHSgps 425
Cdd:smart00220 109 ALEYLHSKGIVHRDLKPENILL--DEDGH--VKLADFGLARQLDPGEKL----TTFV-----GTPeyMAPEVLLGKG--- 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545   426 avidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPES--VPPEARRLVRSLLQREASKRPSAR 500
Cdd:smart00220 173 ----YGkAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwdISPEAKDLIRKLLVKDPEKRLTAE 246
Pkinase pfam00069
Protein kinase domain;
270-500 4.45e-25

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 104.23  E-value: 4.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545  270 HPNIIRVFRAFTSsvpllpgaladypdmlPPHYYpeglghgrtlfLVMKNYPCT-LRQYLEEQTP-SSRLATMMTLQLLE 347
Cdd:pfam00069  57 HPNIVRLYDAFED----------------KDNLY-----------LVLEYVEGGsLFDLLSEKGAfSEREAKFIMKQILE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545  348 GVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFG-CCLADQHVGLrlpfnSSSVerggnGSL--MAPEV--STAHS 422
Cdd:pfam00069 110 GLEYLHSNGIVHRDLKPENILIDEDGN----LKITDFGlARQLNSGSSL-----TTFV-----GTPwyMAPEVlgGNPYG 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545  423 gpsavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSY-QEAQLPEMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:pfam00069 176 --------PKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIdQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTAT 246
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
265-525 8.43e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 85.56  E-value: 8.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSvpllpgaladypdmlPPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEqtpssrlATMMTLQ 344
Cdd:COG0515   52 ASLNHPPNIVKLYDFFQDE---------------GSLYLVMEYVDGGSLEDLLKKIGRKGPLSESE-------ALFILAQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpWLVISDFGCCLADQHVGLRLPFNSSSVERGGNGSLMAPEVstaHSGP 424
Cdd:COG0515  110 ILSALEYLHSKGIIHRDIKPENILLDRDGR---VVKLIDFGLAKLLPDPGSTSSIPALPSTSVGTPGYMAPEV---LLGL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 425 SAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQ-------EAQLPEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:COG0515  184 SLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelptPSLASPLSPSNPELISKAASDLLKKLLAKDP 263
                        250       260
                 ....*....|....*....|....*...
gi 126215545 498 SARLAANVLHLSLWGEHLLALKNLKLDK 525
Cdd:COG0515  264 KNRLSSSSDLSHDLLAHLKLKESDLSDL 291
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
324-500 8.34e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 61.42  E-value: 8.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRL-----ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwLV-ISDFGCCladqhvglRL 397
Cdd:PTZ00283 126 LRQEIKSRAKTNRTfreheAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL--CSNG---LVkLGDFGFS--------KM 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 398 PFNSSSVERG----GNGSLMAPEVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQeAQLPE 472
Cdd:PTZ00283 193 YAATVSDDVGrtfcGTPYYVAPEIWRRKP-------YSKkADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLA-GRYDP 264
                        170       180
                 ....*....|....*....|....*...
gi 126215545 473 MPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:PTZ00283 265 LPPSISPEMQEIVTALLSSDPKRRPSSS 292
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
314-385 8.54e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 48.64  E-value: 8.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 314 FLVMKnY--PCTLRQYLEEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwLV-ISDFG 385
Cdd:NF033483  83 YIVME-YvdGRTLKDYIREHGPlSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI--TKDG---RVkVTDFG 152
 
Name Accession Description Interval E-value
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
162-511 0e+00

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: 531.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 162 IGKGCNAAVYEATMptlpqhlekakhlgligkgpdvvlkgadgeqapgtptFPFAIKMMWNISAGSSSEAILSKMSQELV 241
Cdd:cd14018    1 IGKGCNAAVYEAAL-------------------------------------FPLAIKMMWNISAGSSSEAILRSMGNELV 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 242 PASRVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYP 321
Cdd:cd14018   44 PAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNYP 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 322 CTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADQHVGLRLPFNS 401
Cdd:cd14018  124 CTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVERGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEA 481
Cdd:cd14018  204 WYVDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPDV 283
                        330       340       350
                 ....*....|....*....|....*....|
gi 126215545 482 RRLVRSLLQREASKRPSARLAANVLHLSLW 511
Cdd:cd14018  284 RQVVKDLLQRDPNKRVSARVAANVLHLSLW 313
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
270-500 3.10e-28

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 113.39  E-value: 3.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   270 HPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYPC-TLRQYLEEQTP-SSRLATMMTLQLLE 347
Cdd:smart00220  56 HPNIVRLYDVFE---------------------------DEDKLYLVMEYCEGgDLFDLLKKRGRlSEDEARFYLRQILS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   348 GVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVGLRlpfnSSSVerggnGSL--MAPEVSTAHSgps 425
Cdd:smart00220 109 ALEYLHSKGIVHRDLKPENILL--DEDGH--VKLADFGLARQLDPGEKL----TTFV-----GTPeyMAPEVLLGKG--- 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545   426 avidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPES--VPPEARRLVRSLLQREASKRPSAR 500
Cdd:smart00220 173 ----YGkAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwdISPEAKDLIRKLLVKDPEKRLTAE 246
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
270-500 1.59e-25

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: 104.66  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSsvpllpgaladypdmlpphyypeglghGRTLFLVMKNYP-CTLRQYLEEQ--TPSSRLATMMTLQLL 346
Cdd:cd00180   50 HPNIVKLYDVFET---------------------------ENFLYLVMEYCEgGSLKDLLKENkgPLSEEEALSILRQLL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVGLRLPFNSSSVERGgngsLMAPEVstaHSGPSa 426
Cdd:cd00180  103 SALEYLHSNGIIHRDLKPENILL--DSDGT--VKLADFGLAKDLDSDDSLLKTTGGTTPPY----YAPPEL---LGGRY- 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 427 viDYSKADTWAVGAIAYEIfglanpfygqgsahlesrsyqeaqlpempesvpPEARRLVRSLLQREASKRPSAR 500
Cdd:cd00180  171 --YGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPKKRPSAK 209
Pkinase pfam00069
Protein kinase domain;
270-500 4.45e-25

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 104.23  E-value: 4.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545  270 HPNIIRVFRAFTSsvpllpgaladypdmlPPHYYpeglghgrtlfLVMKNYPCT-LRQYLEEQTP-SSRLATMMTLQLLE 347
Cdd:pfam00069  57 HPNIVRLYDAFED----------------KDNLY-----------LVLEYVEGGsLFDLLSEKGAfSEREAKFIMKQILE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545  348 GVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFG-CCLADQHVGLrlpfnSSSVerggnGSL--MAPEV--STAHS 422
Cdd:pfam00069 110 GLEYLHSNGIVHRDLKPENILIDEDGN----LKITDFGlARQLNSGSSL-----TTFV-----GTPwyMAPEVlgGNPYG 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545  423 gpsavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSY-QEAQLPEMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:pfam00069 176 --------PKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIdQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTAT 246
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
342-500 6.16e-24

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: 101.06  E-value: 6.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCladqhvgLRLpfnSSSVERGGNGSL------MAP 415
Cdd:cd06606  105 TRQILEGLEYLHSNGIVHRDIKGANILV--DSDGV--VKLADFGCA-------KRL---AEIATGEGTKSLrgtpywMAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EV--STAHSgpsavidySKADTWAVGAIAYEIFGLANPFYGQGS-AHLESRSYQEAQLPEMPESVPPEARRLVRSLLQRE 492
Cdd:cd06606  171 EVirGEGYG--------RAADIWSLGCTVIEMATGKPPWSELGNpVAALFKIGSSGEPPPIPEHLSEEAKDFLRKCLQRD 242

                 ....*...
gi 126215545 493 ASKRPSAR 500
Cdd:cd06606  243 PKKRPTAD 250
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
270-507 3.23e-22

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: 96.12  E-value: 3.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYP-CTLRQYLEEQTP-SSRLATMMTLQLLE 347
Cdd:cd14014   59 HPNIVRVYDVGE---------------------------DDGRPYIVMEYVEgGSLADLLRERGPlPPREALRILAQIAD 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVEWDsdgcPWLVISDFGccLAdqhvglrLPFNSSSVERGGN--GSL--MAPEVstAHSG 423
Cdd:cd14014  112 ALAAAHRAGIVHRDIKPANILLTED----GRVKLTDFG--IA-------RALGDSGLTQTGSvlGTPayMAPEQ--ARGG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PsavIDYsKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEA--QLPEMPESVPPEARRLVRSLLQREASKRP-SAR 500
Cdd:cd14014  177 P---VDP-RSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAppPPSPLNPDVPPALDAIILRALAKDPEERPqSAA 252

                 ....*..
gi 126215545 501 LAANVLH 507
Cdd:cd14014  253 ELLAALR 259
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
270-498 4.29e-22

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: 95.68  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSsvpllpgaladypdmlPPHYYpeglghgrtlfLVMKNYPC-TLRQYLEEQTP--SSRLATMMTLQLL 346
Cdd:cd13999   49 HPNIVQFIGACLS----------------PPPLC-----------IVTEYMPGgSLYDLLHKKKIplSWSLRLKIALDIA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL--MAPEVstAHSGP 424
Cdd:cd13999  102 RGMNYLHSPPIIHRDLKSLNILL--DENFT--VKIADFG--LS------RIKNSTTEKMTGVVGTPrwMAPEV--LRGEP 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 425 savidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd13999  168 -----YTeKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEKRPS 237
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
323-499 2.71e-20

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: 90.61  E-value: 2.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 323 TLRQYLEEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLadqhvglrlpFNS 401
Cdd:cd14007   86 ELYKELKKQKRfDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILL--GSNGE--LKLADFGWSV----------HAP 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVERGGNGSL--MAPEV--STAHsgpsaviDYsKADTWAVGAIAYE-IFGLAnPFygqgsahlESRSYQEAQ------L 470
Cdd:cd14007  152 SNRRKTFCGTLdyLPPEMveGKEY-------DY-KVDIWSLGVLCYElLVGKP-PF--------ESKSHQETYkriqnvD 214
                        170       180
                 ....*....|....*....|....*....
gi 126215545 471 PEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14007  215 IKFPSSVSPEAKDLISKLLQKDPSKRLSL 243
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
344-502 1.83e-19

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: 87.96  E-value: 1.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladQHVGLRLPFNSSSVerggnGSL--MAPEVSTAH 421
Cdd:cd05123  101 EIVLALEYLHSLGIIYRDLKPENILL--DSDG--HIKLTDFGLA---KELSSDGDRTYTFC-----GTPeyLAPEVLLGK 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 sgpsaviDYSKA-DTWAVGAIAYE-IFGLAnPFYGQGSAHLEsRSYQEAQLpEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd05123  169 -------GYGKAvDWWSLGVLLYEmLTGKP-PFYAENRKEIY-EKILKSPL-KFPEYVSPEAKSLISGLLQKDPTKRLGS 238

                 ...
gi 126215545 500 RLA 502
Cdd:cd05123  239 GGA 241
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
344-502 1.18e-18

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: 85.40  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVISDFGccLA---DQHVGLRLPFnsssvergGNGSLMAPEvsta 420
Cdd:cd14006   97 QLLEGLQYLHNHHILHLDLKPENILL--ADRPSPQIKIIDFG--LArklNPGEELKEIF--------GTPEFVAPE---- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 hsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGSAHLES--RSYQEAQLPEMPESVPPEARRLVRSLLQREAS 494
Cdd:cd14006  161 ------IVNGEpvslATDMWSIGVLTYVLLSGLSPFLGEDDQETLAniSACRVDFSEEYFSSVSQEAKDFIRKLLVKEPR 234

                 ....*...
gi 126215545 495 KRPSARLA 502
Cdd:cd14006  235 KRPTAQEA 242
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
270-500 4.23e-18

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: 84.06  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSsvpllpgaladypdmlPPHYY--PEgLGHGRTLF--LVMKNYpctlrqYLEEQTpssrlATMMTlQL 345
Cdd:cd05117   58 HPNIVKLYEVFED----------------DKNLYlvME-LCTGGELFdrIVKKGS------FSEREA-----AKIMK-QI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGccLADQhvglrlpFNSSSVERGGNGSL--MAPEVSTAHSg 423
Cdd:cd05117  109 LSAVAYLHSQGIVHRDLKPENILLASKDPDSP-IKIIDFG--LAKI-------FEEGEKLKTVCGTPyyVAPEVLKGKG- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 psavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLEsRSYQEAQL---PEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd05117  178 ------YGKKcDIWSLGVILYILLCGYPPFYGETEQELF-EKILKGKYsfdSPEWKNVSEEAKDLIKRLLVVDPKKRLTA 250

                 .
gi 126215545 500 R 500
Cdd:cd05117  251 A 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
265-525 8.43e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 85.56  E-value: 8.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSvpllpgaladypdmlPPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEqtpssrlATMMTLQ 344
Cdd:COG0515   52 ASLNHPPNIVKLYDFFQDE---------------GSLYLVMEYVDGGSLEDLLKKIGRKGPLSESE-------ALFILAQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpWLVISDFGCCLADQHVGLRLPFNSSSVERGGNGSLMAPEVstaHSGP 424
Cdd:COG0515  110 ILSALEYLHSKGIIHRDIKPENILLDRDGR---VVKLIDFGLAKLLPDPGSTSSIPALPSTSVGTPGYMAPEV---LLGL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 425 SAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQ-------EAQLPEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:COG0515  184 SLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelptPSLASPLSPSNPELISKAASDLLKKLLAKDP 263
                        250       260
                 ....*....|....*....|....*...
gi 126215545 498 SARLAANVLHLSLWGEHLLALKNLKLDK 525
Cdd:COG0515  264 KNRLSSSSDLSHDLLAHLKLKESDLSDL 291
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
344-498 4.49e-17

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: 81.02  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG-CCLADQHVGLRlpfnsSSVerggnGSL--MAPEV--S 418
Cdd:cd14003  107 QLISAVDYCHSNGIVHRDLKLENILL--DKNGN--LKIIDFGlSNEFRGGSLLK-----TFC-----GTPayAAPEVllG 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHSGPsavidysKADTWAVGAIAYeiFGLAN--PFYGQGSAHLESRSYQEAqlPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14003  173 RKYDGP-------KADVWSLGVILY--AMLTGylPFDDDNDSKLFRKILKGK--YPIPSHLSPDARDLIRRMLVVDPSKR 241

                 ..
gi 126215545 497 PS 498
Cdd:cd14003  242 IT 243
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
329-499 1.01e-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: 80.16  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwLVISDFGCCladqhvglRLPFNSSSVERGG 408
Cdd:cd08222   99 SGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-----IKVGDFGIS--------RILMGTSDLATTF 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 NGS--LMAPEVsTAHSGPSavidySKADTWAVGAIAYEIFGLANPFYGQGsahLESRSYQ--EAQLPEMPESVPPEARRL 484
Cdd:cd08222  166 TGTpyYMSPEV-LKHEGYN-----SKSDIWSLGCILYEMCCLKHAFDGQN---LLSVMYKivEGETPSLPDKYSKELNAI 236
                        170
                 ....*....|....*
gi 126215545 485 VRSLLQREASKRPSA 499
Cdd:cd08222  237 YSRMLNKDPALRPSA 251
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
310-499 1.75e-16

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: 79.66  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPC-TLRQYLEEQ-TPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGCC 387
Cdd:cd13994   70 HGKWCLVMEYCPGgDLFTLIEKAdSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL----DEDGVLKLTDFGTA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 388 ladqhVGLRLPFNSSS-VERGGNGS--LMAPEVSTahsgpSAVIDYSKADTWAVGAIAYEIFGLANPFygqGSAHLESRS 464
Cdd:cd13994  146 -----EVFGMPAEKESpMSAGLCGSepYMAPEVFT-----SGSYDGRAVDVWSCGIVLFALFTGRFPW---RSAKKSDSA 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 126215545 465 YQEAQL--------PEMPESVPP-EARRLVRSLLQREASKRPSA 499
Cdd:cd13994  213 YKAYEKsgdftngpYEPIENLLPsECRRLIYRMLHPDPEKRITI 256
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
270-500 2.45e-16

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: 79.04  E-value: 2.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKnYpC---TLRQYLEEQTPSSRLATM-----M 341
Cdd:cd08215   58 HPNIVKYYESFE---------------------------ENGKLCIVME-Y-AdggDLAQKIKKQKKKGQPFPEeqildW 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG--------CCLADQHVGLrlPFNsssverggngslM 413
Cdd:cd08215  109 FVQICLALKYLHSRKILHRDLKTQNIFL--TKDGV--VKLGDFGiskvlestTDLAKTVVGT--PYY------------L 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVstAHSGPsavidYS-KADTWAVGAIAYEIFGLANPFYGQgsaHLESRSYQ--EAQLPEMPESVPPEARRLVRSLLQ 490
Cdd:cd08215  171 SPEL--CENKP-----YNyKSDIWALGCVLYELCTLKHPFEAN---NLPALVYKivKGQYPPIPSQYSSELRDLVNSMLQ 240
                        250
                 ....*....|
gi 126215545 491 REASKRPSAR 500
Cdd:cd08215  241 KDPEKRPSAN 250
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
344-499 2.89e-16

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: 79.12  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccladqhVGLRLPFNSSSVERGGN-----GSL--MAPE 416
Cdd:cd06628  114 QILKGLNYLHNRGIIHRDIKGANILV--DNKGG--IKISDFG-------ISKKLEANSLSTKNNGArpslqGSVfwMAPE 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 V--STAHSgpsavidySKADTWAVGAIAYEIFGLANPF--YGQGSAHLESRSYqeaQLPEMPESVPPEARRLVRSLLQRE 492
Cdd:cd06628  183 VvkQTSYT--------RKADIWSLGCLVVEMLTGTHPFpdCTQMQAIFKIGEN---ASPTIPSNISSEARDFLEKTFEID 251

                 ....*..
gi 126215545 493 ASKRPSA 499
Cdd:cd06628  252 HNKRPTA 258
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
311-505 8.56e-16

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: 77.64  E-value: 8.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYP-----CTLRQ--YLEEQtpssrLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISD 383
Cdd:cd05579   66 KNLYLVMEYLPggdlySLLENvgALDED-----VARIYIAEIVLALEYLHSHGIIHRDLKPDNILI--DANG--HLKLTD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 384 FGCC---LADQHVGLRLPFNSSSVERGGNGSL------MAPEV--STAHSgpsavidySKADTWAVGAIAYE-IFGLAnP 451
Cdd:cd05579  137 FGLSkvgLVRRQIKLSIQKKSNGAPEKEDRRIvgtpdyLAPEIllGQGHG--------KTVDWWSLGVILYEfLVGIP-P 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 452 FYGQGS----AHLESRSYqeaQLPEMPEsVPPEARRLVRSLLQREASKRPSARLAANV 505
Cdd:cd05579  208 FHAETPeeifQNILNGKI---EWPEDPE-VSDEAKDLISKLLTPDPEKRLGAKGIEEI 261
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
348-496 1.07e-15

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: 77.30  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAHsgpsav 427
Cdd:cd05578  112 ALDYLHSKNIIHRDIKPDNILL--DEQG--HVHITDFN-------IATKLTDGTLATSTSGTKPYMAPEVFMRA------ 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126215545 428 iDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLES-RSYQEAQLPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05578  175 -GYSFAvDWWSLGVTAYEMLRGKRPYEIHSRTSIEEiRAKFETASVLYPAGWSEEAIDLINKLLERDPQKR 244
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
341-504 1.37e-15

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: 77.13  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcPWLV-ISDFGccLAD-QHVGLRLpfnsssVERGGNGSLMAPEV- 417
Cdd:cd14098  106 LTKQILEAMAYTHSMGITHRDLKPENILITQDD---PVIVkISDFG--LAKvIHTGTFL------VTFCGTMAYLAPEIl 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 -STAHSGPSAvidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESR----SYQEAQLPEMpeSVPPEARRLVRSLLQR 491
Cdd:cd14098  175 mSKEQNLQGG---YSnLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRirkgRYTQPPLVDF--NISEEAIDFILRLLDV 249
                        170
                 ....*....|...
gi 126215545 492 EASKRPSARLAAN 504
Cdd:cd14098  250 DPEKRMTAAQALD 262
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
313-498 7.34e-15

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: 74.60  E-value: 7.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYPCTLRQYLEEQtPSSRL----ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCpwLVISDFGccL 388
Cdd:cd14119   71 LYMVMEYCVGGLQEMLDSA-PDKRLpiwqAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLT--TDGT--LKISDFG--V 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQhvglrL-PFNSSSVERGGNGS--LMAPEVSTAHSGPSAVidysKADTWAVGAIAYEIFGLANPFYGQGSAHL-ESRS 464
Cdd:cd14119  144 AEA-----LdLFAEDDTCTTSQGSpaFQPPEIANGQDSFSGF----KVDIWSAGVTLYNMTTGKYPFEGDNIYKLfENIG 214
                        170       180       190
                 ....*....|....*....|....*....|....
gi 126215545 465 YQEAQlpeMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14119  215 KGEYT---IPDDVDPDLQDLLRGMLEKDPEKRFT 245
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
349-504 1.58e-14

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: 73.97  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFgccladqhvGLRLPFNSSSVERG----GNGSLMAPEV-STAHSG 423
Cdd:cd05583  112 LEHLHKLGIIYRDIKLENILL--DSEG--HVVLTDF---------GLSKEFLPGENDRAysfcGTIEYMAPEVvRGGSDG 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSAVIDYskadtWAVGAIAYEIFGLANPFY--GQGSAHLE-SRSYQEAQlPEMPESVPPEARRLVRSLLQreasKRPSAR 500
Cdd:cd05583  179 HDKAVDW-----WSLGVLTYELLTGASPFTvdGERNSQSEiSKRILKSH-PPIPKTFSAEAKDFILKLLE----KDPKKR 248

                 ....
gi 126215545 501 LAAN 504
Cdd:cd05583  249 LGAG 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
265-500 1.74e-14

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: 73.74  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLApHPNIIRVFRAFtssvpllpgalaDYPDMlpphyypeglghgRTLFLVMKNYPCTLRQYLEEQTPSSRL----ATM 340
Cdd:cd14008   59 KKLD-HPNIVRLYEVI------------DDPES-------------DKLYLVLEYCEGGPVMELDSGDRVPPLpeetARK 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCcladqhvglrlpfnSSSVERGG------NGS--L 412
Cdd:cd14008  113 YFRDLVLGLEYLHENGIVHRDIKPENLLL--TADGT--VKISDFGV--------------SEMFEDGNdtlqktAGTpaF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 MAPEVSTAHSGPsavIDYSKADTWAVGAIAYE-IFGLAnPFYGqgsaHLESRSYQEAQL----PEMPESVPPEARRLVRS 487
Cdd:cd14008  175 LAPELCDGDSKT---YSGKAADIWALGVTLYClVFGRL-PFNG----DNILELYEAIQNqndeFPIPPELSPELKDLLRR 246
                        250
                 ....*....|...
gi 126215545 488 LLQREASKRPSAR 500
Cdd:cd14008  247 MLEKDPEKRITLK 259
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
270-500 1.80e-14

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: 73.87  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLlpgaladYPDMlppHYYPEGlghgrtlflvmknypcTLRQYLEEQTPSSR----LATMMTLQL 345
Cdd:cd13996   63 HPNIVRYYTAWVEEPPL-------YIQM---ELCEGG----------------TLRDWIDRRNSSSKndrkLALELFKQI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwLVISDFG--CCLADQHVGL----RLPFNSSSVERGGNGSL--MAPEV 417
Cdd:cd13996  117 LKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ---VKIGDFGlaTSIGNQKRELnnlnNNNNGNTSNNSVGIGTPlyASPEQ 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHsgpsaviDY-SKADTWAVGAIAYEIfglanpFYGQGSAHLESRSYQEA---QLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd13996  194 LDGE-------NYnEKADIYSLGIILFEM------LHPFKTAMERSTILTDLrngILPESFKAKHPKEADLIQSLLSKNP 260

                 ....*..
gi 126215545 494 SKRPSAR 500
Cdd:cd13996  261 EERPSAE 267
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
223-500 2.28e-14

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: 73.19  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 223 ISAGSSSEA--ILSKMSQEL--VPASRVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTssvpllpgaladypdml 298
Cdd:cd13997    8 IGSGSFSEVfkVRSKVDGCLyaVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWE----------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 299 pphyypeglgHGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLE----GVDHLVQQGIAHRDLKSDNILVewDS 373
Cdd:cd13997   71 ----------EGGHLYIQMELCENgSLQDALEELSPISKLSEAEVWDLLLqvalGLAFIHSKGIVHLDIKPDNIFI--SN 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 374 DGCpwLVISDFGCCladqhvgLRLPfnSSSVERGGNGSLMAPEVSTAHSGPSavidySKADTWAVGAIAYE-IFGLANPF 452
Cdd:cd13997  139 KGT--CKIGDFGLA-------TRLE--TSGDVEEGDSRYLAPELLNENYTHL-----PKADIFSLGVTVYEaATGEPLPR 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 126215545 453 YGQGSAHLesrsyQEAQLPEMPESV-PPEARRLVRSLLQREASKRPSAR 500
Cdd:cd13997  203 NGQQWQQL-----RQGKLPLPPGLVlSQELTRLLKVMLDPDPTRRPTAD 246
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
337-500 4.16e-14

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: 72.26  E-value: 4.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 337 LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwLV-ISDFGccladqhVGLRLpfnsSSVERGGNGSL--- 412
Cdd:cd06627  100 LVAVYIYQVLEGLAYLHEQGVIHRDIKGANILT--TKDG---LVkLADFG-------VATKL----NEVEKDENSVVgtp 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 --MAPEVsTAHSGPSavidySKADTWAVGAIAYEIFGLANPFYGQGSAhleSRSYQEAQLPEM--PESVPPEARRLVRSL 488
Cdd:cd06627  164 ywMAPEV-IEMSGVT-----TASDIWSVGCTVIELLTGNPPYYDLQPM---AALFRIVQDDHPplPENISPELRDFLLQC 234
                        170
                 ....*....|..
gi 126215545 489 LQREASKRPSAR 500
Cdd:cd06627  235 FQKDPTLRPSAK 246
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
325-507 4.49e-14

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: 72.75  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 325 RQYLEEQTpssrlATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFgcclaDQHVGLRLPFNSSSV 404
Cdd:cd14173   94 RRHFNELE-----ASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSP-VKICDF-----DLGSGIKLNSDCSPI 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 ERG------GNGSLMAPEVSTAHSGPSAVIDySKADTWAVGAIAYEIFGLANPFYG--------------QGSAHLESRS 464
Cdd:cd14173  163 STPelltpcGSAEYMAPEVVEAFNEEASIYD-KRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwdrgeacPACQNMLFES 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 126215545 465 YQEAQLpEMPES----VPPEARRLVRSLLQREASKRPSarlAANVLH 507
Cdd:cd14173  242 IQEGKY-EFPEKdwahISCAAKDLISKLLVRDAKQRLS---AAQVLQ 284
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
342-499 4.96e-14

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: 72.44  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLADQHVGLRLPfnsSSVErgGNGSLMAPEVSTAH 421
Cdd:cd06632  108 TRQILSGLAYLHSRNTVHRDIKGANILV--DTNGV--VKLADFG--MAKHVEAFSFA---KSFK--GSPYWMAPEVIMQK 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGPSAVidysKADTWAVGAIAYEIFGLANPF--YGQGSAHLESRSYQEaqLPEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd06632  177 NSGYGL----AVDIWSLGCTVLEMATGKPPWsqYEGVAAIFKIGNSGE--LPPIPDHLSPDAKDFIRLCLQRDPEDRPTA 250
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
269-499 5.63e-14

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: 72.03  E-value: 5.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 269 PHPNIIRVFRAFTSSVpllpgalaDYPDMLPPHyypeglGHGRTLFLVMKnypctLRQYLEEQtpssrLATMMTLQLLEG 348
Cdd:cd14004   66 SHPNIVKLLDFFEDDE--------FYYLVMEKH------GSGMDLFDFIE-----RKPNMDEK-----EAKYIFRQVADA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVewDSDGCPWLVisDFGccladqhvglrlpfNSSSVERG------GNGSLMAPEV--STA 420
Cdd:cd14004  122 VKHLHDQGIVHRDIKDENVIL--DGNGTIKLI--DFG--------------SAAYIKSGpfdtfvGTIDYAAPEVlrGNP 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 421 HSGPsavidysKADTWAVGAIAYEIFGLANPFYgqgsahlESRSYQEAQLpEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14004  184 YGGK-------EQDIWALGVLLYTLVFKENPFY-------NIEEILEADL-RIPYAVSEDLIDLISRMLNRDVGDRPTI 247
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
270-498 6.16e-14

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: 72.19  E-value: 6.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLL-------PGALADYpdmlpphyypeglghgrtlfLVMKNYPctlRQYLEEQTPSSRLATMMT 342
Cdd:cd00192   55 HPNVVRLLGVCTEEEPLYlvmeymeGGDLLDF--------------------LRKSRPV---FPSPEPSTLSLKDLLSFA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwlV-ISDFGccLADQHvglrlpFNSSSVERGGNGSL----MAPEv 417
Cdd:cd00192  112 IQIAKGMEYLASKKFVHRDLAARNCLV--GEDLV---VkISDFG--LSRDI------YDDDYYRKKTGGKLpirwMAPE- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsaVIDY----SKADTWAVGAIAYEIFGL-ANPFYG----QGSAHLESRSYqeaqlPEMPESVPPEARRLVRSL 488
Cdd:cd00192  178 ---------SLKDgiftSKSDVWSFGVLLWEIFTLgATPYPGlsneEVLEYLRKGYR-----LPKPENCPDELYELMLSC 243
                        250
                 ....*....|
gi 126215545 489 LQREASKRPS 498
Cdd:cd00192  244 WQLDPEDRPT 253
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
269-504 8.11e-14

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: 71.50  E-value: 8.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 269 PHPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYPCTLRQYLEEQTP--SSRLATMMTLQLL 346
Cdd:cd05118   57 GHPNIVKLLDVFEHR-------------------------GGNHLCLVFELMGMNLYELIKDYPRglPLDLIKSYLYQLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwLVISDFG-CCLADQHvglrlPFNSSSVERGgngsLMAPEVSTahsgps 425
Cdd:cd05118  112 QALDFLHSNGIIHRDLKPENILINLELGQ---LKLADFGlARSFTSP-----PYTPYVATRW----YRAPEVLL------ 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 426 AVIDYSKA-DTWAVGAIAYEIFglanpfygQGSAHLESRSYQEaQLPEMPESV-PPEARRLVRSLLQREASKRPSARLAA 503
Cdd:cd05118  174 GAKPYGSSiDIWSLGCILAELL--------TGRPLFPGDSEVD-QLAKIVRLLgTPEALDLLSKMLKYDPAKRITASQAL 244

                 .
gi 126215545 504 N 504
Cdd:cd05118  245 A 245
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
323-500 1.18e-13

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: 71.26  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 323 TLRQY--LEEQtpssrLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDG-CPwlvISDFGCCLADQHVglrlPF 399
Cdd:cd06629   98 CLRKYgkFEED-----LVRFFTRQILDGLAYLHSKGILHRDLKADNILV--DLEGiCK---ISDFGISKKSDDI----YG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 400 NSSSVERGGNGSLMAPEV-STAHSGPSAvidysKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESV- 477
Cdd:cd06629  164 NNGATSMQGSVFWMAPEViHSQGQGYSA-----KVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPEDVn 238
                        170       180
                 ....*....|....*....|....
gi 126215545 478 -PPEARRLVRSLLQREASKRPSAR 500
Cdd:cd06629  239 lSPEALDFLNACFAIDPRDRPTAA 262
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
338-499 2.11e-13

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 70.91  E-value: 2.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDF----GCCLADQHV-GLRLPFNSSSVergGNGSL 412
Cdd:cd14090  102 ASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSP-VKICDFdlgsGIKLSSTSMtPVTTPELLTPV---GSAEY 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 MAPEVSTAHSGPSAVIDySKADTWAVGAIAYEIFGLANPFYG---------QGSA-----HLESRSYQEAQLpEMPES-- 476
Cdd:cd14090  178 MAPEVVDAFVGEALSYD-KRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdRGEAcqdcqELLFHSIQEGEY-EFPEKew 255
                        170       180
                 ....*....|....*....|....*
gi 126215545 477 --VPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14090  256 shISAEAKDLISHLLVRDASQRYTA 280
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
270-499 2.34e-13

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: 70.31  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYPC-TLRQYLEeqtpssrlATMMTLQ---- 344
Cdd:cd05122   56 HPNIVKYYGSYL---------------------------KKDELWIVMEFCSGgSLKDLLK--------NTNKTLTeqqi 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 ------LLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwLV-ISDFGCC--LADqhvglrlpfNSSSVERGGNGSLMAP 415
Cdd:cd05122  101 ayvckeVLKGLEYLHSHGIIHRDIKAANILL--TSDG---EVkLIDFGLSaqLSD---------GKTRNTFVGTPYWMAP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAhsgpsavIDYS-KADTWAVGAIAYEIFGLANPFYGQGS--AHLESRSYQEAQLPEmPESVPPEARRLVRSLLQRE 492
Cdd:cd05122  167 EVIQG-------KPYGfKADIWSLGITAIEMAEGKPPYSELPPmkALFLIATNGPPGLRN-PKKWSKEFKDFLKKCLQKD 238

                 ....*..
gi 126215545 493 ASKRPSA 499
Cdd:cd05122  239 PEKRPTA 245
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
349-489 3.12e-13

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: 71.16  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADQHVGLRLPFNSSSVERG--------------------- 407
Cdd:cd05573  114 LDSLHKLGFIHRDIKPDNILL--DADG--HIKLADFGLCTKMNKSGDRESYLNDSVNTLfqdnvlarrrphkqrrvrays 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 408 --GNGSLMAPEVSTAHS-GPSavidyskADTWAVGAIAYE-IFGLAnPFYGQGSAHLESR--SYQEA-QLPEMPEsVPPE 480
Cdd:cd05573  190 avGTPDYIAPEVLRGTGyGPE-------CDWWSLGVILYEmLYGFP-PFYSDSLVETYSKimNWKESlVFPDDPD-VSPE 260

                 ....*....
gi 126215545 481 ARRLVRSLL 489
Cdd:cd05573  261 AIDLIRRLL 269
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
324-498 3.60e-13

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 69.48  E-value: 3.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   324 LRQYLEEQTPSSRLATM--MTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLADQHvglrlpfNS 401
Cdd:smart00219  88 LLSYLRKNRPKLSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLV--GENLV--VKISDFG--LSRDL-------YD 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   402 SSVERGGNGSL----MAPEvstahsgpsaVIDY----SKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSyQEAQLPE 472
Cdd:smart00219 155 DDYYRKRGGKLpirwMAPE----------SLKEgkftSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYL-KNGYRLP 223
                          170       180
                   ....*....|....*....|....*.
gi 126215545   473 MPESVPPEARRLVRSLLQREASKRPS 498
Cdd:smart00219 224 QPPNCPPELYDLMLQCWAEDPEDRPT 249
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
344-499 3.80e-13

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: 69.94  E-value: 3.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCclADQhvglrLPFNSSSVERGGNGSLMAPE------- 416
Cdd:cd05581  109 EIVLALEYLHSKGIIHRDLKPENILL--DEDM--HIKITDFGT--AKV-----LGPDSSPESTKGDADSQIAYnqaraas 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 -VSTAHSGPSAVIDYSKA----DTWAVGAIAYEIF-GLAnPFYGQGSAHL----ESRSYqeaqlpEMPESVPPEARRLVR 486
Cdd:cd05581  178 fVGTAEYVSPELLNEKPAgkssDLWALGCIIYQMLtGKP-PFRGSNEYLTfqkiVKLEY------EFPENFPPDAKDLIQ 250
                        170
                 ....*....|...
gi 126215545 487 SLLQREASKRPSA 499
Cdd:cd05581  251 KLLVLDPSKRLGV 263
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
270-500 4.11e-13

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: 69.61  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVF-----RAFTS-SVPLLPGALADYPDmlPPHYYPEGLGHGRTLFLVMKnypctlrqyleeqtpssrlatmmtl 343
Cdd:cd13982   54 HPNVIRYFctekdRQFLYiALELCAASLQDLVE--SPRESKLFLRPGLEPVRLLR------------------------- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWD-SDGCPWLVISDFGCCladqhvgLRLPFNSSSVER--GGNGSL--MAPEV- 417
Cdd:cd13982  107 QIASGLAHLHSLNIVHRDLKPQNILISTPnAHGNVRAMISDFGLC-------KKLDVGRSSFSRrsGVAGTSgwIAPEMl 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 --STAHSGPSAVidyskaDTWAVGAIAYEIF-GLANPFygqGS-----AHLESRSYQEAQLPEMpESVPPEARRLVRSLL 489
Cdd:cd13982  180 sgSTKRRQTRAV------DIFSLGCVFYYVLsGGSHPF---GDklereANILKGKYSLDKLLSL-GEHGPEAQDLIERMI 249
                        250
                 ....*....|.
gi 126215545 490 QREASKRPSAR 500
Cdd:cd13982  250 DFDPEKRPSAE 260
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
265-500 4.82e-13

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: 69.87  E-value: 4.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghgRTLFLVMKNYPCTLRQYLEEQT----PSSRLATM 340
Cdd:cd07830   52 RKLNEHPNIVKLKEVFREN---------------------------DELYFVFEYMEGNLYQLMKDRKgkpfSESVIRSI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MtLQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCpwLVISDFGccLAdQHVGLRLPFN---SSSVERggngslmAPEV 417
Cdd:cd07830  105 I-YQILQGLAHIHKHGFFHRDLKPENLLVS--GPEV--VKIADFG--LA-REIRSRPPYTdyvSTRWYR-------APEI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSgpsaviDYSKA-DTWAVGAIAYEIFGLaNPFYgQGSAHLE-----------------SRSYQEAQ-----LPEMP 474
Cdd:cd07830  170 LLRST------SYSSPvDIWALGCIMAELYTL-RPLF-PGSSEIDqlykicsvlgtptkqdwPEGYKLASklgfrFPQFA 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 126215545 475 E--------SVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd07830  242 PtslhqlipNASPEAIDLIKDMLRWDPKKRPTAS 275
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
342-499 6.51e-13

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: 68.97  E-value: 6.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwlvISDFGCC--LAdqhvGLrlpfNSSSVERGGNGSLMAPEvst 419
Cdd:cd06624  114 TKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVK---ISDFGTSkrLA----GI----NPCTETFTGTLQYMAPE--- 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 ahsgpsaVID-----YSK-ADTWAVGAIAYEIFGLANPFYGQGSAH---LESRSYQEAqlPEMPESVPPEARRLVRSLLQ 490
Cdd:cd06624  180 -------VIDkgqrgYGPpADIWSLGCTIIEMATGKPPFIELGEPQaamFKVGMFKIH--PEIPESLSEEAKSFILRCFE 250

                 ....*....
gi 126215545 491 REASKRPSA 499
Cdd:cd06624  251 PDPDKRATA 259
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
344-496 7.73e-13

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: 69.95  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFgccladqhvGLRLPFNSSSVERG----GNGSLMAPEVST 419
Cdd:cd05614  113 EIILALEHLHKLGIVYRDIKLENILL--DSEG--HVVLTDF---------GLSKEFLTEEKERTysfcGTIEYMAPEIIR 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPSAVIDYskadtWAVGAIAYEIFGLANPFYGQGSAHLE---SRSYQEAQlPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05614  180 GKSGHGKAVDW-----WSLGILMFELLTGASPFTLEGEKNTQsevSRRILKCD-PPFPSFIGPVARDLLQKLLCKDPKKR 253
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
342-499 7.92e-13

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: 68.62  E-value: 7.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewdsdgCPWLVIS--DFGCcladqhvGLRLPFNSSSVERG-------GNGSL 412
Cdd:cd06631  109 TKQILEGVAYLHNNNVIHRDIKGNNIML------MPNGVIKliDFGC-------AKRLCINLSSGSQSqllksmrGTPYW 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 MAPEV--STAHSgpsavidySKADTWAVGAIAYEIFG----------LANPFY-GQGSAhlesrsyqeaQLPEMPESVPP 479
Cdd:cd06631  176 MAPEVinETGHG--------RKSDIWSIGCTVFEMATgkppwadmnpMAAIFAiGSGRK----------PVPRLPDKFSP 237
                        170       180
                 ....*....|....*....|
gi 126215545 480 EARRLVRSLLQREASKRPSA 499
Cdd:cd06631  238 EARDFVHACLTRDQDERPSA 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
344-498 8.42e-13

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: 68.47  E-value: 8.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCPWLVISDFGccLAdQHVGLRlpfNSSSVERggnGS--LMAPEVSTAH 421
Cdd:cd14121  103 QLASALQFLREHNISHMDLKPQNLLLS--SRYNPVLKLADFG--FA-QHLKPN---DEAHSLR---GSplYMAPEMILKK 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SgpsavidY-SKADTWAVGAIAYEI-FGLAnPFYGQGSAHLES--RSYQEAQLPEMPEsVPPEARRLVRSLLQREASKRP 497
Cdd:cd14121  172 K-------YdARVDLWSVGVILYEClFGRA-PFASRSFEELEEkiRSSKPIEIPTRPE-LSADCRDLLLRLLQRDPDRRI 242

                 .
gi 126215545 498 S 498
Cdd:cd14121  243 S 243
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
342-499 8.50e-13

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: 68.87  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVGLRLPFNSSSvERGGNGSLMAPEVSTah 421
Cdd:cd06626  105 TLQLLEGLAYLHENGIVHRDIKPANIFL--DSNGL--IKLGDFGSAVKLKNNTTTMAPGEVN-SLVGTPAYMAPEVIT-- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 sGPSAVIDYSKADTWAVGAIAYE-IFG------LANPF---YGQGSAHlesrsyqEAQLPEmPESVPPEARRLVRSLLQR 491
Cdd:cd06626  178 -GNKGEGHGRAADIWSLGCVVLEmATGkrpwseLDNEWaimYHVGMGH-------KPPIPD-SLQLSPEGKDFLSRCLES 248

                 ....*...
gi 126215545 492 EASKRPSA 499
Cdd:cd06626  249 DPKKRPTA 256
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
303-498 1.06e-12

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: 68.19  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 303 YPEGLGHGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMT-----LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgc 376
Cdd:cd08530   64 YKEAFLDGNRLCIVMEYAPFgDLSKLISKRKKKRRLFPEDDiwrifIQMLRGLKALHDQKILHRDLKSANILLSAGDL-- 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 377 pwLVISDFGCC------LADQHVGLrlPFnsssverggngsLMAPEV--STAHSgpsavidySKADTWAVGAIAYEIFGL 448
Cdd:cd08530  142 --VKIGDLGISkvlkknLAKTQIGT--PL------------YAAPEVwkGRPYD--------YKSDIWSLGCLLYEMATF 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 126215545 449 ANPFYGQGSAHLeSRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd08530  198 RPPFEARTMQEL-RYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPS 246
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
270-498 1.12e-12

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: 68.36  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYPCT-LRQYLEEQTP-SSRLATMMTLQLLE 347
Cdd:cd14080   61 HPNIIQVYSIFE---------------------------RGSKVFIFMEYAEHGdLLEYIQKRGAlSESQARIWFRQLAL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFG---CCLADQHVGLRLPFnsssverggNGSL--MAPEV--STA 420
Cdd:cd14080  114 AVQYLHSLDIAHRDLKCENILL----DSNNNVKLSDFGfarLCPDDDGDVLSKTF---------CGSAayAAPEIlqGIP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPsavidysKADTWAVGAIAYEIFGLANPFygqGSAHLES--RSYQEAQL--PEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14080  181 YDPK-------KYDIWSLGVILYIMLCGSMPF---DDSNIKKmlKDQQNRKVrfPSSVKKLSPECKDLIDQLLEPDPTKR 250

                 ..
gi 126215545 497 PS 498
Cdd:cd14080  251 AT 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
313-496 1.20e-12

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: 68.16  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMK--NYPCtLRQYLEEQ-TPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCP-----WLVISDF 384
Cdd:cd14120   67 VYLVMEycNGGD-LADYLQAKgTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPspndiRLKIADF 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAHSgpsavidY-SKADTWAVGAIAYEIFGLANPFYGQGSAHLESR 463
Cdd:cd14120  146 G-------FARFLQDGMMAATLCGSPMYMAPEVIMSLQ-------YdAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAF 211
                        170       180       190
                 ....*....|....*....|....*....|....
gi 126215545 464 SYQEAQL-PEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14120  212 YEKNANLrPNIPSGTSPALKDLLLGLLKRNPKDR 245
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
265-497 1.54e-12

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: 67.91  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYP-CTLRQYL------EEQTPSSRL 337
Cdd:cd08528   63 KEQLRHPNIVRYYKTFL---------------------------ENDRLYIVMELIEgAPLGEHFsslkekNEHFTEDRI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTlQLLEGVDHL-VQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQhvglrlpfnsssveRGGNGSLMAPE 416
Cdd:cd08528  116 WNIFV-QMVLALRYLhKEKQIVHRDLKPNNIMLGEDDK----VTITDFG--LAKQ--------------KGPESSKMTSV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VST-AHSGPSAVIDY---SKADTWAVGAIAYEIFGLANPFYGQGSAHLESRsYQEAQLPEMPESVPPE-ARRLVRSLLQR 491
Cdd:cd08528  175 VGTiLYSCPEIVQNEpygEKADIWALGCILYQMCTLQPPFYSTNMLTLATK-IVEAEYEPLPEGMYSDdITFVIRSCLTP 253

                 ....*.
gi 126215545 492 EASKRP 497
Cdd:cd08528  254 DPEARP 259
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
266-508 1.81e-12

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: 68.09  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVF-------RAFTSSVPLLpgaladypdmLPphYYPEGlghgrTLFLVMKNYpctlrqyLEEQT--PSSR 336
Cdd:cd13986   52 RLFNHPNILRLLdsqivkeAGGKKEVYLL----------LP--YYKRG-----SLQDEIERR-------LVKGTffPEDR 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 337 LATMMtLQLLEGVDHLVQQ---GIAHRDLKSDNILVewDSDGCPwlVISDFG-CCLAdqhvglRLPFNSSS------VER 406
Cdd:cd13986  108 ILHIF-LGICRGLKAMHEPelvPYAHRDIKPGNVLL--SEDDEP--ILMDLGsMNPA------RIEIEGRRealalqDWA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 407 GGNGSLM--APEVSTAHSGpsAVIDySKADTWAVGAIAYEIFGLANPF---YGQG-SAHLesrSYQEAQL-PEMPESVPP 479
Cdd:cd13986  177 AEHCTMPyrAPELFDVKSH--CTID-EKTDIWSLGCTLYALMYGESPFeriFQKGdSLAL---AVLSGNYsFPDNSRYSE 250
                        250       260
                 ....*....|....*....|....*....
gi 126215545 480 EARRLVRSLLQREASKRPSARLAANVLHL 508
Cdd:cd13986  251 ELHQLVKSMLVVNPAERPSIDDLLSRVHD 279
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
344-499 2.09e-12

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: 67.35  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVeWDSDgCPWLVISDFGcclADQHVGLRLPFNSSSVerggngSLMAPEVSTAHSG 423
Cdd:cd13987   99 QLASALDFMHSKNLVHRDIKPENVLL-FDKD-CRRVKLCDFG---LTRRVGSTVKRVSGTI------PYTAPEVCEAKKN 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSAVIDYSkADTWAVGAIAYEIfgLANPFYGQGSAHLESR-----SYQEAQLPEMP---ESVPPEARRLVRSLLQREASK 495
Cdd:cd13987  168 EGFVVDPS-IDVWAFGVLLFCC--LTGNFPWEKADSDDQFyeefvRWQKRKNTAVPsqwRRFTPKALRMFKKLLAPEPER 244

                 ....
gi 126215545 496 RPSA 499
Cdd:cd13987  245 RCSI 248
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
324-498 2.29e-12

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: 67.19  E-value: 2.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   324 LRQYL---EEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLADQHvglrlpfN 400
Cdd:smart00221  88 LLDYLrknRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV--GENLV--VKISDFG--LSRDL-------Y 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545   401 SSSVERGGNGSL----MAPEvstahsgpsaVIDY----SKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSyQEAQLP 471
Cdd:smart00221 155 DDDYYKVKGGKLpirwMAPE----------SLKEgkftSKSDVWSFGVLLWEIFTLgEEPYPGMSNAEVLEYL-KKGYRL 223
                          170       180
                   ....*....|....*....|....*..
gi 126215545   472 EMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:smart00221 224 PKPPNCPPELYKLMLQCWAEDPEDRPT 250
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
223-496 2.72e-12

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: 67.36  E-value: 2.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 223 ISAGSSSEAILS--KMSQELVPASRVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLlpgaladypdmlpp 300
Cdd:cd14167   11 LGTGAFSEVVLAeeKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHL-------------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 301 hYYPEGLGHGRTLF--LVMKNYpctlrqYLEeqtpssRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNIL---VEWDSDg 375
Cdd:cd14167   77 -YLIMQLVSGGELFdrIVEKGF------YTE------RDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSK- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 376 cpwLVISDFGCcladqhvglrlpfnsSSVErgGNGSLMAPEVST-AHSGPSAVID--YSKA-DTWAVGAIAYEIFGLANP 451
Cdd:cd14167  143 ---IMISDFGL---------------SKIE--GSGSVMSTACGTpGYVAPEVLAQkpYSKAvDCWSIGVIAYILLCGYPP 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 126215545 452 FYGQGSAHLESRSYQEAQLPEMP--ESVPPEARRLVRSLLQREASKR 496
Cdd:cd14167  203 FYDENDAKLFEQILKAEYEFDSPywDDISDSAKDFIQHLMEKDPEKR 249
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
344-496 3.60e-12

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: 67.33  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFgccladqhvGLRLPFNSSSVERG----GNGSLMAPE-VS 418
Cdd:cd05613  113 EIVLALEHLHKLGIIYRDIKLENILL--DSSG--HVVLTDF---------GLSKEFLLDENERAysfcGTIEYMAPEiVR 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHSGPSAVIDYskadtWAVGAIAYEIFGLANPFY--GQGSAHLE-SRSYQEAQlPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd05613  180 GGDSGHDKAVDW-----WSLGVLMYELLTGASPFTvdGEKNSQAEiSRRILKSE-PPYPQEMSALAKDIIQRLLMKDPKK 253

                 .
gi 126215545 496 R 496
Cdd:cd05613  254 R 254
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
328-496 4.82e-12

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: 66.94  E-value: 4.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 328 LEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVeWDSDGCPWLVISDFGCCLADQHvGLRlpfnSSSVerg 407
Cdd:cd14166   92 LERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLY-LTPDENSKIMITDFGLSKMEQN-GIM----STAC--- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 408 GNGSLMAPEVstahsgpSAVIDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMP--ESVPPEARRL 484
Cdd:cd14166  163 GTPGYVAPEV-------LAQKPYSKAvDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPfwDDISESAKDF 235
                        170
                 ....*....|..
gi 126215545 485 VRSLLQREASKR 496
Cdd:cd14166  236 IRHLLEKNPSKR 247
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
309-500 4.91e-12

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 66.36  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545  309 HGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATM--MTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwlV-ISDF 384
Cdd:pfam07714  72 QGEPLYIVTEYMPGgDLLDFLRKHKRKLTLKDLlsMALQIAKGMEYLESKNFVHRDLAARNCLV--SENLV---VkISDF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545  385 GccLAdqhvglRLPFNSSSVERGGNGSL----MAPEvstahsgpsaVIDY----SKADTWAVGAIAYEIFGL-ANPFYGQ 455
Cdd:pfam07714 147 G--LS------RDIYDDDYYRKRGGGKLpikwMAPE----------SLKDgkftSKSDVWSFGVLLWEIFTLgEQPYPGM 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 126215545  456 GSAHLESRSYQEAQLPeMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:pfam07714 209 SNEEVLEYLEDGYRLP-QPENCPDELYDLMKQCWAYDPEDRPTFS 252
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
270-502 5.94e-12

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: 66.35  E-value: 5.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghgRTLFLVMKNYPCTLRQYLEEQTPSSRLATM--MTLQLLE 347
Cdd:cd07829   57 HPNIVKLLDVIHTE---------------------------NKLYLVFEYCDQDLKKYLDKRPGPLPPNLIksIMYQLLR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLADQHvglRLPFNSSSVE------RggngslmAPEV--ST 419
Cdd:cd07829  110 GLAYCHSHRILHRDLKPQNLLI--NRDGV--LKLADFG--LARAF---GIPLRTYTHEvvtlwyR-------APEIllGS 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPSavidyskADTWAVGAIAYEIFGLANPFYGQGSAHL-----------ESRSYQE-AQLP----EMPESVP----- 478
Cdd:cd07829  174 KHYSTA-------VDIWSVGCIFAELITGKPLFPGDSEIDQlfkifqilgtpTEESWPGvTKLPdykpTFPKWPKndlek 246
                        250       260       270
                 ....*....|....*....|....*....|
gi 126215545 479 ------PEARRLVRSLLQREASKRPSARLA 502
Cdd:cd07829  247 vlprldPEGIDLLSKMLQYNPAKRISAKEA 276
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
215-502 6.47e-12

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: 66.22  E-value: 6.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 215 FAIKMMwNISAGSSSEAILSKMSQElvpasrvalageygavtYRRSRDGPKQLAPHPNIIRVFRAFTSSVpllpgalady 294
Cdd:cd14093   31 FAVKII-DITGEKSSENEAEELREA-----------------TRREIEILRQVSGHPNIIELHDVFESPT---------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 295 pdmlpphyypeglghgrTLFLVMKNYP-CTLRQYLEEQ-TPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWD 372
Cdd:cd14093   83 -----------------FIFLVFELCRkGELFDYLTEVvTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 373 SDgcpwLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAHSGPSAViDYSK-ADTWAVGAIAYEIFGLANP 451
Cdd:cd14093  146 LN----VKISDFG-------FATRLDEGEKLRELCGTPGYLAPEVLKCSMYDNAP-GYGKeVDMWACGVIMYTLLAGCPP 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 452 FYgqgsaH----LESRSYQEAQL----PEMpESVPPEARRLVRSLLQREASKRPSARLA 502
Cdd:cd14093  214 FW-----HrkqmVMLRNIMEGKYefgsPEW-DDISDTAKDLISKLLVVDPKKRLTAEEA 266
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
344-496 7.01e-12

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: 65.89  E-value: 7.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG-CCLADQHVGLRLPFNsssveRGGNGSLMAPEVsTAHS 422
Cdd:cd14663  108 QLIDAVDYCHSRGVFHRDLKPENLLL--DEDGN--LKISDFGlSALSEQFRQDGLLHT-----TCGTPNYVAPEV-LARR 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 423 GpsavIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLeSRSYQEAQlPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14663  178 G----YDGAKADIWSCGVILFVLLAGYLPFDDENLMAL-YRKIMKGE-FEYPRWFSPGAKSLIKRILDPNPSTR 245
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
342-500 8.50e-12

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: 66.01  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAh 421
Cdd:cd05577  101 AAEIICGLEHLHNRFIVYRDLKPENILL--DDHGH--VRISDLG-------LAVEFKGGKKIKGRVGTHGYMAPEVLQK- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 sgpSAVIDYSkADTWAVGAIAYEIFGLANPFYGQGSA----HLESRSYQEAQlpEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd05577  169 ---EVAYDFS-VDWFALGCMLYEMIAGRSPFRQRKEKvdkeELKRRTLEMAV--EYPDSFSPEARSLCEGLLQKDPERRL 242

                 ...
gi 126215545 498 SAR 500
Cdd:cd05577  243 GCR 245
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
270-499 1.06e-11

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: 65.27  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgalaDYpdmlppHYYPEGLGHGRTLFLVMKNypctlRQYLEEQTpssrlATMMTLQLLEGV 349
Cdd:cd14099   60 HPNIVKFHDCFEDE---------EN------VYILLELCSNGSLMELLKR-----RKALTEPE-----VRYFMRQILSGV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQ--HVGlrlpfnsssvERG----GNGSLMAPEVSTAHSG 423
Cdd:cd14099  115 KYLHSNRIIHRDLKLGNLFLDENMN----VKIGDFG--LAARleYDG----------ERKktlcGTPNYIAPEVLEKKKG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSavidySKADTWAVGAIAYE-IFGLAnPFygQGS------AHLESRSYqeaqlpEMPES--VPPEARRLVRSLLQREAS 494
Cdd:cd14099  179 HS-----FEVDIWSLGVILYTlLVGKP-PF--ETSdvketyKRIKKNEY------SFPSHlsISDEAKDLIRSMLQPDPT 244

                 ....*
gi 126215545 495 KRPSA 499
Cdd:cd14099  245 KRPSL 249
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
344-499 1.13e-11

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: 65.46  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG--CCLADqhvglrlPFNSSSVERG---GNGSLMAPEVS 418
Cdd:cd06610  110 EVLKGLEYLHSNGQIHRDVKAGNILL--GEDGS--VKIADFGvsASLAT-------GGDRTRKVRKtfvGTPCWMAPEVM 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHSGpsavidY-SKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQlPEMPESVPPEA-----RRLVRSLLQRE 492
Cdd:cd06610  179 EQVRG------YdFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDP-PSLETGADYKKysksfRKMISLCLQKD 251

                 ....*..
gi 126215545 493 ASKRPSA 499
Cdd:cd06610  252 PSKRPTA 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
311-499 1.16e-11

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: 65.25  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVM------------KNYPcTLRQYLEEQTPSSrlatmMTLQLLEGVDH-----LVQQGIAHRDLKSDNILVewDS 373
Cdd:cd08217   74 TTLYIVMeyceggdlaqliKKCK-KENQYIPEEFIWK-----IFTQLLLALYEchnrsVGGGKILHRDLKPANIFL--DS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 374 DGCPWLviSDFGCC--LADQHVglrlpFNSSSVergGNGSLMAPEVSTAHSgpsavidYS-KADTWAVGAIAYEIFGLAN 450
Cdd:cd08217  146 DNNVKL--GDFGLArvLSHDSS-----FAKTYV---GTPYYMSPELLNEQS-------YDeKSDIWSLGCLIYELCALHP 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 126215545 451 PFYGQGSAHLESRsYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd08217  209 PFQAANQLELAKK-IKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSV 256
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
344-500 1.18e-11

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: 65.47  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGccLADQH----VGLRLPFNSS-SVERGGNGSL------ 412
Cdd:cd14046  112 QILEGLAYIHSQGIIHRDLKPVNIFL----DSNGNVKIGDFG--LATSNklnvELATQDINKStSAALGSSGDLtgnvgt 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 ---MAPEVStahSGPSAVIDySKADTWAVGAIAYEifgLANPFygqgsahleSRSYQEAQL------------PEMPESV 477
Cdd:cd14046  186 alyVAPEVQ---SGTKSTYN-EKVDMYSLGIIFFE---MCYPF---------STGMERVQIltalrsvsiefpPDFDDNK 249
                        170       180
                 ....*....|....*....|...
gi 126215545 478 PPEARRLVRSLLQREASKRPSAR 500
Cdd:cd14046  250 HSKQAKLIRWLLNHDPAKRPSAQ 272
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
309-503 1.26e-11

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 65.54  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 309 HGRT-LFLVMKNYP-CTLRQYLEEQTPSSRLATMMTLQLLEGVDHL---------VQQGIAHRDLKSDNILVEwdsdgcp 377
Cdd:cd13998   63 ALRTeLWLVTAFHPnGSL*DYLSLHTIDWVSLCRLALSVARGLAHLhseipgctqGKPAIAHRDLKSKNILVK------- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 378 wlviSDFGCCLADqhVGLRLPFNSSSVE-------RGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEIFGLAN 450
Cdd:cd13998  136 ----NDGTCCIAD--FGLAVRLSPSTGEednanngQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCT 209
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 451 -----------PFYGQGSAHLESRSYQEA-----QLPEMPES-VPPEARRLVRSLLQREASKRPSARLAA 503
Cdd:cd13998  210 dlfgiveeykpPFYSEVPNHPSFEDMQEVvvrdkQRPNIPNRwLSHPGLQSLAETIEECWDHDAEARLTA 279
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
265-448 1.41e-11

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: 65.37  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIR----VFRAFTSSVPLLPGALadypDMlpphyypeglghgrTLFLVMKNYpctlRQYLEEQtpssRLATM 340
Cdd:cd07831   52 RRLSPHPNILRlievLFDRKTGRLALVFELM----DM--------------NLYELIKGR----KRPLPEK----RVKNY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTlQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwLVISDFGCCLAdqhVGLRLPFN---SSSVERggngslmAPE- 416
Cdd:cd07831  106 MY-QLLKSLDHMHRNGIFHRDIKPENILIKDDI-----LKLADFGSCRG---IYSKPPYTeyiSTRWYR-------APEc 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 126215545 417 -VSTAHSGPsavidysKADTWAVGAIAYEIFGL 448
Cdd:cd07831  170 lLTDGYYGP-------KMDIWAVGCVFFEILSL 195
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
344-499 2.56e-11

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: 64.34  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCpWLVISDFGcclADQHVGlrlpfNSSSVE-RGGNGSLMAPEVsTAHS 422
Cdd:cd14084  119 QMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEC-LIKITDFG---LSKILG-----ETSLMKtLCGTPTYLAPEV-LRSF 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPSAvidYSKA-DTWAVGAIAYEIFGLANPF---YGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14084  189 GTEG---YTRAvDCWSLGVILFICLSGYPPFseeYTQMSLKEQILSGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPS 265

                 .
gi 126215545 499 A 499
Cdd:cd14084  266 I 266
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
311-496 3.25e-11

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: 63.78  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKnYpC---TLRQYLE-EQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVISDFGc 386
Cdd:cd14009   65 DFIYLVLE-Y-CaggDLSQYIRkRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLS-TSGDDPVLKIADFG- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 387 cLAdQHvglrLPFNSSSVERGGNGSLMAPEVSTAHsgpsaviDY-SKADTWAVGAIAYE-IFGLAnPFygQGSAHLE--- 461
Cdd:cd14009  141 -FA-RS----LQPASMAETLCGSPLYMAPEILQFQ-------KYdAKADLWSVGAILFEmLVGKP-PF--RGSNHVQllr 204
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126215545 462 --SRSYQEAQLPEMPEsVPPEARRLVRSLLQREASKR 496
Cdd:cd14009  205 niERSDAVIPFPIAAQ-LSPDCKDLLRRLLRRDPAER 240
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
351-496 4.67e-11

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: 64.26  E-value: 4.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 351 HLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADqhvglrLPFNSSSVERGGNGSLMAPEVSTAHsgpsaviDY 430
Cdd:cd05575  111 YLHSLNIIYRDLKPENILL--DSQG--HVVLTDFGLCKEG------IEPSDTTSTFCGTPEYLAPEVLRKQ-------PY 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 431 SKA-DTWAVGAIAYE-IFGLAnPFYGQGSAHLESRS-YQEAQLpemPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05575  174 DRTvDWWCLGAVLYEmLYGLP-PFYSRDTAEMYDNIlHKPLRL---RTNVSPSARDLLEGLLQKDRTKR 238
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
310-499 4.86e-11

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: 63.38  E-value: 4.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMknypctlrQYLE--------EQTPS----SRLATMMtLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCp 377
Cdd:cd06614   68 GDELWVVM--------EYMDggsltdiiTQNPVrmneSQIAYVC-REVLQGLEYLHSQNVIHRDIKSDNILL--SKDGS- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 378 wLVISDFGCC--LADQHvglrlpFNSSSVErgGNGSLMAPEVSTAHsgpsaviDYS-KADTWAVGAIAYEIFGLANPfyg 454
Cdd:cd06614  136 -VKLADFGFAaqLTKEK------SKRNSVV--GTPYWMAPEVIKRK-------DYGpKVDIWSLGIMCIEMAEGEPP--- 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 126215545 455 qgsaHLESRS----YQEAQ--LPEM--PESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd06614  197 ----YLEEPPlralFLITTkgIPPLknPEKWSPEFKDFLNKCLVKDPEKRPSA 245
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
266-452 5.59e-11

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: 63.14  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSSVpllpgalADYPDMlppHYYPEGlghgrTLFLVMKNYpctlRQYLEEQTpssrLATMMTLQL 345
Cdd:cd13993   60 RVSRHPNIITLHDVFETEV-------AIYIVL---EYCPNG-----DLFEAITEN----RIYVGKTE----LIKNVFLQL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwLVISDFGccLADQhvglrlpfNSSSVERG-GNGSLMAPEVSTAHSGP 424
Cdd:cd13993  117 IDAVKHCHSLGIYHRDIKPENILLSQDEGT---VKLCDFG--LATT--------EKISMDFGvGSEFYMAPECFDEVGRS 183
                        170       180
                 ....*....|....*....|....*...
gi 126215545 425 SAVIDYSKADTWAVGAIAYEIFGLANPF 452
Cdd:cd13993  184 LKGYPCAAGDIWSLGIILLNLTFGRNPW 211
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
342-499 6.29e-11

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: 63.14  E-value: 6.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVglRLPFNSSSVErgGNGSLMAPEVSTAH 421
Cdd:cd06625  108 TRQILEGLAYLHSNMIVHRDIKGANILR--DSNGN--VKLGDFGASKRLQTI--CSSTGMKSVT--GTPYWMSPEVINGE 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 sgpsaviDYS-KADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQlPEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd06625  180 -------GYGrKADIWSVGCTVVEMLTTKPPWAEfEPMAAIFKIATQPTN-PQLPPHVSEDARDFLSLIFVRNKKQRPSA 251
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
262-496 6.70e-11

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: 63.25  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 262 DGPK---------QLAPHPNIIRVFRAFTSSVpLLPGALADYPDMLPPHYYPEGlghGRTLFLVMKNYPCTLRQyleeqt 332
Cdd:cd14171   41 DRPKartevrlhmMCSGHPNIVQIYDVYANSV-QFPGESSPRARLLIVMELMEG---GELFDRISQHRHFTEKQ------ 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 333 pssrlATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGCCLADqhvglrlpfnsssverggNGSL 412
Cdd:cd14171  111 -----AAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAP-IKLCDFGFAKVD------------------QGDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 M---------APEVSTAH-------SG---PSAVIDYSKA-DTWAVGAIAYEIFGLANPFYGQG-SAHLESRSYQ----- 466
Cdd:cd14171  167 MtpqftpyyvAPQVLEAQrrhrkerSGiptSPTPYTYDKScDMWSLGVIIYIMLCGYPPFYSEHpSRTITKDMKRkimtg 246
                        250       260       270
                 ....*....|....*....|....*....|.
gi 126215545 467 EAQLPEMP-ESVPPEARRLVRSLLQREASKR 496
Cdd:cd14171  247 SYEFPEEEwSQISEMAKDIVRKLLCVDPEER 277
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
313-516 7.28e-11

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: 63.06  E-value: 7.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYPCTLRQYLEEQTPS---SRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGccLA 389
Cdd:cd07838   81 LTLVFEHVDQDLATYLDKCPKPglpPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILV--TSDG--QVKLADFG--LA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 390 DQHvGLRLPFNSSSVE---RggngslmAPEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHlesrsyq 466
Cdd:cd07838  155 RIY-SFEMALTSVVVTlwyR-------APEVLLQSSYATPV------DMWSVGCIFAELFNRRPLFRGSSEAD------- 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 126215545 467 eaQLPEMPE--SVPPEARRLVRSLLQREA-SKRPSARLAANVLHLSLWGEHLL 516
Cdd:cd07838  214 --QLGKIFDviGLPSEEEWPRNSALPRSSfPSYTPRPFKSFVPEIDEEGLDLL 264
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
270-504 9.06e-11

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: 62.39  E-value: 9.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSsvpllpgaladypdmlPPHYY-PEGLGHGRTLF--LVMKNypctlrQYLEeqtpssRLATMMTLQLL 346
Cdd:cd14083   60 HPNIVQLLDIYES----------------KSHLYlVMELVTGGELFdrIVEKG------SYTE------KDASHLIRQVL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVeWDSDGCPWLVISDFGCcladqhvglrlpfnsSSVERGGNGS-------LMAPEVst 419
Cdd:cd14083  112 EAVDYLHSLGIVHRDLKPENLLY-YSPDEDSKIMISDFGL---------------SKMEDSGVMStacgtpgYVAPEV-- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 ahsgpSAVIDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLES---RSYQEAQLP---EMPESvppeARRLVRSLLQRE 492
Cdd:cd14083  174 -----LAQKPYGKAvDCWSIGVISYILLCGYPPFYDENDSKLFAqilKAEYEFDSPywdDISDS----AKDFIRHLMEKD 244
                        250
                 ....*....|..
gi 126215545 493 ASKRPSARLAAN 504
Cdd:cd14083  245 PNKRYTCEQALE 256
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
344-496 1.59e-10

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: 62.42  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqhvglrlpfnSSSVERG-------GNGSLMAPE 416
Cdd:cd05584  108 EITLALGHLHSLGIIYRDLKPENILL--DAQG--HVKLTDFGLC-------------KESIHDGtvthtfcGTIEYMAPE 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGqgsahlESRSYQ-----EAQLpEMPESVPPEARRLVRSLLQR 491
Cdd:cd05584  171 ILTRSGHGKAV------DWWSLGALMYDMLTGAPPFTA------ENRKKTidkilKGKL-NLPPYLTNEARDLLKKLLKR 237

                 ....*
gi 126215545 492 EASKR 496
Cdd:cd05584  238 NVSSR 242
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
312-496 1.70e-10

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: 61.95  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 312 TLFLVMKNypCT---LRQYLEEQTPSSRLATMMTLQLLEGVDHLVQ-QGIAHRDLKSDNILVEWDS--DGCP---WLVIS 382
Cdd:cd14202   75 SVYLVMEY--CNggdLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHsKGIIHRDLKPQNILLSYSGgrKSNPnniRIKIA 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 383 DFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAHsgpsaviDY-SKADTWAVGAIAYEIFGLANPFygQGSAHLE 461
Cdd:cd14202  153 DFG-------FARYLQNNMMAATLCGSPMYMAPEVIMSQ-------HYdAKADLWSIGTIIYQCLTGKAPF--QASSPQD 216
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 126215545 462 SRSYQEAQ---LPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14202  217 LRLFYEKNkslSPNIPRETSSHLRQLLLGLLQRNQKDR 254
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
338-503 2.49e-10

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: 61.99  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGCcladqhvglrlpfnsSSVErgGNGSLMAPEV 417
Cdd:cd14168  110 ASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESK-IMISDFGL---------------SKME--GKGDVMSTAC 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 ST-AHSGPSAVID--YSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMP--ESVPPEARRLVRSLLQR 491
Cdd:cd14168  172 GTpGYVAPEVLAQkpYSKAvDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPywDDISDSAKDFIRNLMEK 251
                        170
                 ....*....|..
gi 126215545 492 EASKRPSARLAA 503
Cdd:cd14168  252 DPNKRYTCEQAL 263
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
324-499 2.63e-10

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: 61.50  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQ-YLEEQTPSsrlATMMTLqlLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLADQHvglrlpfnss 402
Cdd:cd14091   86 LRQkFFSEREAS---AVMKTL--TKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFG--FAKQL---------- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 403 sveRGGNGSLM---------APEVSTAHSgpsavidYSKA-DTWAVGAIAYEIFGLANPF--------------YGQGSA 458
Cdd:cd14091  149 ---RAENGLLMtpcytanfvAPEVLKKQG-------YDAAcDIWSLGVLLYTMLAGYTPFasgpndtpevilarIGSGKI 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126215545 459 HLESRSYqeaqlpempESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14091  219 DLSGGNW---------DHVSDSAKDLVRKMLHVDPSQRPTA 250
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
313-445 2.68e-10

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 61.69  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHL-----VQQG---IAHRDLKSDNILVEWDSDGCpwlvISD 383
Cdd:cd14142   78 LWLITHYHENgSLYDYLQRTTLDHQEMLRLALSAASGLVHLhteifGTQGkpaIAHRDLKSKNILVKSNGQCC----IAD 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 384 FGccLADQHVGLRLPFNSSSVERGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEI 445
Cdd:cd14142  154 LG--LAVTHSQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEV 213
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
325-499 2.91e-10

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: 61.58  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 325 RQYLEEqtpssRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFgcclaDQHVGLRL-----PF 399
Cdd:cd14174   94 RKHFNE-----REASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSP-VKICDF-----DLGSGVKLnsactPI 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 400 NSSSVERG-GNGSLMAPEVSTAHSGPSAVIDySKADTWAVGAIAYEIFGLANPFYGQ-----GSAHLES---------RS 464
Cdd:cd14174  163 TTPELTTPcGSAEYMAPEVVEVFTDEATFYD-KRCDLWSLGVILYIMLSGYPPFVGHcgtdcGWDRGEVcrvcqnklfES 241
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126215545 465 YQEAQLpEMPES----VPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14174  242 IQEGKY-EFPDKdwshISSEAKDLISKLLVRDAKERLSA 279
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
309-498 2.95e-10

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: 61.24  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 309 HGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMM--TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDsdgcpWLV-ISDF 384
Cdd:cd05038   79 GRRSLRLIMEYLPSgSLRDYLQRHRDQIDLKRLLlfASQICKGMEYLGSQRYIHRDLAARNILVESE-----DLVkISDF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GccLAdqhvglRLPFNSSSVERGGN-GSL----MAPE-VSTAhsgpsavIDYSKADTWAVGAIAYEIFGLANPFY----- 453
Cdd:cd05038  154 G--LA------KVLPEDKEYYYVKEpGESpifwYAPEcLRES-------RFSSASDVWSFGVTLYELFTYGDPSQsppal 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 126215545 454 ---GQGSAHLESRSYQEAQLPE------MPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05038  219 flrMIGIAQGQMIVTRLLELLKsgerlpRPPSCPDEVYDLMKECWEYEPQDRPS 272
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
270-385 3.12e-10

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: 61.36  E-value: 3.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLlpgaladypdmlPPHYYpeglghgrtLFLVMKNYPCTLRQYL-----EEQTPSSRLATMMTLQ 344
Cdd:cd14137   56 HPNIVKLKYFFYSSGEK------------KDEVY---------LNLVMEYMPETLYRVIrhyskNKQTIPIIYVKLYSYQ 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCpwLVISDFG 385
Cdd:cd14137  115 LFRGLAYLHSLGICHRDIKPQNLLVD-PETGV--LKLCDFG 152
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
342-500 3.14e-10

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 61.04  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwlVISDFGCcladqhvglrlpfnsSSVERGGNGSLMAPEVSTAh 421
Cdd:cd05083  106 SLDVAEGMEYLESKKLVHRDLAARNILVSEDGVA----KISDFGL---------------AKVGSMGVDNSRLPVKWTA- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 sgPSAVIDY---SKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05083  166 --PEALKNKkfsSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPS 243

                 ..
gi 126215545 499 AR 500
Cdd:cd05083  244 FK 245
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
328-496 3.28e-10

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: 61.06  E-value: 3.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 328 LEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEW---DSDgcpwLVISDFGCcladqhvglrlpfnsSSV 404
Cdd:cd14169   93 IERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSK----IMISDFGL---------------SKI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 ERGGngslmapEVSTAHSGPSAVI-------DYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMP-- 474
Cdd:cd14169  154 EAQG-------MLSTACGTPGYVApelleqkPYGKAvDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPyw 226
                        170       180
                 ....*....|....*....|..
gi 126215545 475 ESVPPEARRLVRSLLQREASKR 496
Cdd:cd14169  227 DDISESAKDFIRHLLERDPEKR 248
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
344-502 3.51e-10

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: 61.28  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGCCL-ADQHVGLRLPFnsssverGGNGSLMAPEVSTAHS 422
Cdd:cd14086  108 QILESVNHCHQNGIVHRDLKPENLLLASKSKGAA-VKLADFGLAIeVQGDQQAWFGF-------AGTPGYLSPEVLRKDP 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 gpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPE--SVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14086  180 -------YGKPvDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEwdTVTPEAKDLINQMLTVNPAKRITA 252

                 ...
gi 126215545 500 RLA 502
Cdd:cd14086  253 AEA 255
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
344-499 3.69e-10

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: 60.67  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDS--DgcpwLVISDFGCCladQHV-GLRLPFNsssveRGGNGSLMAPEVstA 420
Cdd:cd14107  106 QVLEGIGYLHGMNILHLDIKPDNILMVSPTreD----IKICDFGFA---QEItPSEHQFS-----KYGSPEFVAPEI--V 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAH-----LESRSYQEAqlPEMpESVPPEARRLVRSLLQREAS 494
Cdd:cd14107  172 HQEP-----VSAAtDIWALGVIAYLSLTCHSPFAGENDRAtllnvAEGVVSWDT--PEI-THLSEDAKDFIKRVLQPDPE 243

                 ....*
gi 126215545 495 KRPSA 499
Cdd:cd14107  244 KRPSA 248
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
344-503 4.36e-10

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: 61.26  E-value: 4.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCL-ADQHVGLRLPFnSSSVErggngsLMAPEVSTAHS 422
Cdd:cd05582  105 ELALALDHLHSLGIIYRDLKPENILL--DEDG--HIKLTDFGLSKeSIDHEKKAYSF-CGTVE------YMAPEVVNRRG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPSAvidyskADTWAVGAIAYEIFGLANPFYGQgsahleSRSYQEAQLPE----MPESVPPEARRLVRSLLQREaskrPS 498
Cdd:cd05582  174 HTQS------ADWWSFGVLMFEMLTGSLPFQGK------DRKETMTMILKaklgMPQFLSPEAQSLLRALFKRN----PA 237

                 ....*
gi 126215545 499 ARLAA 503
Cdd:cd05582  238 NRLGA 242
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
310-511 4.87e-10

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: 60.57  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccL 388
Cdd:cd06917   74 GPSLWIIMDYCEGgSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN----VKLCDFG--V 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQhvglrlpFNSSSVERG---GNGSLMAPEVSTahSGPSavIDYsKADTWAVGAIAYEIfGLANPFYGQGSAHLESRSY 465
Cdd:cd06917  148 AAS-------LNQNSSKRStfvGTPYWMAPEVIT--EGKY--YDT-KADIWSLGITTYEM-ATGNPPYSDVDALRAVMLI 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 126215545 466 QEAQLPEMP-ESVPPEARRLVRSLLQREaskrPSARLAANVLHLSLW 511
Cdd:cd06917  215 PKSKPPRLEgNGYSPLLKEFVAACLDEE----PKDRLSADELLKSKW 257
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
344-496 6.53e-10

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: 60.79  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqhvglRLPFNSSSVERG--GNGSLMAPEVSTAH 421
Cdd:cd05595  103 EIVSALEYLHSRDVVYRDIKLENLML--DKDG--HIKITDFGLC--------KEGITDGATMKTfcGTPEYLAPEVLEDN 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 422 sgpsaviDYSKA-DTWAVGAIAYEIFGLANPFYGQGsahlESRSYQEAQLPEM--PESVPPEARRLVRSLLQREASKR 496
Cdd:cd05595  171 -------DYGRAvDWWGLGVVMYEMMCGRLPFYNQD----HERLFELILMEEIrfPRTLSPEAKSLLAGLLKKDPKQR 237
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
265-499 7.85e-10

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: 59.81  E-value: 7.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLA--PHPNIIRVFRAFTssvpllpgalaDYPDMLPPHYYPEGLGHGRTLFLVMKNypC---TLRQYLEEQTPSSR--- 336
Cdd:cd14047   51 KALAklDHPNIVRYNGCWD-----------GFDYDPETSSSNSSRSKTKCLFIQMEF--CekgTLESWIEKRNGEKLdkv 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 337 LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQHVGLRlpfnsssVERGGNGSLMAPE 416
Cdd:cd14047  118 LALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK----VKIGDFGLVTSLKNDGKR-------TKSKGTLSYMSPE 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VSTAHsgpsaviDY-SKADTWAVGAIAYEIfglanpFYGQGSAHLESRSYQE---AQLPEMPESVPPEARRLVRSLLQRE 492
Cdd:cd14047  187 QISSQ-------DYgKEVDIYALGLILFEL------LHVCDSAFEKSKFWTDlrnGILPDIFDKRYKIEKTIIKKMLSKK 253

                 ....*..
gi 126215545 493 ASKRPSA 499
Cdd:cd14047  254 PEDRPNA 260
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
306-445 7.85e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 60.18  E-value: 7.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 306 GLGHGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHL-----VQQG---IAHRDLKSDNILVEwdsdgc 376
Cdd:cd14144   61 GTGSWTQLYLITDYHENgSLYDFLRGNTLDTQSMLKLAYSAACGLAHLhteifGTQGkpaIAHRDIKSKNILVK------ 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 377 pwlviSDFGCCLADqhVGLRLPFNSSSVE-------RGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEI 445
Cdd:cd14144  135 -----KNGTCCIAD--LGLAVKFISETNEvdlppntRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEI 203
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
324-500 8.34e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 61.42  E-value: 8.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRL-----ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwLV-ISDFGCCladqhvglRL 397
Cdd:PTZ00283 126 LRQEIKSRAKTNRTfreheAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL--CSNG---LVkLGDFGFS--------KM 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 398 PFNSSSVERG----GNGSLMAPEVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQeAQLPE 472
Cdd:PTZ00283 193 YAATVSDDVGrtfcGTPYYVAPEIWRRKP-------YSKkADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLA-GRYDP 264
                        170       180
                 ....*....|....*....|....*...
gi 126215545 473 MPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:PTZ00283 265 LPPSISPEMQEIVTALLSSDPKRRPSSS 292
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
338-504 9.21e-10

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: 60.28  E-value: 9.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladqhvGLRLPFNSSSVERGGNGSLMAPEV 417
Cdd:cd05585   96 ARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH----IALCDFGLC------KLNMKDDDKTNTFCGTPEYLAPEL 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSgpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLpeMPESVPPEARRLVRSLLQREaskr 496
Cdd:cd05585  166 LLGHG-------YTKAvDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLR--FPDGFDRDAKDLLIGLLNRD---- 232

                 ....*...
gi 126215545 497 PSARLAAN 504
Cdd:cd05585  233 PTKRLGYN 240
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
329-496 9.39e-10

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: 59.65  E-value: 9.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccladqhVGLRLPFNSSSVERGG 408
Cdd:cd14194  101 EKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFG-------LAHKIDFGNEFKNIFG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 NGSLMAPEvstahsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAQlpEMPESVPPE 480
Cdd:cd14194  174 TPEFVAPE----------IVNYEplglEADMWSIGVITYILLSGASPFLGDTKqetlANVSAVNYEFED--EYFSNTSAL 241
                        170
                 ....*....|....*.
gi 126215545 481 ARRLVRSLLQREASKR 496
Cdd:cd14194  242 AKDFIRRLLVKDPKKR 257
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
344-441 1.13e-09

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: 59.27  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVG-LRLpfnssSVERGGNGSLMAPEV--STA 420
Cdd:cd14069  108 QLMAGLKYLHSCGITHRDIKPENLLL--DENDN--LKISDFGLATVFRYKGkERL-----LNKMCGTLPYVAPELlaKKK 178
                         90       100
                 ....*....|....*....|.
gi 126215545 421 HSGPsavidysKADTWAVGAI 441
Cdd:cd14069  179 YRAE-------PVDVWSCGIV 192
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
270-445 1.13e-09

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: 60.18  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLLPGALADypdmlpphyypegLGHGRTLFLVMKNYPCTLRQYLEEQTPSSRLATMMTLQLLEGV 349
Cdd:cd07854   61 HDNIVKVYEVLGPSGSDLTEDVGS-------------LTELNSVYIVQEYMETDLANVLEQGPLSEEHARLFMYQLLRGL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSdgcPWLVISDFGCC-LADQHVGLRlpfnsssverggnGSLMAPEVSTAHSGPSAVI 428
Cdd:cd07854  128 KYIHSANVLHRDLKPANVFINTED---LVLKIGDFGLArIVDPHYSHK-------------GYLSEGLVTKWYRSPRLLL 191
                        170       180
                 ....*....|....*....|.
gi 126215545 429 ---DYSKA-DTWAVGAIAYEI 445
Cdd:cd07854  192 spnNYTKAiDMWAAGCIFAEM 212
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
344-496 1.18e-09

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: 59.19  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCcladqhvglrlpfnsSSVERGGN------GSL--MAP 415
Cdd:cd14081  109 QIISALDYCHSHSICHRDLKPENLLL--DEKNN--IKIADFGM---------------ASLQPEGSlletscGSPhyACP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAHSgpsavIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAqlPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd14081  170 EVIKGEK-----YDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGV--FHIPHFISPDAQDLLRRMLEVNPEK 242

                 .
gi 126215545 496 R 496
Cdd:cd14081  243 R 243
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
313-496 1.34e-09

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: 59.63  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYP-----CTLRQYlEEQTPSSrLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFG-- 385
Cdd:cd05601   76 LYLVMEYHPggdllSLLSRY-DDIFEES-MARFYLAELVLAIHSLHSMGYVHRDIKPENILI----DRTGHIKLADFGsa 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 CCL-ADQHVGLRLPFnsssvergGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYE-IFGlANPFYGQGSAHLESR 463
Cdd:cd05601  150 AKLsSDKTVTSKMPV--------GTPDYIAPEVLTSMNGGSKGTYGVECDWWSLGIVAYEmLYG-KTPFTEDTVIKTYSN 220
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 126215545 464 --SYQEA-QLPEMPeSVPPEARRLVRSLLQrEASKR 496
Cdd:cd05601  221 imNFKKFlKFPEDP-KVSESAVDLIKGLLT-DAKER 254
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
338-500 1.63e-09

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: 59.65  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADqhvglrLPFNSSSVERGGNGSLMAPEV 417
Cdd:cd05602  110 ARFYAAEIASALGYLHSLNIVYRDLKPENILL--DSQG--HIVLTDFGLCKEN------IEPNGTTSTFCGTPEYLAPEV 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stAHSGPsavidYSKA-DTWAVGAIAYE-IFGLAnPFYGQGSAHLESRSYQEAQlpEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd05602  180 --LHKQP-----YDRTvDWWCLGAVLYEmLYGLP-PFYSRNTAEMYDNILNKPL--QLKPNITNSARHLLEGLLQKDRTK 249

                 ....*
gi 126215545 496 RPSAR 500
Cdd:cd05602  250 RLGAK 254
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
270-445 1.72e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 59.35  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpGALADYPDmlpphyypeglghgrtLFLVMKNYPCTLRQYLEEQTPSSRLATMMtLQLLEGV 349
Cdd:cd07850   58 HKNIIGLLNVFTPQ-----KSLEEFQD----------------VYLVMELMDANLCQVIQMDLDHERMSYLL-YQMLCGI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDsdgCPwLVISDFGccLAdqhvglrlpfnsssvERGGNGSLMAPEVSTAHSGPSAVI- 428
Cdd:cd07850  116 KHLHSAGIIHRDLKPSNIVVKSD---CT-LKILDFG--LA---------------RTAGTSFMMTPYVVTRYYRAPEVIl 174
                        170       180
                 ....*....|....*....|
gi 126215545 429 --DYS-KADTWAVGAIAYEI 445
Cdd:cd07850  175 gmGYKeNVDIWSVGCIMGEM 194
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
348-532 2.62e-09

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: 58.50  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAHSgpsav 427
Cdd:cd05630  114 GLEDLHRERIVYRDLKPENILL--DDHG--HIRISDLG-------LAVHVPEGQTIKGRVGTVGYMAPEVVKNER----- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 428 idYS-KADTWAVGAIAYEIFGLANPFygQGSAHLESRSYQEAQLPEMPES----VPPEARRLVRSLLqreaSKRPSARLA 502
Cdd:cd05630  178 --YTfSPDWWALGCLLYEMIAGQSPF--QQRKKKIKREEVERLVKEVPEEysekFSPQARSLCSMLL----CKDPAERLG 249
                        170       180       190
                 ....*....|....*....|....*....|
gi 126215545 503 ANVLHLSLWGEHLLaLKNLKLDKMIAWLLQ 532
Cdd:cd05630  250 CRGGGAREVKEHPL-FKKLNFKRLGAGMLE 278
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
313-504 2.70e-09

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: 58.90  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMkNYPC-----TLRQYLEEQTPSSrLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGCC 387
Cdd:cd05597   76 LYLVM-DYYCggdllTLLSKFEDRLPEE-MARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL----DRNGHIRLADFGSC 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 388 L---ADQHVglrlpFNSSSVergGNGSLMAPEVSTAHSGPSAVidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESR 463
Cdd:cd05597  150 LklrEDGTV-----QSSVAV---GTPDYISPEILQAMEDGKGR--YGPeCDWWSLGVCMYEMLYGETPFYAESLVETYGK 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 126215545 464 --SYQEA-QLPEMPESVPPEARRLVRSLLQreaskRPSARLAAN 504
Cdd:cd05597  220 imNHKEHfSFPDDEDDVSEEAKDLIRRLIC-----SRERRLGQN 258
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
329-504 2.79e-09

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: 58.04  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCcladqhvglrlpfnSSSVERG- 407
Cdd:cd14196  101 QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGL--------------AHEIEDGv 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 408 ------GNGSLMAPEvstahsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAQlpEM 473
Cdd:cd14196  167 efknifGTPEFVAPE----------IVNYEplglEADMWSIGVITYILLSGASPFLGDTKqetlANITAVSYDFDE--EF 234
                        170       180       190
                 ....*....|....*....|....*....|.
gi 126215545 474 PESVPPEARRLVRSLLQREASKRPSARLAAN 504
Cdd:cd14196  235 FSHTSELAKDFIRKLLVKETRKRLTIQEALR 265
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
342-500 3.30e-09

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: 57.50  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladqhvgLRLPFNSSSVERGGNGSLMAPEVstAH 421
Cdd:cd14059   87 SKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV----LKISDFGTS-------KELSEKSTKMSFAGTVAWMAPEV--IR 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGPSAvidySKADTWAVGAIAYEIFGLANPF---------YGQGSAHLesrsyqeaQLPeMPESVPPEARRLVRSLLQRE 492
Cdd:cd14059  154 NEPCS----EKVDIWSFGVVLWELLTGEIPYkdvdssaiiWGVGSNSL--------QLP-VPSTCPDGFKLLMKQCWNSK 220

                 ....*...
gi 126215545 493 ASKRPSAR 500
Cdd:cd14059  221 PRNRPSFR 228
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
313-505 3.59e-09

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: 57.88  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYP---C-TLRQ---YLEEQTPSSRLAtmmtlQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFG 385
Cdd:cd05611   72 LYLVMEYLNggdCaSLIKtlgGLPEDWAKQYIA-----EVVLGVEDLHQRGIIHRDIKPENLLI--DQTG--HLKLTDFG 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 CcladQHVGLrlpFNSSSVERGGNGSLMAPEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGS----AHLE 461
Cdd:cd05611  143 L----SRNGL---EKRHNKKFVGTPDYLAPETILGVGDDKMS------DWWSLGCVIFEFLFGYPPFHAETPdavfDNIL 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 126215545 462 SRSYQEAQlpEMPESVPPEARRLVRSLLQREaskrPSARLAANV 505
Cdd:cd05611  210 SRRINWPE--EVKEFCSPEAVDLINRLLCMD----PAKRLGANG 247
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
327-509 3.78e-09

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: 58.10  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 327 YLEEQ-TPSSRLATMMTLQLLEGVDHL--VQQGIAHRDLKSDNIL-VEWDSDGCpwLVISDFGCC-LADQHVGlrlpfNS 401
Cdd:cd13990   95 YLKQHkSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILlHSGNVSGE--IKITDFGLSkIMDDESY-----NS 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVE--RGGNGSL--MAPEvsTAHSGPSAVIDYSKADTWAVGAIAYEIFGLANPFyGQGS---AHLESRSYQEAQLPEMP 474
Cdd:cd13990  168 DGMEltSQGAGTYwyLPPE--CFVVGKTPPKISSKVDVWSVGVIFYQMLYGRKPF-GHNQsqeAILEENTILKATEVEFP 244
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126215545 475 E--SVPPEARRLVRSLLQREASKRPsarlaaNVLHLS 509
Cdd:cd13990  245 SkpVVSSEAKDFIRRCLTYRKEDRP------DVLQLA 275
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
270-503 4.00e-09

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: 57.56  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghGRTLFLVMKNYPCTLRQYLEE-QTPSSRLATMMTLQLLEG 348
Cdd:cd14164   59 HPNIVQMFECIEVA--------------------------NGRLYIVMEAAATDLLQKIQEvHHIPKDLARDMFAQMVGA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVEWDSDGcpwLVISDFGccLADQHVGlrlpFNSSSVERGGNGSLMAPEVSTAHSgpsavI 428
Cdd:cd14164  113 VNYLHDMNIVHRDLKCENILLSADDRK---IKIADFG--FARFVED----YPELSTTFCGSRAYTPPEVILGTP-----Y 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 429 DYSKADTWAVGAIAYEIFGLANPFYGQGSAHLesRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSARLAA 503
Cdd:cd14164  179 DPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRGVLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQVA 251
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
311-511 4.36e-09

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: 57.56  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKnyPCT---LRQYLEEQTPSSRLATMMTLQ-LLEGVDHLVQQGIAHRDLKSDNILVE-WDSDGCPWLVI--SD 383
Cdd:cd14097   73 KRMYLVME--LCEdgeLKELLLRKGFFSENETRHIIQsLASAVAYLHKNDIVHRDLKLENILVKsSIIDNNDKLNIkvTD 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 384 FGCCLADQHVGLRLPFNSSsvergGNGSLMAPEVSTAHsgpsaviDYSK-ADTWAVGAIAYEIFGLANPFYGQGsahlES 462
Cdd:cd14097  151 FGLSVQKYGLGEDMLQETC-----GTPIYMAPEVISAH-------GYSQqCDIWSIGVIMYMLLCGEPPFVAKS----EE 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 463 RSYQEAQLPEMP------ESVPPEARRLVRSLLQREaskrPSARLAANVLHLSLW 511
Cdd:cd14097  215 KLFEEIRKGDLTftqsvwQSVSDAAKNVLQQLLKVD----PAHRMTASELLDNPW 265
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
337-496 4.36e-09

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: 58.10  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 337 LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqhVGLRLPFNS------SSVergGNG 410
Cdd:cd05598  102 LARFYIAELVCAIESVHKMGFIHRDIKPDNILI--DRDG--HIKLTDFGLC-----TGFRWTHDSkyylahSLV---GTP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 411 SLMAPEVstahsgpSAVIDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRS---YQEAQLPEMPEsVPPEARRLVR 486
Cdd:cd05598  170 NYIAPEV-------LLRTGYTQLcDWWSVGVILYEMLVGQPPFLAQTPAETQLKVinwRTTLKIPHEAN-LSPEAKDLIL 241
                        170
                 ....*....|
gi 126215545 487 SLLqREASKR 496
Cdd:cd05598  242 RLC-CDAEDR 250
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
328-496 4.58e-09

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: 57.97  E-value: 4.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 328 LEEQTP--SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLAdqhVGLRlpfNSSSVE 405
Cdd:cd05608   95 VDEENPgfQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL--DDDGN--VRISDLG--LA---VELK---DGQTKT 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 406 RG--GNGSLMAPEVSTAHSgpsavIDYSkADTWAVGAIAYEIFGLANPFYGQGSaHLESRSYQEAQLPE---MPESVPPE 480
Cdd:cd05608  163 KGyaGTPGFMAPELLLGEE-----YDYS-VDYFTLGVTLYEMIAARGPFRARGE-KVENKELKQRILNDsvtYSEKFSPA 235
                        170
                 ....*....|....*.
gi 126215545 481 ARRLVRSLLQREASKR 496
Cdd:cd05608  236 SKSICEALLAKDPEKR 251
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
338-500 4.80e-09

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: 58.01  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCClADQHVGlrlpfNSSSVERGGNGSLMAPEV 417
Cdd:cd05619  108 ATFYAAEIICGLQFLHSKGIVYRDLKLDNILL--DKDG--HIKIADFGMC-KENMLG-----DAKTSTFCGTPDYIAPEI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLesrsYQEAQL--PEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd05619  178 LLGQKYNTSV------DWWSFGVLLYEMLIGQSPFHGQDEEEL----FQSIRMdnPFYPRWLEKEAKDILVKLFVREPER 247

                 ....*
gi 126215545 496 RPSAR 500
Cdd:cd05619  248 RLGVR 252
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
324-441 4.96e-09

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: 57.95  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVISDFGCCLADQHVGLRlPFNSSS 403
Cdd:cd13977  122 MNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILIS-HKRGEPILKVADFGLSKVCSGSGLN-PEEPAN 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 126215545 404 VERG------GNGSLMAPEVSTAHSGpsavidySKADTWAVGAI 441
Cdd:cd13977  200 VNKHflssacGSDFYMAPEVWEGHYT-------AKADIFALGII 236
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
344-499 5.36e-09

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: 57.24  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNIL-VEWDSDgcpWLVISDFGccLADQHVG---LRLPFnsssvergGNGSLMAPEvst 419
Cdd:cd14103   99 QICEGVQYMHKQGILHLDLKPENILcVSRTGN---QIKIIDFG--LARKYDPdkkLKVLF--------GTPEFVAPE--- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 ahsgpsaVIDY----SKADTWAVGAIAYEIF-GLAnPFygQGSAHLESRS--------YQEaqlpEMPESVPPEARRLVR 486
Cdd:cd14103  163 -------VVNYepisYATDMWSVGVICYVLLsGLS-PF--MGDNDAETLAnvtrakwdFDD----EAFDDISDEAKDFIS 228
                        170
                 ....*....|...
gi 126215545 487 SLLQREASKRPSA 499
Cdd:cd14103  229 KLLVKDPRKRMSA 241
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
338-500 6.09e-09

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: 56.88  E-value: 6.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLADQHVGlrlPFNSSSvergGNGSLMAPEV 417
Cdd:cd14185  100 AALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFG--LAKYVTG---PIFTVC----GTPTYVAPEI 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 sTAHSGpsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLEsrSYQEAQLPEMpESVPP-------EARRLVRSLL 489
Cdd:cd14185  171 -LSEKG------YGlEVDMWAAGVILYILLCGFPPFRSPERDQEE--LFQIIQLGHY-EFLPPywdniseAAKDLISRLL 240
                        170
                 ....*....|.
gi 126215545 490 QREASKRPSAR 500
Cdd:cd14185  241 VVDPEKRYTAK 251
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
310-510 7.24e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 57.93  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPCTLRQYLEEQTPSSrLATMMTLQ--LLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwlVISDFG-C 386
Cdd:PHA03207 158 KSTVCMVMPKYKCDLFTYVDRSGPLP-LEQAITIQrrLLEALAYLHGRGIIHRDVKTENIFLDEPENA----VLGDFGaA 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 387 CLADQHVglrlpfnSSSVERGGNGSLM--APEVstahsgpSAVIDY-SKADTWAVGAIAYE-------IFGLANP----- 451
Cdd:PHA03207 233 CKLDAHP-------DTPQCYGWSGTLEtnSPEL-------LALDPYcAKTDIWSAGLVLFEmsvknvtLFGKQVKssssq 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 452 --------------FYGQGSAHLESRSYQEAQLPEMPESVPPEARR---------LVRSLLQREASKRPSARlaaNVLHL 508
Cdd:PHA03207 299 lrsiircmqvhpleFPQNGSTNLCKHFKQYAIVLRPPYTIPPVIRKygmhmdveyLIAKMLTFDQEFRPSAQ---DILSL 375

                 ..
gi 126215545 509 SL 510
Cdd:PHA03207 376 PL 377
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
270-502 7.71e-09

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: 56.49  E-value: 7.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghgRTLFLVMKNYPCTLRQYLE-EQTPSSRLATMMTLQLLEG 348
Cdd:cd14002   59 HPNIIEMLDSFETK---------------------------KEFVVVTEYAQGELFQILEdDGTLPEEEVRSIAKQLVSA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLAdqhvglrLPFNS---SSVErgGNGSLMAPEVstAHSGPs 425
Cdd:cd14002  112 LHYLHSNRIIHRDMKPQNILI--GKGGV--VKLCDFGFARA-------MSCNTlvlTSIK--GTPLYMAPEL--VQEQP- 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 426 avIDYsKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEaqlP-EMPESVPPEARRLVRSLLQreasKRPSARLA 502
Cdd:cd14002  176 --YDH-TADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKD---PvKWPSNMSPEFKSFLQGLLN----KDPSKRLS 243
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
265-505 8.04e-09

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: 56.90  E-value: 8.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLApHPNIIRVFRAFTSSVPL-LPGALADYPDMlpphyypeglghGRtlflvMKNYPCTLRQYLEEQTPSSRLatmmtL 343
Cdd:cd08224   55 QQLN-HPNIIKYLASFIENNELnIVLELADAGDL------------SR-----LIKHFKKQKRLIPERTIWKYF-----V 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwlVISdfgccLADqhVGLRLPFNSSSVERG---GNGSLMAPEVstA 420
Cdd:cd08224  112 QLCSALEHMHSKRIMHRDIKPANVFI--TANG----VVK-----LGD--LGLGRFFSSKTTAAHslvGTPYYMSPER--I 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPsavidYS-KADTWAVGAIAYEIFGLANPFYGQGS------AHLESRSYqeAQLPemPESVPPEARRLVRSLLQREA 493
Cdd:cd08224  177 REQG-----YDfKSDIWSLGCLLYEMAALQSPFYGEKMnlyslcKKIEKCEY--PPLP--ADLYSQELRDLVAACIQPDP 247
                        250
                 ....*....|..
gi 126215545 494 SKRPSARLAANV 505
Cdd:cd08224  248 EKRPDISYVLDV 259
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
350-496 8.10e-09

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: 57.25  E-value: 8.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEwdSDGcpWLVISDFG-CCLAD------------------QHVGLRLPFNSSSVERG--- 407
Cdd:cd05574  117 EYLHLLGFVYRDLKPENILLH--ESG--HIMLTDFDlSKQSSvtpppvrkslrkgsrrssVKSIEKETFVAEPSARSnsf 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 408 -GNGSLMAPEVSTAHSGPSAVidyskaDTWAVGAIAYEI-FGlANPFygQGSAHLESRS---YQEAQLPEMPEsVPPEAR 482
Cdd:cd05574  193 vGTEEYIAPEVIKGDGHGSAV------DWWTLGILLYEMlYG-TTPF--KGSNRDETFSnilKKELTFPESPP-VSSEAK 262
                        170
                 ....*....|....
gi 126215545 483 RLVRSLLQREASKR 496
Cdd:cd05574  263 DLIRKLLVKDPSKR 276
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
266-500 8.63e-09

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: 56.55  E-value: 8.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFtssvpllpgaladypdmlpphyypEGLGHgrtLFLVMKNYPCTLRQYLEEQ--TPSSRLATMMtL 343
Cdd:cd14050   56 KLGEHPNCVRFIKAW------------------------EEKGI---LYIQTELCDTSLQQYCEEThsLPESEVWNIL-L 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILvewdsdgcpwlvISDFGCC-LADQHVGLRLPFNSSSVERGGNGSLMAPEVSTAHS 422
Cdd:cd14050  108 DLLKGLKHLHDHGLIHLDIKPANIF------------LSKDGVCkLGDFGLVVELDKEDIHDAQEGDPRYMAPELLQGSF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPSavidyskADTWAVGAIAYEI-FGLANPFYGQGSAHLesrsyQEAQLP-EMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd14050  176 TKA-------ADIFSLGITILELaCNLELPSGGDGWHQL-----RQGYLPeEFTAGLSPELRSIIKLMMDPDPERRPTAE 243
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
270-498 8.78e-09

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: 56.89  E-value: 8.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLLP-------GALADYPdMLPPHYYPEGLGHGRTlflvmknypctlRQYLEEQTPSSRLATMMT 342
Cdd:cd05045   62 HPHVIKLYGACSQDGPLLLiveyakyGSLRSFL-RESRKVGPSYLGSDGN------------RNSSYLDNPDERALTMGD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 L-----QLLEGVDHLVQQGIAHRDLKSDNILVewdSDGcPWLVISDFGCCladqhvglRLPFNSSSVERGGNGSL----M 413
Cdd:cd05045  129 LisfawQISRGMQYLAEMKLVHRDLAARNVLV---AEG-RKMKISDFGLS--------RDVYEEDSYVKRSKGRIpvkwM 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVSTAHsgpsavIDYSKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRsYQEAQLPEMPESVPPEARRLVRSLLQRE 492
Cdd:cd05045  197 AIESLFDH------IYTTQSDVWSFGVLLWEIVTLgGNPYPGIAPERLFNL-LKTGYRMERPENCSEEMYNLMLTCWKQE 269

                 ....*.
gi 126215545 493 ASKRPS 498
Cdd:cd05045  270 PDKRPT 275
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
337-503 9.63e-09

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: 56.65  E-value: 9.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 337 LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGcpWLVISDFGCC----------LADQHVGLRLP-FNSSSVe 405
Cdd:cd05609  101 MARMYFAETVLALEYLHSYGIVHRDLKPDNLLIT--SMG--HIKLTDFGLSkiglmslttnLYEGHIEKDTReFLDKQV- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 406 rGGNGSLMAPEVSTAHSgpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESR-SYQEAQLPEMPESVPPEARR 483
Cdd:cd05609  176 -CGTPEYIAPEVILRQG-------YGKPvDWWAMGIILYEFLVGCVPFFGDTPEELFGQvISDEIEWPEGDDALPDDAQD 247
                        170       180
                 ....*....|....*....|
gi 126215545 484 LVRSLLQreasKRPSARLAA 503
Cdd:cd05609  248 LITRLLQ----QNPLERLGT 263
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
342-500 9.68e-09

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: 56.67  E-value: 9.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcPWLVISDFGCC--LADQHVGLRLpFNSSSVergGNGSLMAPEVST 419
Cdd:cd06630  109 TLQILRGLAYLHDNQIIHRDLKGANLLV--DSTG-QRLRIADFGAAarLASKGTGAGE-FQGQLL---GTIAFMAPEVLR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSgpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQG-SAHLE--SRSYQEAQLPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd06630  182 GEQ-------YGRScDVWSVGCVIIEMATAKPPWNAEKiSNHLAliFKIASATTPPPIPEHLSPGLRDVTLRCLELQPED 254

                 ....*
gi 126215545 496 RPSAR 500
Cdd:cd06630  255 RPPAR 259
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
356-445 1.04e-08

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 56.51  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 356 GIAHRDLKSDNILVEwdsdgcpwlviSDFGCCLADqhVGLRLPFNSSSVE-------RGGNGSLMAPEVSTAHSGPSAVI 428
Cdd:cd14056  120 AIAHRDLKSKNILVK-----------RDGTCCIAD--LGLAVRYDSDTNTidippnpRVGTKRYMAPEVLDDSINPKSFE 186
                         90
                 ....*....|....*..
gi 126215545 429 DYSKADTWAVGAIAYEI 445
Cdd:cd14056  187 SFKMADIYSFGLVLWEI 203
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
312-499 1.13e-08

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: 56.36  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 312 TLFLVMKNYPCTLRQYL--------EEQTPSS-------RLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDgc 376
Cdd:cd14049   81 MLYIQMQLCELSLWDWIvernkrpcEEEFKSApytpvdvDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLH-GSD-- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 377 PWLVISDFGCCLADQHVGLRLPFN----SSSVERGGNGSLM--APE-VSTAHSGPsavidysKADTWAVGAIAYEIFgla 449
Cdd:cd14049  158 IHVRIGDFGLACPDILQDGNDSTTmsrlNGLTHTSGVGTCLyaAPEqLEGSHYDF-------KSDMYSIGVILLELF--- 227
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 126215545 450 NPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14049  228 QPFGTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSERPSA 277
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
265-499 1.14e-08

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: 56.57  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSVPLLPGALadypdmlpphyypeglghgrtlfLVMKNYPCTLRQYLEeQTPSSRLATMMTL- 343
Cdd:cd13985   52 KRLCGHPNIVQYYDSAILSSEGRKEVL-----------------------LLMEYCPGSLVDILE-KSPPSPLSEEEVLr 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 ---QLLEGVDHLVQQG--IAHRDLKSDNILVewdSDGCPWlVISDFGcCLADQHVglrlPFNSSS------VERGGNGSL 412
Cdd:cd13985  108 ifyQICQAVGHLHSQSppIIHRDIKIENILF---SNTGRF-KLCDFG-SATTEHY----PLERAEevniieEEIQKNTTP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 M--APEVSTAHSGPSavIDySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYqeaQLPEMPeSVPPEARRLVRSLLQ 490
Cdd:cd13985  179 MyrAPEMIDLYSKKP--IG-EKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKY---SIPEQP-RYSPELHDLIRHMLT 251

                 ....*....
gi 126215545 491 REASKRPSA 499
Cdd:cd13985  252 PDPAERPDI 260
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
266-446 1.17e-08

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: 56.56  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghGRtLFLVMKNYPCTLRQYLEEQtPS--SRLAT-MMT 342
Cdd:cd07833   55 RQLRHENIVNLKEAFRRK--------------------------GR-LYLVFEYVERTLLELLEAS-PGglPPDAVrSYI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLADQ-HVGLRLPFNSSSVERGgngsLMAPE--VST 419
Cdd:cd07833  107 WQLLQAIAYCHSHNIIHRDIKPENILV--SESGV--LKLCDFG--FARAlTARPASPLTDYVATRW----YRAPEllVGD 176
                        170       180
                 ....*....|....*....|....*..
gi 126215545 420 AHSGPSavidyskADTWAVGAIAYEIF 446
Cdd:cd07833  177 TNYGKP-------VDVWAIGCIMAELL 196
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
344-496 1.18e-08

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: 56.59  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGccLAdqhvgLRLPFNSSSVERGGNGSLMAPEVSTAHSg 423
Cdd:cd05605  110 EITCGLEHLHSERIVYRDLKPENILL--DDHG--HVRISDLG--LA-----VEIPEGETIRGRVGTVGYMAPEVVKNER- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 psavidYS-KADTWAVGAIAYEIFGLANPFygqgSAHLE--SRSYQEAQLPEMPE----SVPPEARRLVRSLLQREASKR 496
Cdd:cd05605  178 ------YTfSPDWWGLGCLIYEMIEGQAPF----RARKEkvKREEVDRRVKEDQEeyseKFSEEAKSICSQLLQKDPKTR 247
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
338-496 1.23e-08

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: 56.88  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCClADQHVGlrlpfNSSSVERGGNGSLMAPEV 417
Cdd:cd05620   98 ATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML--DRDG--HIKIADFGMC-KENVFG-----DNRASTFCGTPDYIAPEI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAhsgpsavIDYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAqlPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05620  168 LQG-------LKYTfSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDT--PHYPRWITKESKDILEKLFERDPTRR 238
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
305-499 1.55e-08

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: 55.75  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 305 EGLGHgrtLFLVMKNypCT---LRQYLEEQtpSSRLATMMTL-----QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgc 376
Cdd:cd08219   68 EADGH---LYIVMEY--CDggdLMQKIKLQ--RGKLFPEDTIlqwfvQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK-- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 377 pwLVISDFGCCladqhvglRLPFNSssverggnGSLMAPEVSTAHSGPSAV---IDYS-KADTWAVGAIAYEIFGLANPF 452
Cdd:cd08219  139 --VKLGDFGSA--------RLLTSP--------GAYACTYVGTPYYVPPEIwenMPYNnKSDIWSLGCILYELCTLKHPF 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 126215545 453 YGQGSAHLESRSYQEAQLPeMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd08219  201 QANSWKNLILKVCQGSYKP-LPSHYSYELRSLIKQMFKRNPRSRPSA 246
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
325-499 2.11e-08

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: 55.43  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 325 RQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFG-CCLADQHVGLRlpfnsss 403
Cdd:cd14106   97 TLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGD-IKLCDFGiSRVIGEGEEIR------- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 404 vERGGNGSLMAPEVstAHSGPSAVidysKADTWAVGAIAYEIFGLANPFYGQgsahlesrSYQEAQL----------PEM 473
Cdd:cd14106  169 -EILGTPDYVAPEI--LSYEPISL----ATDMWSIGVLTYVLLTGHSPFGGD--------DKQETFLnisqcnldfpEEL 233
                        170       180
                 ....*....|....*....|....*.
gi 126215545 474 PESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14106  234 FKDVSPLAIDFIKRLLVKDPEKRLTA 259
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
215-502 2.30e-08

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: 55.75  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 215 FAIKMMwnisagsssEAILSKMSQELVPASRVALAGEYGAVtyrrsrdgpKQLAPHPNIIRVFRAFTSSVPLLpgalady 294
Cdd:cd14181   38 FAVKII---------EVTAERLSPEQLEEVRSSTLKEIHIL---------RQVSGHPSIITLIDSYESSTFIF------- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 295 pdmlpphyypeglghgrTLFLVMKNypCTLRQYLEEQ-TPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewds 373
Cdd:cd14181   93 -----------------LVFDLMRR--GELFDYLTEKvTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 374 DGCPWLVISDFG-CCLADQHVGLRlpfnsssvERGGNGSLMAPEV-----STAHSGpsavidYSK-ADTWAVGAIAYEIF 446
Cdd:cd14181  150 DDQLHIKLSDFGfSCHLEPGEKLR--------ELCGTPGYLAPEIlkcsmDETHPG------YGKeVDLWACGVILFTLL 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 447 GLANPFYGQGSAhLESRSYQEAQL----PEMPESvPPEARRLVRSLLQREASKRPSARLA 502
Cdd:cd14181  216 AGSPPFWHRRQM-LMLRMIMEGRYqfssPEWDDR-SSTVKDLISRLLVVDPEIRLTAEQA 273
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
344-500 3.08e-08

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 54.95  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILV-EWDsdgcpWLVISDFGC---CLadqhvglrLP----------FNSSSVERggn 409
Cdd:cd13980  105 QLLHALNQCHKRGVCHGDIKTENVLVtSWN-----WVYLTDFASfkpTY--------LPednpadfsyfFDTSRRRT--- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 410 gSLMAPEVSTAHSGPSAVIDYS------KADTWAVGAIAYEIFGLANPFYGQgSAHLESRSYQEAQLPEMPESVPPEARR 483
Cdd:cd13980  169 -CYIAPERFVDALTLDAESERRdgeltpAMDIFSLGCVIAELFTEGRPLFDL-SQLLAYRKGEFSPEQVLEKIEDPNIRE 246
                        170
                 ....*....|....*..
gi 126215545 484 LVRSLLQREASKRPSAR 500
Cdd:cd13980  247 LILHMIQRDPSKRLSAE 263
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
334-504 3.11e-08

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: 55.24  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGccladqhVGLRLPfNSSSVERG--GNGS 411
Cdd:cd14094  107 SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFG-------VAIQLG-ESGLVAGGrvGTPH 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 412 LMAPEVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQL-PEMPESVPPEARRLVRSLL 489
Cdd:cd14094  178 FMAPEVVKREP-------YGKpVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMnPRQWSHISESAKDLVRRML 250
                        170
                 ....*....|....*
gi 126215545 490 QREASKRPSARLAAN 504
Cdd:cd14094  251 MLDPAERITVYEALN 265
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
326-498 3.13e-08

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: 54.84  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 326 QYLEEQtpssrLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGCPWLV-ISDFGcclADQHVGlrlpfNSSSV 404
Cdd:cd14112   95 YYSEEQ-----VATTVR-QILDALHYLHFKGIAHLDVQPDNIMF---QSVRSWQVkLVDFG---RAQKVS-----KLGKV 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 ERGGNGSLMAPEVstaHSGPSAVidYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESR---SYQEAQLPEMPESVPPEA 481
Cdd:cd14112  158 PVDGDTDWASPEF---HNPETPI--TVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKenvIFVKCRPNLIFVEATQEA 232
                        170
                 ....*....|....*..
gi 126215545 482 RRLVRSLLQREASKRPS 498
Cdd:cd14112  233 LRFATWALKKSPTRRMR 249
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
270-499 3.30e-08

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: 54.64  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSsvpllpgaladypdmlPPHYYpeglghgrtlfLVMK--------NYPCTLRQYLEEQtpssrlATMM 341
Cdd:cd14095   57 HPNIVQLIEEYDT----------------DTELY-----------LVMElvkggdlfDAITSSTKFTERD------ASRM 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLAdQHVGLRLpfnsSSVerGGNGSLMAPEVsTAH 421
Cdd:cd14095  104 VTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLKLADFG--LA-TEVKEPL----FTV--CGTPTYVAPEI-LAE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGpsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLE-SRSYQEAQLpEMP----ESVPPEARRLVRSLLQREASK 495
Cdd:cd14095  174 TG------YGlKVDIWAAGVITYILLCGFPPFRSPDRDQEElFDLILAGEF-EFLspywDNISDSAKDLISRMLVVDPEK 246

                 ....
gi 126215545 496 RPSA 499
Cdd:cd14095  247 RYSA 250
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
348-496 3.33e-08

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: 55.47  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqhvGLRLPFNSSSVERGGNGSLMAPEVSTAHSGPSAV 427
Cdd:cd05592  108 GLQFLHSRGIIYRDLKLDNVLL--DREG--HIKIADFGMC------KENIYGENKASTFCGTPDYIAPEILKGQKYNQSV 177
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 428 idyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAqlPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05592  178 ------DWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDT--PHYPRWLTKEAASCLSLLLERNPEKR 238
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
310-452 3.36e-08

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: 55.41  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLV---MKNYPcTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGc 386
Cdd:cd14177   70 GRYVYLVtelMKGGE-LLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFG- 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 387 cLADQHvglrlpfnsssveRGGNGSLMAPEVSTAHSGPSAVID--YSKA-DTWAVGAIAYEIFGLANPF 452
Cdd:cd14177  148 -FAKQL-------------RGENGLLLTPCYTANFVAPEVLMRqgYDAAcDIWSLGVLLYTMLAGYTPF 202
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
344-499 3.62e-08

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: 55.04  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLAdqhvglrlpfNSSSVERG----GNGSLMAPEVST 419
Cdd:cd06644  118 QMLEALQYLHSMKIIHRDLKAGNVLLTLDGD----IKLADFGVSAK----------NVKTLQRRdsfiGTPYWMAPEVVM 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPSAVIDYsKADTWAVGAIAYEIFGLANPFYGQGSAH-LESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd06644  184 CETMKDTPYDY-KADIWSLGITLIEMAQIEPPHHELNPMRvLLKIAKSEPPTLSQPSKWSMEFRDFLKTALDKHPETRPS 262

                 .
gi 126215545 499 A 499
Cdd:cd06644  263 A 263
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
270-499 4.21e-08

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: 55.22  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgalaDYPDMlpphyypeglghgRTLFLVMKNYPCTL------RQYLEEQtpssRLATMMtL 343
Cdd:cd07834   58 HENIIGLLDILRPP---------SPEEF-------------NDVYIVTELMETDLhkviksPQPLTDD----HIQYFL-Y 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLAdqhvglRlpfnssSVERGGNGSLMAPEVSTAHSG 423
Cdd:cd07834  111 QILRGLKYLHSAGVIHRDLKPSNILVNSNCD----LKICDFG--LA------R------GVDPDEDKGFLTEYVVTRWYR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSAVI----DYSKA-DTWAVGAIAYEIFGLANPFYGQGSAH----------------------------LESRSYQEAQ- 469
Cdd:cd07834  173 APELLlsskKYTKAiDIWSVGCIFAELLTRKPLFPGRDYIDqlnlivevlgtpseedlkfissekarnyLKSLPKKPKKp 252
                        250       260       270
                 ....*....|....*....|....*....|
gi 126215545 470 LPEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd07834  253 LSEVFPGASPEAIDLLEKMLVFNPKKRITA 282
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
311-497 4.37e-08

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: 54.38  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLV---MKNyPCtLRQYLEEQTPSSRLATM--MTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG 385
Cdd:cd05059   72 RPIFIVteyMAN-GC-LLNYLRERRGKFQTEQLleMCKDVCEAMEYLESNGFIHRDLAARNCLV--GEQNV--VKVSDFG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 CC---LADQHV---GLRLPFNSSsverggngslmAPEVSTaHSGPSavidySKADTWAVGAIAYEIFGLAN-PFYGQGSA 458
Cdd:cd05059  146 LAryvLDDEYTssvGTKFPVKWS-----------PPEVFM-YSKFS-----SKSDVWSFGVLMWEVFSEGKmPYERFSNS 208
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126215545 459 HLESRSYQEAQLPEmPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd05059  209 EVVEHISQGYRLYR-PHLAPTEVYTIMYSCWHEKPEERP 246
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
343-498 4.50e-08

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: 54.32  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQG---IAHRDLKSDNIL----VEWDSDGCPWLVISDFGccLADQHvglrlpFNSSSVERGGNGSLMAP 415
Cdd:cd14061   99 IQIARGMNYLHNEApvpIIHRDLKSSNILileaIENEDLENKTLKITDFG--LAREW------HKTTRMSAAGTYAWMAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAHSgpsavidYSKA-DTWAVGAIAYEIFGLANPF---------YGQGSAHLesrsyqeaQLPeMPESVPPEARRLV 485
Cdd:cd14061  171 EVIKSST-------FSKAsDVWSYGVLLWELLTGEVPYkgidglavaYGVAVNKL--------TLP-IPSTCPEPFAQLM 234
                        170
                 ....*....|...
gi 126215545 486 RSLLQREASKRPS 498
Cdd:cd14061  235 KDCWQPDPHDRPS 247
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
340-499 4.50e-08

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: 54.52  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 340 MMTLQLLEGVDHLVQQ-GIAHRDLKSDNILVewDSDGCPwlVISDFGCCladQHVGLRLPFNSSSVergGNGSLMAPEvs 418
Cdd:cd06623  103 YIARQILKGLDYLHTKrHIIHRDIKPSNLLI--NSKGEV--KIADFGIS---KVLENTLDQCNTFV---GTVTYMSPE-- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 tahsgpsaVID---YS-KADTWAVGAIAYEIFGLANPFygqgsAHLESRSY--------QEAQLPEMPESVPPEARRLVR 486
Cdd:cd06623  171 --------RIQgesYSyAADIWSLGLTLLECALGKFPF-----LPPGQPSFfelmqaicDGPPPSLPAEEFSPEFRDFIS 237
                        170
                 ....*....|...
gi 126215545 487 SLLQREASKRPSA 499
Cdd:cd06623  238 ACLQKDPKKRPSA 250
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
344-502 4.55e-08

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: 54.60  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVISDFGccladQHVGLRLPFNSSSVErgGNGSLMAPEVSTAHsg 423
Cdd:cd14113  111 EILEALQYLHNCRIAHLDLKPENILVD-QSLSKPTIKLADFG-----DAVQLNTTYYIHQLL--GSPEFAAPEIILGN-- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSAVidysKADTWAVGAIAYEIFGLANPFYGQGsahLESRSYQEAQLP-EMPES----VPPEARRLVRSLLQREASKRPS 498
Cdd:cd14113  181 PVSL----TSDLWSIGVLTYVLLSGVSPFLDES---VEETCLNICRLDfSFPDDyfkgVSQKAKDFVCFLLQMDPAKRPS 253

                 ....
gi 126215545 499 ARLA 502
Cdd:cd14113  254 AALC 257
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
312-496 4.80e-08

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: 54.63  E-value: 4.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 312 TLFLVMKNypCT---LRQYLEEQ-TPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwlVISDFGCC 387
Cdd:cd14201   79 SVFLVMEY--CNggdLADYLQAKgTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKS--SVSGIRIK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 388 LADQHVGLRLPFNSSSVERGGNGSLMAPEVSTAHSGPsavidySKADTWAVGAIAYEIFGLANPFygQGSAHLESRSYQE 467
Cdd:cd14201  155 IADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYD------AKADLWSIGTVIYQCLVGKPPF--QANSPQDLRMFYE 226
                        170       180       190
                 ....*....|....*....|....*....|..
gi 126215545 468 AQ---LPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14201  227 KNknlQPSIPRETSPYLADLLLGLLQRNQKDR 258
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
313-492 5.06e-08

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: 55.40  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYP----CTLRQYLEEQTPSSrLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCL 388
Cdd:cd05624  147 LYLVMDYYVggdlLTLLSKFEDKLPED-MARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL--DMNG--HIRLADFGSCL 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQHVGLRlpfnSSSVERgGNGSLMAPEVSTAHS------GPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAHLES 462
Cdd:cd05624  222 KMNDDGTV----QSSVAV-GTPDYISPEILQAMEdgmgkyGP-------ECDWWSLGVCMYEMLYGETPFYAESLVETYG 289
                        170       180       190
                 ....*....|....*....|....*....|....
gi 126215545 463 R--SYQEA-QLPEMPESVPPEARRLVRSLL-QRE 492
Cdd:cd05624  290 KimNHEERfQFPSHVTDVSEEAKDLIQRLIcSRE 323
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
338-499 5.62e-08

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: 54.20  E-value: 5.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVIsDFGccLADQHV---GLRLPFnsssvergGNGSLMA 414
Cdd:cd14192  104 AILFTRQICEGVHYLHQHYILHLDLKPENILCV-NSTGNQIKII-DFG--LARRYKpreKLKVNF--------GTPEFLA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEvstahsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGSAhlESRSY----QEAQLPEMPESVPPEARRLVR 486
Cdd:cd14192  172 PE----------VVNYDfvsfPTDMWSVGVITYMLLSGLSPFLGETDA--ETMNNivncKWDFDAEAFENLSEEAKDFIS 239
                        170
                 ....*....|...
gi 126215545 487 SLLQREASKRPSA 499
Cdd:cd14192  240 RLLVKEKSCRMSA 252
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
329-496 6.57e-08

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: 54.24  E-value: 6.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccladqhVGLRLPFNSSSVERGG 408
Cdd:cd14195  101 EKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFG-------IAHKIEAGNEFKNIFG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 NGSLMAPEvstahsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGSAH-LESRSYQEAQLPEMPESVPPE-AR 482
Cdd:cd14195  174 TPEFVAPE----------IVNYEplglEADMWSIGVITYILLSGASPFLGETKQEtLTNISAVNYDFDEEYFSNTSElAK 243
                        170
                 ....*....|....
gi 126215545 483 RLVRSLLQREASKR 496
Cdd:cd14195  244 DFIRRLLVKDPKKR 257
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
342-499 7.04e-08

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: 53.89  E-value: 7.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVGLRlpfNSSSVERGGNGSLMAPEVSTAH 421
Cdd:cd06652  112 TRQILEGVHYLHSNMIVHRDIKGANILR--DSVGN--VKLGDFGASKRLQTICLS---GTGMKSVTGTPYWMSPEVISGE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SgpsavidYS-KADTWAVGAIAYEIFGLANPFygqgsAHLESRS--YQEAQLPEMPEsVPPEARRLVRSLLQR---EASK 495
Cdd:cd06652  185 G-------YGrKADIWSVGCTVVEMLTEKPPW-----AEFEAMAaiFKIATQPTNPQ-LPAHVSDHCRDFLKRifvEAKL 251

                 ....
gi 126215545 496 RPSA 499
Cdd:cd06652  252 RPSA 255
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
310-500 8.21e-08

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: 53.57  E-value: 8.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPC-TLRQYLEEQTpSSRLATMMT----LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDF 384
Cdd:cd08529   71 KGKLNIVMEYAENgDLHSLIKSQR-GRPLPEDQIwkffIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN----VKIGDL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GCC--LADQHVglrlpFNSSSVergGNGSLMAPEVSTAHSgpsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLe 461
Cdd:cd08529  146 GVAkiLSDTTN-----FAQTIV---GTPYYLSPELCEDKP-------YNeKSDVWALGCVLYELCTGKHPFEAQNQGAL- 209
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126215545 462 SRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd08529  210 ILKIVRGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTT 248
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
334-499 8.82e-08

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: 53.57  E-value: 8.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVISDFGCCladQHVGLRlPFNSSSVergGNGSLM 413
Cdd:cd14082  101 PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLA-SAEPFPQVKLCDFGFA---RIIGEK-SFRRSVV---GTPAYL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVSTAHSgpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAH--LESRSYqeaQLPEMPES-VPPEARRLVRSLL 489
Cdd:cd14082  173 APEVLRNKG-------YNRSlDMWSVGVIIYVSLSGTFPFNEDEDINdqIQNAAF---MYPPNPWKeISPDAIDLINNLL 242
                        170
                 ....*....|
gi 126215545 490 QREASKRPSA 499
Cdd:cd14082  243 QVKMRKRYSV 252
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
315-539 9.87e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.11  E-value: 9.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 315 LVMKNYPCTLRQYL-EEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCpwlvISDFGCCladqh 392
Cdd:PHA03209 134 MVLPHYSSDLYTYLtKRSRPlPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVC----IGDLGAA----- 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 393 vglRLPFNSSS-VERGGNGSLMAPEVstahsgpSAVIDY-SKADTWAVGAIAYEIfgLANP---FYGQGSAHLESRSYQE 467
Cdd:PHA03209 205 ---QFPVVAPAfLGLAGTVETNAPEV-------LARDKYnSKADIWSAGIVLFEM--LAYPstiFEDPPSTPEEYVKSCH 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 468 AQLPEM-------PESVPPE-ARRLVRSLLQREASKR-PSARLAA-NVLHLSLWGEHLlalknlkLDKMIAW--LLQQSA 535
Cdd:PHA03209 273 SHLLKIistlkvhPEEFPRDpGSRLVRGFIEYASLERqPYTRYPCfQRVNLPIDGEFL-------VHKMLTFdaAMRPSA 345

                 ....
gi 126215545 536 ATLL 539
Cdd:PHA03209 346 EEIL 349
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
270-499 1.11e-07

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: 53.13  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFrAFTssvpllpgaladypdmlpphYYPEGLGHGRTLFLVMKNYP-CTLRQYLEeQTPSSRLAT--MMTLQLL 346
Cdd:cd14012   57 HPNLVSYL-AFS--------------------IERRGRSDGWKVYLLTEYAPgGSLSELLD-SVGSVPLDTarRWTLQLL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVEWD-SDGCPWLVISDFGCCLADQHVGLRLPFNSSSVERggngslmAPEVSTAHSGPS 425
Cdd:cd14012  115 EALEYLHRNGVVHKSLHAGNVLLDRDaGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQTYWL-------PPELAQGSKSPT 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 426 avidySKADTWAVGAIAYE-IFGLANPFYgqgsahlesrsYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14012  188 -----RKTDVWDLGLLFLQmLFGLDVLEK-----------YTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTA 246
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
265-510 1.12e-07

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: 53.26  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLApHPNIIRVFRAFTSSVPLlpGALADYPDmlpphyypeglghGRTLFLVMKNypctlRQYLEEQTPSSRLAtmmtlQ 344
Cdd:cd14076   61 KGLT-HPNIVRLLDVLKTKKYI--GIVLEFVS-------------GGELFDYILA-----RRRLKDSVACRLFA-----Q 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQHVGLRLPFNSSSVergGNGSLMAPEVSTAHSGP 424
Cdd:cd14076  115 LISGVAYLHKKGVVHRDLKLENLLLDKNRN----LVITDFG--FANTFDHFNGDLMSTSC---GSPCYAAPELVVSDSMY 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 425 SAvidySKADTWAVGAIAYEIFGLANPF-----YGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRpsA 499
Cdd:cd14076  186 AG----RKADIWSCGVILYAMLAGYLPFdddphNPNGDNVPRLYRYICNTPLIFPEYVTPKARDLLRRILVPNPRKR--I 259
                        250
                 ....*....|.
gi 126215545 500 RLAANVLHLSL 510
Cdd:cd14076  260 RLSAIMRHAWL 270
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
344-496 1.22e-07

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: 53.46  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGccLAdqhvglRLpfnsssveRGGNGSLM---------A 414
Cdd:cd14092  107 QLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAE-IKIVDFG--FA------RL--------KPENQPLKtpcftlpyaA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEV-STAHSGPSavidYSKA-DTWAVGAIAYEIFGLANPFygqgsahlESRSYQEaQLPEMPE---------------SV 477
Cdd:cd14092  170 PEVlKQALSTQG----YDEScDLWSLGVILYTMLSGQVPF--------QSPSRNE-SAAEIMKriksgdfsfdgeewkNV 236
                        170
                 ....*....|....*....
gi 126215545 478 PPEARRLVRSLLQREASKR 496
Cdd:cd14092  237 SSEAKSLIQGLLTVDPSKR 255
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
343-498 1.26e-07

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: 53.27  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCC-------LADQHVGLRLPFNSSSVERGGNGSLMAP 415
Cdd:cd14027   97 LEIIEGMAYLHGKGVIHKDLKPENILVDNDFH----IKIADLGLAsfkmwskLTKEEHNEQREVDGTAKKNAGTLYYMAP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 E-VSTAHSGPSavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLP---EMPESVPPEARRLVRSLLQR 491
Cdd:cd14027  173 EhLNDVNAKPT-----EKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPdvdDITEYCPREIIDLMKLCWEA 247

                 ....*..
gi 126215545 492 EASKRPS 498
Cdd:cd14027  248 NPEARPT 254
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
313-489 1.31e-07

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: 53.87  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYP----CTLRQYLEEQTPSSrLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCL 388
Cdd:cd05623  147 LYLVMDYYVggdlLTLLSKFEDRLPED-MARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGH----IRLADFGSCL 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQHVGLRlpfnSSSVERgGNGSLMAPEVSTAHSGPSAVIDySKADTWAVGAIAYEIFGLANPFYGQGSAHLESR--SYQ 466
Cdd:cd05623  222 KLMEDGTV----QSSVAV-GTPDYISPEILQAMEDGKGKYG-PECDWWSLGVCMYEMLYGETPFYAESLVETYGKimNHK 295
                        170       180
                 ....*....|....*....|....
gi 126215545 467 EA-QLPEMPESVPPEARRLVRSLL 489
Cdd:cd05623  296 ERfQFPTQVTDVSENAKDLIRRLI 319
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
349-496 1.34e-07

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: 53.51  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADqhvglrLPFNSSSVERGGNGSLMAPEVSTAHsgpsavi 428
Cdd:cd05571  108 LGYLHSQGIVYRDLKLENLLL--DKDG--HIKITDFGLCKEE------ISYGATTKTFCGTPEYLAPEVLEDN------- 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 429 DYSKA-DTWAVGAIAYEIFGLANPFYgqgsahleSRSYQ---EAQLPE---MPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05571  171 DYGRAvDWWGLGVVMYEMMCGRLPFY--------NRDHEvlfELILMEevrFPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
344-452 1.35e-07

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: 53.57  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLA-DQHVGLRLPFNsssvergGNGSLMAPEVSTAHS 422
Cdd:cd06637  119 EILRGLSHLHQHKVIHRDIKGQNVLLTENAE----VKLVDFGVSAQlDRTVGRRNTFI-------GTPYWMAPEVIACDE 187
                         90       100       110
                 ....*....|....*....|....*....|
gi 126215545 423 GPSAVIDYsKADTWAVGAIAYEIFGLANPF 452
Cdd:cd06637  188 NPDATYDF-KSDLWSLGITAIEMAEGAPPL 216
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
330-496 1.46e-07

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: 53.49  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 330 EQTPSSRLATMMTLQLLEGVDHL-VQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADQHVGLRLPFNSSSVErgg 408
Cdd:cd05594  119 ERVFSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLML--DKDG--HIKITDFGLCKEGIKDGATMKTFCGTPE--- 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 ngsLMAPEVSTAHsgpsaviDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAqlPEMPESVPPEARRLVRS 487
Cdd:cd05594  192 ---YLAPEVLEDN-------DYGRAvDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE--IRFPRTLSPEAKSLLSG 259

                 ....*....
gi 126215545 488 LLQREASKR 496
Cdd:cd05594  260 LLKKDPKQR 268
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
265-498 1.54e-07

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: 53.19  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSVPLL-------PGALADYpdmLPPHYYPEglghgrtlflvMKNYPCTLRqyLEEQTPSSRL 337
Cdd:cd05053   71 KMIGKHKNIINLLGACTQDGPLYvvveyasKGNLREF---LRARRPPG-----------EEASPDDPR--VPEEQLTQKD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLA-DQHvglrlpfNSSSVERGGNGSL---- 412
Cdd:cd05053  135 LVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV----MKIADFG--LArDIH-------HIDYYRKTTNGRLpvkw 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 413 MAPE-----VSTAHSgpsavidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRS 487
Cdd:cd05053  202 MAPEalfdrVYTHQS-----------DVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMEKPQNCTQELYMLMRD 270
                        250
                 ....*....|.
gi 126215545 488 LLQREASKRPS 498
Cdd:cd05053  271 CWHEVPSQRPT 281
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
343-502 1.55e-07

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: 52.95  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLAdqhvglRlPFNSSSVERGGNGSLM----APEV- 417
Cdd:cd07840  111 KQLLEGLQYLHSNGILHRDIKGSNILI--NNDGV--LKLADFG--LA------R-PYTKENNADYTNRVITlwyrPPELl 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 --STahsgpsaviDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQ------EAQLP--------EMPESVPPE 480
Cdd:cd07840  178 lgAT---------RYGPEvDMWSVGCILAELFTGKPIFQGKTELEQLEKIFElcgsptEENWPgvsdlpwfENLKPKKPY 248
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126215545 481 ARR---------------LVRSLLQREASKRPSARLA 502
Cdd:cd07840  249 KRRlrevfknvidpsaldLLDKLLTLDPKKRISADQA 285
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
341-500 1.62e-07

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: 53.02  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhVGLRLPFNSSsvERG---GNGSLMAPEV 417
Cdd:cd06609  103 ILREVLLGLEYLHSEGKIHRDIKAANILLSEEGD----VKLADFG-------VSGQLTSTMS--KRNtfvGTPFWMAPEV 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STaHSGpsavidY-SKADTWAVGAIAYEifgLANpfygqGSAHLESRSYQEAqLPEMPESVPP---------EARRLVRS 487
Cdd:cd06609  170 IK-QSG------YdEKADIWSLGITAIE---LAK-----GEPPLSDLHPMRV-LFLIPKNNPPslegnkfskPFKDFVEL 233
                        170
                 ....*....|...
gi 126215545 488 LLQREASKRPSAR 500
Cdd:cd06609  234 CLNKDPKERPSAK 246
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
311-500 1.70e-07

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: 53.10  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPC-TLRQYLE---EQTPSSRLaTMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGC 386
Cdd:cd14205   80 RNLRLIMEYLPYgSLRDYLQkhkERIDHIKL-LQYTSQICKGMEYLGTKRYIHRDLATRNILVENENR----VKIGDFGL 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 387 CLAdqhvglrLPFNSS--SVERGGNGSLM--APEVSTAHSGPSAvidyskADTWAVGAIAYEIFG--------------- 447
Cdd:cd14205  155 TKV-------LPQDKEyyKVKEPGESPIFwyAPESLTESKFSVA------SDVWSFGVVLYELFTyieksksppaefmrm 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 126215545 448 LANPFYGQGSA-HLESRSYQEAQLPEmPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd14205  222 IGNDKQGQMIVfHLIELLKNNGRLPR-PDGCPDEIYMIMTECWNNNVNQRPSFR 274
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
324-499 1.70e-07

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: 53.00  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLATM-MTLQLLEGVDHLVQQGIAHRDLKSDNILV-EWDSDGCPWLVISDFGCCladqhvglRLPFNS 401
Cdd:cd14000   99 LQQDSRSFASLGRTLQQrIALQVADGLRYLHSAMIIYRDLKSHNVLVwTLYPNSAIIIKIADYGIS--------RQCCRM 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVERGGNGSLMAPEVStahsgPSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQ--LPEMPESVPP 479
Cdd:cd14000  171 GAKGSEGTPGFRAPEIA-----RGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRppLKQYECAPWP 245
                        170       180
                 ....*....|....*....|
gi 126215545 480 EARRLVRSLLQREASKRPSA 499
Cdd:cd14000  246 EVEVLMKKCWKENPQQRPTA 265
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
303-503 1.75e-07

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: 53.10  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 303 YPEGLGhgrtLFLVMKNYPCTLRQYL-EEQTPSSRLAT-MMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLV 380
Cdd:cd07832   69 FPHGTG----FVLVFEYMLSSLSEVLrDEERPLTEAQVkRYMRMLLKGVAYMHANRIMHRDLKPANLLI--SSTGV--LK 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 381 ISDFGccLAdqhvglRLPFNSSSV---ERGGNGSLMAPEVSTAHSgpsaviDYSKA-DTWAVGAIAYEIFGLANPFYGQ- 455
Cdd:cd07832  141 IADFG--LA------RLFSEEDPRlysHQVATRWYRAPELLYGSR------KYDEGvDLWAVGCIFAELLNGSPLFPGEn 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126215545 456 ------------GSAHLES----RS---YQEAQLPEMP----ESVPPEARRLVRSLLQREASKRPSARLAA 503
Cdd:cd07832  207 dieqlaivlrtlGTPNEKTwpelTSlpdYNKITFPESKgirlEEIFPDCSPEAIDLLKGLLVYNPKKRLSA 277
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
343-498 1.79e-07

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: 52.73  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQG---IAHRDLKSDNIL----VEWDSDGCPWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSLMAP 415
Cdd:cd14146  109 VQIARGMLYLHEEAvvpILHRDLKSSNILllekIEHDDICNKTLKITDFG--LA------REWHRTTKMSAAGTYAWMAP 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQLPeMPESVPPEARRLVRSLLQREA 493
Cdd:cd14146  181 EVIKSSL-------FSKgSDIWSYGVLLWELLTGEVPYRGiDGLAVAYGVAVNKLTLP-IPSTCPEPFAKLMKECWEQDP 252

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd14146  253 HIRPS 257
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
345-506 1.79e-07

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: 52.68  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFG--CCLAD------QHVGLRLPFNSSSVERGGNGS--LMA 414
Cdd:cd14010  103 LVRGLHYIHSKGIIYCDLKPSNILL----DGNGTLKLSDFGlaRREGEilkelfGQFSDEGNVNKVSKKQAKRGTpyYMA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEVstAHSGPsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLeSRSYQEAQLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd14010  179 PEL--FQGGV-----HSFAsDLWALGCVLYEMFTGKPPFVAESFTEL-VEKILNEDPPPPPPKVSSKPSPDFKSLLKGLL 250
                        170
                 ....*....|...
gi 126215545 494 SKRPSARLAANVL 506
Cdd:cd14010  251 EKDPAKRLSWDEL 263
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
329-499 1.83e-07

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: 52.44  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQtpssrLATMmTLQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCpwLVISDFGCCladQHVGLRLPFNSSSVergG 408
Cdd:cd06648  102 EEQ-----IATV-CRAVLKALSFLHSQGVIHRDIKSDSILLT--SDGR--VKLSDFGFC---AQVSKEVPRRKSLV---G 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 NGSLMAPEV-STAHSGPsavidysKADTWAVGAIAYEIFGLANPFYGQGSahLES-RSYQEAQLPEM--PESVPPEARRL 484
Cdd:cd06648  166 TPYWMAPEViSRLPYGT-------EVDIWSLGIMVIEMVDGEPPYFNEPP--LQAmKRIRDNEPPKLknLHKVSPRLRSF 236
                        170
                 ....*....|....*
gi 126215545 485 VRSLLQREASKRPSA 499
Cdd:cd06648  237 LDRMLVRDPAQRATA 251
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
336-498 2.11e-07

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: 52.29  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 336 RLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGCC-LADQHVGLRLP-FNSSSVerggngslm 413
Cdd:cd14089  100 REAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAI-LKLTDFGFAkETTTKKSLQTPcYTPYYV--------- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVstahSGPSAvidYSKA-DTWAVGAIAYEIFGLANPFYGQG----SAHLESRSYQ-EAQLPEmPE--SVPPEARRLV 485
Cdd:cd14089  170 APEV----LGPEK---YDKScDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKKRIRNgQYEFPN-PEwsNVSEEAKDLI 241
                        170
                 ....*....|...
gi 126215545 486 RSLLQREASKRPS 498
Cdd:cd14089  242 RGLLKTDPSERLT 254
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
325-502 2.13e-07

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: 52.51  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 325 RQYLEEqtpssRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQHVGLRLPFnsssV 404
Cdd:cd14070   97 KKRLEE-----REARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN----IKLIDFGLSNCAGILGYSDPF----S 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 ERGGNGSLMAPE-VSTAHSGPsavidysKADTWAVGAIAYEIFGLANPFYGQG-SAHLESRSYQEAQLPEMPESVPPEAR 482
Cdd:cd14070  164 TQCGSPAYAAPElLARKKYGP-------KVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQKMVDKEMNPLPTDLSPGAI 236
                        170       180
                 ....*....|....*....|
gi 126215545 483 RLVRSLLQREASKRPSARLA 502
Cdd:cd14070  237 SFLRSLLEPDPLKRPNIKQA 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
334-502 2.16e-07

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: 52.54  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVeWDSDGCPWLVISDFGccLADQHVGLRlpfNSSSVERGGNGSLM 413
Cdd:cd14087   95 TERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLY-YHPGPDSKIMITDFG--LASTRKKGP---NCLMKTTCGTPEYI 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESR------SYQeaqlPEMPESVPPEARRLVRS 487
Cdd:cd14087  169 APEILLRKPYTQSV------DMWAVGVIAYILLSGTMPFDDDNRTRLYRQilrakySYS----GEPWPSVSNLAKDFIDR 238
                        170
                 ....*....|....*
gi 126215545 488 LLQREASKRPSARLA 502
Cdd:cd14087  239 LLTVNPGERLSATQA 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
344-500 2.44e-07

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: 52.24  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQhvglrlPFNSSSVERGGNGSLMAPEVSTAHS- 422
Cdd:cd06647  111 ECLQALEFLHSNQVIHRDIKSDNILLGMDGS----VKLTDFGFCAQIT------PEQSKRSTMVGTPYWMAPEVVTRKAy 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPsavidysKADTWAVGAIAYEIFGLANPFYGQG--SAHLESRSYQEAQLPEmPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd06647  181 GP-------KVDIWSLGIMAIEMVEGEPPYLNENplRALYLIATNGTPELQN-PEKLSAIFRDFLNRCLEMDVEKRGSAK 252
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
334-453 2.46e-07

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: 52.52  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGCC-LADQHVGLrlpfnsSSVerGGNGSL 412
Cdd:cd14085   96 SERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAP-LKIADFGLSkIVDQQVTM------KTV--CGTPGY 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126215545 413 MAPEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFY 453
Cdd:cd14085  167 CAPEILRGCAYGPEV------DMWSVGVITYILLCGFEPFY 201
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
290-498 2.48e-07

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: 52.32  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 290 ALADYPDMLPPH--YYPEGLGHGRTLFLVMK-----NYPCTLRQYLEEQTPSSRLATMMTL-QLLEGVDHLVQQGIAHRD 361
Cdd:cd06638   70 ALSDHPNVVKFYgmYYKKDVKNGDQLWLVLElcnggSVTDLVKGFLKRGERMEEPIIAYILhEALMGLQHLHVNKTIHRD 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 362 LKSDNILVEwdSDGCPWLVisDFGccLADQHVGLRLPFNSSSvergGNGSLMAPEVSTAHSGPSAVIDySKADTWAVGAI 441
Cdd:cd06638  150 VKGNNILLT--TEGGVKLV--DFG--VSAQLTSTRLRRNTSV----GTPFWMAPEVIACEQQLDSTYD-ARCDVWSLGIT 218
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 442 AYEIfglanpfyGQGSAHLESRSYQEAqLPEMPESVPPEARR----------LVRSLLQREASKRPS 498
Cdd:cd06638  219 AIEL--------GDGDPPLADLHPMRA-LFKIPRNPPPTLHQpelwsnefndFIRKCLTKDYEKRPT 276
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
343-463 2.53e-07

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: 52.13  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladqhvglrLPFNSSSVERGGN--GSL--MAPEVS 418
Cdd:cd14111  106 VQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA----IKIVDFGSA---------QSFNPLSLRQLGRrtGTLeyMAPEMV 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 126215545 419 TAHSGPSAvidyskADTWAVGAIAYEIFGLANPFYGQGSAHLESR 463
Cdd:cd14111  173 KGEPVGPP------ADIWSIGVLTYIMLSGRSPFEDQDPQETEAK 211
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
310-452 2.59e-07

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: 52.32  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPC--TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLV-ISDFGc 386
Cdd:cd14178   69 GKFVYLVMELMRGgeLLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYM-DESGNPESIrICDFG- 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 387 cLADQHvglrlpfnsssveRGGNGSLMAPEVSTAHSGPSAVI--DYSKA-DTWAVGAIAYEIFGLANPF 452
Cdd:cd14178  147 -FAKQL-------------RAENGLLMTPCYTANFVAPEVLKrqGYDAAcDIWSLGILLYTMLAGFTPF 201
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
297-498 2.65e-07

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: 52.35  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 297 MLPPHY-YPEGLGHGRTLFlvmknypctlrQYLEEQT---PSSRLAtMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWD 372
Cdd:cd14063   66 MDPPHLaIVTSLCKGRTLY-----------SLIHERKekfDFNKTV-QIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 373 SdgcpwLVISDFGCcladqhvglrlpFNSSSVERGG--NGSLM---------APEVSTAHSGPSAVID---YSKA-DTWA 437
Cdd:cd14063  134 R-----VVITDFGL------------FSLSGLLQPGrrEDTLVipngwlcylAPEIIRALSPDLDFEEslpFTKAsDVYA 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 438 VGAIAYEIFGLANPFYGQgsaHLESRSYQEAQLPEMPES---VPPEARRLVRSLLQREASKRPS 498
Cdd:cd14063  197 FGTVWYELLAGRWPFKEQ---PAESIIWQVGCGKKQSLSqldIGREVKDILMQCWAYDPEKRPT 257
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
344-499 2.91e-07

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: 51.83  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVeWDSdGCPWLVISDFGCcladqhvGLRLPFNSSSVERGGNGSLMAPEVsTAHSG 423
Cdd:cd14108  105 QLLEGIEYLHQNDVLHLDLKPENLLM-ADQ-KTDQVRICDFGN-------AQELTPNEPQYCKYGTPEFVAPEI-VNQSP 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 424 PSAVidyskADTWAVGAIAYEIFGLANPFYGQG--SAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREaSKRPSA 499
Cdd:cd14108  175 VSKV-----TDIWPVGVIAYLCLTGISPFVGENdrTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLVSD-RLRPDA 246
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
348-496 2.98e-07

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: 52.69  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADQHVGLrlpfnsSSVERGGNGSLMAPEVstahsgpSAV 427
Cdd:cd05616  113 GLFFLQSKGIIYRDLKLDNVML--DSEG--HIKIADFGMCKENIWDGV------TTKTFCGTPDYIAPEI-------IAY 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 428 IDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLeSRSYQEAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05616  176 QPYGKSvDWWAFGVLLYEMLAGQAPFEGEDEDEL-FQSIMEHNV-AYPKSMSKEAVAICKGLMTKHPGKR 243
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
270-497 3.06e-07

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: 52.04  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRvfraftssvplLPGALADYPdmlpphyypeglghgrtLFLVMKNYPC-TLRQYLEEQTPSSRLATMMT--LQLL 346
Cdd:cd05056   66 HPHIVK-----------LIGVITENP-----------------VWIVMELAPLgELRSYLQVNKYSLDLASLILyaYQLS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVEwdSDGCPWLviSDFGccladqhvgLRLPFNSSSVERGGNGSL----MAPEVstahs 422
Cdd:cd05056  118 TALAYLESKRFVHRDIAARNVLVS--SPDCVKL--GDFG---------LSRYMEDESYYKASKGKLpikwMAPES----- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 gpsavIDY----SKADTWAVGAIAYEIFGLA-NPFYGQGSAHLESRSYQEAQLPeMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd05056  180 -----INFrrftSASDVWMFGVCMWEILMLGvKPFQGVKNNDVIGRIENGERLP-MPPNCPPTLYSLMTKCWAYDPSKRP 253
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
344-496 3.13e-07

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: 52.28  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVSTAHSg 423
Cdd:cd05632  112 EILCGLEDLHRENTVYRDLKPENILL--DDYG--HIRISDLG-------LAVKIPEGESIRGRVGTVGYMAPEVLNNQR- 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 424 psavidYS-KADTWAVGAIAYEIFGLANPFygQGSAHLESRSYQEAQLPEMPESVPP----EARRLVRSLLQREASKR 496
Cdd:cd05632  180 ------YTlSPDYWGLGCLIYEMIEGQSPF--RGRKEKVKREEVDRRVLETEEVYSAkfseEAKSICKMLLTKDPKQR 249
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
348-496 3.75e-07

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: 52.30  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADQHVGLRlpfnSSSVerGGNGSLMAPEVSTAHSgpsav 427
Cdd:cd05589  113 GLQFLHEHKIVYRDLKLDNLLL--DTEG--YVKIADFGLCKEGMGFGDR----TSTF--CGTPEFLAPEVLTDTS----- 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126215545 428 idYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHL-ESRSYQEAQLPEMpesVPPEARRLVRSLLQREASKR 496
Cdd:cd05589  178 --YTRAvDWWGLGVLIYEMLVGESPFPGDDEEEVfDSIVNDEVRYPRF---LSTEAISIMRRLLRKNPERR 243
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
245-498 3.78e-07

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: 51.90  E-value: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 245 RVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPllPGAladYPDMLPPHYYPEGlghgrTLFLVMKNypcTL 324
Cdd:cd14037   35 RVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSANRSG--NGV---YEVLLLMEYCKGG-----GVIDLMNQ---RL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 325 RQYLEEQtpssRLATMMTlQLLEGVD--HLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFG----CCLADQHVgLRLP 398
Cdd:cd14037  102 QTGLTES----EILKIFC-DVCEAVAamHYLKPPLIHRDLKVENVLISDSGN----YKLCDFGsattKILPPQTK-QGVT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 399 FNSSSVERGGNGSLMAPEVSTAHSGPSavIDySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYqeaQLPEMPESVP 478
Cdd:cd14037  172 YVEEDIKKYTTLQYRAPEMIDLYRGKP--IT-EKSDIWALGCLLYKLCFYTTPFEESGQLAILNGNF---TFPDNSRYSK 245
                        250       260
                 ....*....|....*....|
gi 126215545 479 PEaRRLVRSLLQREASKRPS 498
Cdd:cd14037  246 RL-HKLIRYMLEEDPEKRPN 264
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
323-445 3.89e-07

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 52.06  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 323 TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQ--------GIAHRDLKSDNILVEwdsdgcpwlviSDFGCCLADQHVG 394
Cdd:cd14143   79 SLFDYLNRYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVK-----------KNGTCCIADLGLA 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 395 LRLPFNSSSVE-----RGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEI 445
Cdd:cd14143  148 VRHDSATDTIDiapnhRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEI 203
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
314-456 4.50e-07

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: 51.84  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 314 FLVMKNYPCTLRQYLEEQTPS---SRLATMMtLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLAD 390
Cdd:cd07843   82 YMVMEYVEHDLKSLMETMKQPflqSEVKCLM-LQLLSGVAHLHDNWILHRDLKTSNLLL--NNRGI--LKICDFG--LAR 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 391 QHVGLRLPFNSSSVE---RggngslmAPEVSTahsGPSaviDYSKA-DTWAVGAIAYEIFGLANPFYGQG 456
Cdd:cd07843  155 EYGSPLKPYTQLVVTlwyR-------APELLL---GAK---EYSTAiDMWSVGCIFAELLTKKPLFPGKS 211
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
341-500 4.59e-07

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: 51.30  E-value: 4.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVD--HLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLAD-QHVGLRLPFNSSSVERGGNGSLMAPE- 416
Cdd:cd13978   98 IIHEIALGMNflHNMDPPLLHHDLKPENILLDNHFH----VKISDFG--LSKlGMKSISANRRRGTENLGGTPIYMAPEa 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VSTAHSGPSavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPE---SVPPEARRLVRSLLQREA 493
Cdd:cd13978  172 FDDFNKKPT-----SKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPSLDDigrLKQIENVQELISLMIRCW 246

                 ....*..
gi 126215545 494 SKRPSAR 500
Cdd:cd13978  247 DGNPDAR 253
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
346-500 4.61e-07

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: 51.91  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladQHVGLRLPFNSSSVergGNGSLMAPEVSTAHSGPS 425
Cdd:cd06659  127 LQALAYLHSQGVIHRDIKSDSILLTLDGR----VKLSDFGFC---AQISKDVPKRKSLV---GTPYWMAPEVISRCPYGT 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 426 AVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRsYQEAQLPEMPES--VPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd06659  197 EV------DIWSLGIMVIEMVDGEPPYFSDSPVQAMKR-LRDSPPPKLKNShkASPVLRDFLERMLVRDPQERATAQ 266
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
344-499 4.66e-07

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: 51.43  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCpwLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVstAHSG 423
Cdd:cd14114  108 QVCEGLCHMHENNIVHLDIKPENIMCTTKRSNE--VKLIDFG-------LATHLDPKESVKVTTGTAEFAAPEI--VERE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PsaVIDYSkaDTWAVGAIAYEIFGLANPFYGQGSahLESRSYQEAQLPEMPES----VPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14114  177 P--VGFYT--DMWAVGVLSYVLLSGLSPFAGEND--DETLRNVKSCDWNFDDSafsgISEEAKDFIRKLLLADPNKRMTI 250
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
344-498 4.75e-07

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: 51.17  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhVGLRL-PFNSSSVERGGNGSLMAPEV--STA 420
Cdd:cd14188  109 QIVSGLKYLHEQEILHRDLKLGNFFINENME----LKVGDFG-------LAARLePLEHRRRTICGTPNYLSPEVlnKQG 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 421 HSgpsavidySKADTWAVGAIAYEIFgLANPFYGQGSAHLESRSYQEAQLpEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14188  178 HG--------CESDIWALGCVMYTML-LGRPPFETTNLKETYRCIREARY-SLPSSLLAPAKHLIASMLSKNPEDRPS 245
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
338-511 4.79e-07

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: 51.80  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVIsDFGccladqHVGLRLPfnsssvergGNGSLMAPEV 417
Cdd:cd14180  103 ASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVI-DFG------FARLRPQ---------GSRPLQTPCF 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSGPSAVID--YSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRS------YQEAQLP---EMPESVPPEARRLV 485
Cdd:cd14180  167 TLQYAAPELFSNqgYDEScDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAadimhkIKEGDFSlegEAWKGVSEEAKDLV 246
                        170       180
                 ....*....|....*....|....*.
gi 126215545 486 RSLLQREaskrPSARLAANVLHLSLW 511
Cdd:cd14180  247 RGLLTVD----PAKRLKLSELRESDW 268
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
344-470 4.81e-07

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: 51.90  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLAdqhvglRLpFNSSSVE-RGGNGSLM-----APEV 417
Cdd:cd07842  116 QILNGIHYLHSNWVLHRDLKPANILVMGEGPERGVVKIGDLG--LA------RL-FNAPLKPlADLDPVVVtiwyrAPEL 186
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 418 --STAHsgpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQgSAHLESRS-YQEAQL 470
Cdd:cd07842  187 llGARH--------YTKAiDIWAIGCIFAELLTLEPIFKGR-EAKIKKSNpFQRDQL 234
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
348-496 4.81e-07

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: 51.67  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFG--CCLADqhvglRLPfnSSSVergGNGSLMAPEV---STAHS 422
Cdd:cd05606  110 GLEHMHNRFIVYRDLKPANILL--DEHG--HVRISDLGlaCDFSK-----KKP--HASV---GTHGYMAPEVlqkGVAYD 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 423 gpsavidySKADTWAVGAIAYEIFGLANPFYGQGSA-HLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05606  176 --------SSADWFSLGCMLYKLLKGHSPFRQHKTKdKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSKR 242
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
324-498 4.93e-07

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: 51.57  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSR-----------LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLAdqh 392
Cdd:cd05032   96 LKSYLRSRRPEAEnnpglgpptlqKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMV--AEDLT--VKIGDFG--MT--- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 393 vglRLPFNSSSVERGGNGSL----MAPEvstahSGPSAVIDySKADTWAVGAIAYEIFGLANPFYgQGSAHLESRSY-QE 467
Cdd:cd05032  167 ---RDIYETDYYRKGGKGLLpvrwMAPE-----SLKDGVFT-TKSDVWSFGVVLWEMATLAEQPY-QGLSNEEVLKFvID 236
                        170       180       190
                 ....*....|....*....|....*....|.
gi 126215545 468 AQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05032  237 GGHLDLPENCPDKLLELMRMCWQYNPKMRPT 267
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
344-498 5.22e-07

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 51.01  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQhvgLRLPfNSSSVERGGNGSLMAPEVST--AH 421
Cdd:cd14186  110 QIVTGMLYLHSHGILHRDLTLSNLLLTRNMN----IKIADFG--LATQ---LKMP-HEKHFTMCGTPNYISPEIATrsAH 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 422 SGPSavidyskaDTWAVGAIAYEIFGLANPFygqgSAHLESRSYQEAQLP--EMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14186  180 GLES--------DVWSLGCMFYTLLVGRPPF----DTDTVKNTLNKVVLAdyEMPAFLSREAQDLIHQLLRKNPADRLS 246
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
344-499 5.48e-07

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: 51.47  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDsdgCPW--LVISDFGCCladqhvglRLPFNSSSV-ERGGNGSLMAPEVSTA 420
Cdd:cd14197  119 QILEGVSFLHNNNVVHLDLKPQNILLTSE---SPLgdIKIVDFGLS--------RILKNSEELrEIMGTPEYVAPEILSY 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPSAvidyskADTWAVGAIAYEIFGLANPFYGQGSAHL------ESRSYQEAQLPEMPESvppeARRLVRSLLQREAS 494
Cdd:cd14197  188 EPISTA------TDMWSIGVLAYVMLTGISPFLGDDKQETflnisqMNVSYSEEEFEHLSES----AIDFIKTLLIKKPE 257

                 ....*
gi 126215545 495 KRPSA 499
Cdd:cd14197  258 NRATA 262
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
266-498 5.54e-07

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: 51.26  E-value: 5.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSSVPLlpgaladypdmlpphYYPEGLGHGRTLF-LVMKNypctlRQYLEEQTPSSRLAtmmtlQ 344
Cdd:cd14074   57 KLVQHPNVVRLYEVIDTQTKL---------------YLILELGDGGDMYdYIMKH-----ENGLNEDLARKYFR-----Q 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNIlVEWDSDGCpwLVISDFGccladqhvglrlpFnSSSVERGGN-----GSLM--APEV 417
Cdd:cd14074  112 IVSAISYCHKLHVVHRDLKPENV-VFFEKQGL--VKLTDFG-------------F-SNKFQPGEKletscGSLAysAPEI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSgpsavIDYSKADTWAVGAIAYEIFGLANPFygqgsahlesrsyQEAQLPE-----------MPESVPPEARRLVR 486
Cdd:cd14074  175 LLGDE-----YDAPAVDIWSLGVILYMLVCGQPPF-------------QEANDSEtltmimdckytVPAHVSPECKDLIR 236
                        250
                 ....*....|..
gi 126215545 487 SLLQREASKRPS 498
Cdd:cd14074  237 RMLIRDPKKRAS 248
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
344-496 5.55e-07

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: 51.43  E-value: 5.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqhvgLRLPFNSSSVerGGNGSLMAPEVSTaHSG 423
Cdd:cd05580  109 EVVLALEYLHSLDIVYRDLKPENLLL--DSDG--HIKITDFGFA-------KRVKDRTYTL--CGTPEYLAPEIIL-SKG 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 424 psavidYSKA-DTWAVGAIAYEIFGLANPFYGQGsahlESRSYQ---EAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05580  175 ------HGKAvDWWALGILIYEMLAGYPPFFDEN----PMKIYEkilEGKI-RFPSFFDPDAKDLIKRLLVVDLTKR 240
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
344-503 5.65e-07

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: 51.80  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADqhvglrLPFNSSSVERGGNGSLMAPEVSTAHSG 423
Cdd:cd05586  104 ELVLALEHLHKNDIVYRDLKPENILL--DANG--HIALCDFGLSKAD------LTDNKTTNTFCGTTEYLAPEVLLDEKG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSAVIDYskadtWAVGAIAYEIFGLANPFYGQGSAHLESR-SYQEAQLPEmpESVPPEARRLVRSLLQREaskrPSARLA 502
Cdd:cd05586  174 YTKMVDF-----WSLGVLVFEMCCGWSPFYAEDTQQMYRNiAFGKVRFPK--DVLSDEGRSFVKGLLNRN----PKHRLG 242

                 .
gi 126215545 503 A 503
Cdd:cd05586  243 A 243
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
314-498 6.55e-07

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: 51.00  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 314 FLVM-KNYPCT-LRQYLEEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdGCPWLVisDFgcclad 390
Cdd:cd14101   83 LLVLeRPQHCQdLFDYITERGAlDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRT-GDIKLI--DF------ 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 391 qhvglrlpfnsssvergGNGSLMAPEVSTAHSG-----PSAVIDYSK-----ADTWAVGAIAYEIFGLANPFYgQGSAHL 460
Cdd:cd14101  154 -----------------GSGATLKDSMYTDFDGtrvysPPEWILYHQyhalpATVWSLGILLYDMVCGDIPFE-RDTDIL 215
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 126215545 461 ESRsyqeaqlPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14101  216 KAK-------PSFNKRVSNDCRSLIRSCLAYNPSDRPS 246
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
340-496 6.73e-07

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: 51.46  E-value: 6.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 340 MMTL-----------------QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCC--LADQHvglrLPFn 400
Cdd:cd05599   88 MMTLlmkkdtlteeetrfyiaETVLAIESIHKLGYIHRDIKPDNLLL--DARG--HIKLSDFGLCtgLKKSH----LAY- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 401 sSSVergGNGSLMAPEVSTaHSGpsavidYSK-ADTWAVGAIAYEIFGLANPFYgqgsahleSRSYQEAQL--------- 470
Cdd:cd05599  159 -STV---GTPDYIAPEVFL-QKG------YGKeCDWWSLGVIMYEMLIGYPPFC--------SDDPQETCRkimnwretl 219
                        170       180
                 ....*....|....*....|....*....
gi 126215545 471 ---PEMPesVPPEARRLVRSLLQrEASKR 496
Cdd:cd05599  220 vfpPEVP--ISPEAKDLIERLLC-DAEHR 245
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
324-453 7.15e-07

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: 51.07  E-value: 7.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLATMMTLQ-LLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhVGLRLPFNSS 402
Cdd:cd14182   97 LFDYLTEKVTLSEKETRKIMRaLLEVICALHKLNIVHRDLKPENILLDDDMN----IKLTDFG-------FSCQLDPGEK 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 403 SVERGGNGSLMAPEV-----STAHSGpsavidYSKA-DTWAVGAIAYEIFGLANPFY 453
Cdd:cd14182  166 LREVCGTPGYLAPEIiecsmDDNHPG------YGKEvDMWSTGVIMYTLLAGSPPFW 216
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
334-499 7.39e-07

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: 50.76  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFgccladqhvGLRLPFNSSSVERGGNGSLM 413
Cdd:cd14183  102 TERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDF---------GLATVVDGPLYTVCGTPTYV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVsTAHSGPSAvidysKADTWAVGAIAYEIFGLANPFYGQG---SAHLESRSYQEAQLPeMP--ESVPPEARRLVRSL 488
Cdd:cd14183  173 APEI-IAETGYGL-----KVDIWAAGVITYILLCGFPPFRGSGddqEVLFDQILMGQVDFP-SPywDNVSDSAKELITMM 245
                        170
                 ....*....|.
gi 126215545 489 LQREASKRPSA 499
Cdd:cd14183  246 LQVDVDQRYSA 256
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
314-446 7.99e-07

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: 50.82  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 314 FLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQ---------GIAHRDLKSDNILVEwdSDG-CpwlVIS 382
Cdd:cd14054   70 LLVLEYAPKgSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVK--ADGsC---VIC 144
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 383 DFGC----CLADQHVGLRLPFNSSSVERGGNGSLMAPEV----STAHSGPSAVidySKADTWAVGAIAYEIF 446
Cdd:cd14054  145 DFGLamvlRGSSLVRGRPGAAENASISEVGTLRYMAPEVlegaVNLRDCESAL---KQVDVYALGLVLWEIA 213
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
328-499 8.10e-07

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: 50.69  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 328 LEEQTPSSRLaTMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGCPW--LVISDFGCCLADQHVG-LRlpfnsssv 404
Cdd:cd14198  103 LAEMVSENDI-IRLIRQILEGVYYLHQNNIVHLDLKPQNILL---SSIYPLgdIKIVDFGMSRKIGHACeLR-------- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 ERGGNGSLMAPEVSTAHSGPSAvidyskADTWAVGAIAYEIFGLANPFYGQGS--AHLESRSYQEAQLPEMPESVPPEAR 482
Cdd:cd14198  171 EIMGTPEYLAPEILNYDPITTA------TDMWNIGVIAYMLLTHESPFVGEDNqeTFLNISQVNVDYSEETFSSVSQLAT 244
                        170
                 ....*....|....*..
gi 126215545 483 RLVRSLLQREASKRPSA 499
Cdd:cd14198  245 DFIQKLLVKNPEKRPTA 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
344-451 8.23e-07

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: 50.80  E-value: 8.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLAdqhvglrlpfNSSSVERG----GNGSLMAPEVST 419
Cdd:cd06643  111 QTLEALVYLHENKIIHRDLKAGNILFTLDGD----IKLADFGVSAK----------NTRTLQRRdsfiGTPYWMAPEVVM 176
                         90       100       110
                 ....*....|....*....|....*....|..
gi 126215545 420 AHSGPSAVIDYsKADTWAVGAIAYEIFGLANP 451
Cdd:cd06643  177 CETSKDRPYDY-KADVWSLGVTLIEMAQIEPP 207
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
342-504 8.34e-07

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: 50.67  E-value: 8.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwlvisdfGCCLADQHVGLRLPFNSSSVERGGNGSLMAPEVSTAH 421
Cdd:cd05607  110 SAQITCGILHLHSLKIVYRDMKPENVLL--DDNG---------NCRLSDLGLAVEVKEGKPITQRAGTNGYMAPEILKEE 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGPSAVidyskaDTWAVGAIAYEIFGLANPFygqgSAHLESRSYQEAQLPEMPESV-------PPEARRLVRSLLqreaS 494
Cdd:cd05607  179 SYSYPV------DWFAMGCSIYEMVAGRTPF----RDHKEKVSKEELKRRTLEDEVkfehqnfTEEAKDICRLFL----A 244
                        170
                 ....*....|
gi 126215545 495 KRPSARLAAN 504
Cdd:cd05607  245 KKPENRLGSR 254
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
344-500 8.38e-07

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: 50.88  E-value: 8.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQhvglrlPFNSSSVERGGNGSLMAPEVSTAHS- 422
Cdd:cd06656  123 ECLQALDFLHSNQVIHRDIKSDNILLGMDGS----VKLTDFGFCAQIT------PEQSKRSTMVGTPYWMAPEVVTRKAy 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAH----LESRSYQEAQLPEMPESVppeARRLVRSLLQREASKRPS 498
Cdd:cd06656  193 GP-------KVDIWSLGIMAIEMVEGEPPYLNENPLRalylIATNGTPELQNPERLSAV---FRDFLNRCLEMDVDRRGS 262

                 ..
gi 126215545 499 AR 500
Cdd:cd06656  263 AK 264
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
344-452 8.52e-07

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: 50.78  E-value: 8.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLA-DQHVGLRLPFNsssvergGNGSLMAPEVSTAHS 422
Cdd:cd06636  129 EILRGLAHLHAHKVIHRDIKGQNVLLTENAE----VKLVDFGVSAQlDRTVGRRNTFI-------GTPYWMAPEVIACDE 197
                         90       100       110
                 ....*....|....*....|....*....|
gi 126215545 423 GPSAVIDYsKADTWAVGAIAYEIFGLANPF 452
Cdd:cd06636  198 NPDATYDY-RSDIWSLGITAIEMAEGAPPL 226
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
325-500 8.78e-07

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: 51.12  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 325 RQYLEeqtPSSRLatmMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqHVGLRLPFNSSSV 404
Cdd:cd05603   91 RCFLE---PRARF---YAAEVASAIGYLHSLNIIYRDLKPENILL--DCQG--HVVLTDFGLC----KEGMEPEETTSTF 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 erGGNGSLMAPEVSTAHSGPSAVidyskaDTWAVGAIAYE-IFGLAnPFYGQGSAHL-ESRSYQEAQLpemPESVPPEAR 482
Cdd:cd05603  157 --CGTPEYLAPEVLRKEPYDRTV------DWWCLGAVLYEmLYGLP-PFYSRDVSQMyDNILHKPLHL---PGGKTVAAC 224
                        170
                 ....*....|....*...
gi 126215545 483 RLVRSLLQREASKRPSAR 500
Cdd:cd05603  225 DLLQGLLHKDQRRRLGAK 242
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
315-498 9.81e-07

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: 50.31  E-value: 9.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 315 LVM-KNYPC-TLRQYLEEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDsDGCPWLVisDFGCcladq 391
Cdd:cd14005   83 LIMeRPEPCqDLFDFITERGAlSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLR-TGEVKLI--DFGC----- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 392 hvGLRLPfNSSSVERGGNGSLMAPEV---STAHSGPSAVidyskadtWAVGAIAYEIFGLANPFygqgsahlESRSYQEA 468
Cdd:cd14005  155 --GALLK-DSVYTDFDGTRVYSPPEWirhGRYHGRPATV--------WSLGILLYDMLCGDIPF--------ENDEQILR 215
                        170       180       190
                 ....*....|....*....|....*....|
gi 126215545 469 QLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14005  216 GNVLFRPRLSKECCDLISRCLQFDPSKRPS 245
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
343-499 1.01e-06

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: 50.81  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGcpWLVISDFGCCladQHVGLRLPFNSSSVergGNGSLMAPEVStahs 422
Cdd:cd06658  125 LSVLRALSYLHNQGVIHRDIKSDSILLT--SDG--RIKLSDFGFC---AQVSKEVPKRKSLV---GTPYWMAPEVI---- 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 423 gpSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHlESRSYQEAQLPEMPES--VPPEARRLVRSLLQREASKRPSA 499
Cdd:cd06658  191 --SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQ-AMRRIRDNLPPRVKDShkVSSVLRGFLDLMLVREPSQRATA 266
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
333-498 1.02e-06

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: 50.37  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 333 PSSRlATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwLVISDFGccLADQhvglrLPFNSSSVERG--GNG 410
Cdd:cd14163   99 PEHR-AKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT-----LKLTDFG--FAKQ-----LPKGGRELSQTfcGST 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 411 SLMAPEV--STAHsgpsaviDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMpESVPPEARRLVRSL 488
Cdd:cd14163  166 AYAAPEVlqGVPH-------DSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGVSLPGH-LGVSRTCQDLLKRL 237
                        170
                 ....*....|
gi 126215545 489 LQREASKRPS 498
Cdd:cd14163  238 LEPDMVLRPS 247
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
341-500 1.09e-06

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: 50.13  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEgvdhlvQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGCCladqhvglRLPFNSSSVE--RGGNGSLMAPEVS 418
Cdd:cd08223  113 MALQYMH------ERNILHRDLKTQNIFLTKSN----IIKVGDLGIA--------RVLESSSDMAttLIGTPYYMSPELF 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TahSGPsavidYS-KADTWAVGAIAYEIFGLANPFygqGSAHLESRSYQ--EAQLPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd08223  175 S--NKP-----YNhKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYKilEGKLPPMPKQYSPELGELIKAMLHQDPEK 244

                 ....*
gi 126215545 496 RPSAR 500
Cdd:cd08223  245 RPSVK 249
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
344-498 1.17e-06

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: 50.31  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhVGLRL-PFNSSSVERGGNGSLMAPEV--STA 420
Cdd:cd14189  109 QIISGLKYLHLKGILHRDLKLGNFFINENME----LKVGDFG-------LAARLePPEQRKKTICGTPNYLAPEVllRQG 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 421 HsGPsavidysKADTWAVGAIAYEIFGLANPFygQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14189  178 H-GP-------ESDVWSLGCVMYTLLCGNPPF--ETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLT 245
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
270-496 1.17e-06

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: 50.16  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglgHGRtLFLVMK-NYPCTLRQYLEEQ-TPSSRLATMMTLQLLE 347
Cdd:cd14165   60 HKSIIKTYEIFETS-------------------------DGK-VYIVMElGVQGDLLEFIKLRgALPEDVARKMFHQLSS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhvglrlpFnSSSVERGGNGSLMAPEV---STAHSGP 424
Cdd:cd14165  114 AIKYCHELDIVHRDLKCENLLLDKDFN----IKLTDFG-------------F-SKRCLRDENGRIVLSKTfcgSAAYAAP 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 425 SAV----IDYSKADTWAVGAIAYEIFGLANPFygQGSAHLESRSYQEAQLPEMPESV--PPEARRLVRSLLQREASKR 496
Cdd:cd14165  176 EVLqgipYDPRIYDIWSLGVILYIMVCGSMPY--DDSNVKKMLKIQKEHRVRFPRSKnlTSECKDLIYRLLQPDVSQR 251
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
405-511 1.18e-06

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 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 TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 50.05  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 405 ERGGNGSLMAPEV---STAHSGPSAvidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRsYQEAQLPeMPESVPPEA 481
Cdd:cd14023  145 DKHGCPAYVSPEIlntTGTYSGKSA-------DVWSLGVMLYTLLVGRYPFHDSDPSALFSK-IRRGQFC-IPDHVSPKA 215
                         90       100       110
                 ....*....|....*....|....*....|
gi 126215545 482 RRLVRSLLQREaskrPSARLAANVLHLSLW 511
Cdd:cd14023  216 RCLIRSLLRRE----PSERLTAPEILLHPW 241
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
329-496 1.19e-06

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: 50.18  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLADQhvglrlpfnsssVERG- 407
Cdd:cd14105  101 EKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFG--LAHK------------IEDGn 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 408 ------GNGSLMAPEVSTAHS-GPsavidysKADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAQlpEMPES 476
Cdd:cd14105  167 efknifGTPEFVAPEIVNYEPlGL-------EADMWSIGVITYILLSGASPFLGDTKqetlANITAVNYDFDD--EYFSN 237
                        170       180
                 ....*....|....*....|
gi 126215545 477 VPPEARRLVRSLLQREASKR 496
Cdd:cd14105  238 TSELAKDFIRQLLVKDPRKR 257
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
270-524 1.26e-06

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: 50.42  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghgRT-----LFLVMKNYPCTLRQYLEEQ----TPSSRLATM 340
Cdd:cd07862   63 HPNVVRLFDVCTVS---------------------------RTdretkLTLVFEHVDQDLTTYLDKVpepgVPTETIKDM 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MtLQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGcpWLVISDFGCC------LADQHVGLRLPFNsssverggngslmA 414
Cdd:cd07862  116 M-FQLLRGLDFLHSHRVVHRDLKPQNILVT--SSG--QIKLADFGLAriysfqMALTSVVVTLWYR-------------A 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEmPESVPPEArrlvrSLLQREAS 494
Cdd:cd07862  178 PEVLLQSSYATPV------DLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPG-EEDWPRDV-----ALPRQAFH 245
                        250       260       270
                 ....*....|....*....|....*....|
gi 126215545 495 KRPSARLAANVLHLSLWGEHLLalknLKLD 524
Cdd:cd07862  246 SKSAQPIEKFVTDIDELGKDLL----LKCL 271
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
344-497 1.27e-06

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: 50.02  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwdsDGcpWLV-ISDFGccLADqhVGLRLPFNSSSVERGGNGSLMAPEV-STAH 421
Cdd:cd14150  104 QTAQGMDYLHAKNIIHRDLKSNNIFLH---EG--LTVkIGDFG--LAT--VKTRWSGSQQVEQPSGSILWMAPEViRMQD 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGPsavidYS-KADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14150  175 TNP-----YSfQSDVYAYGVVLYELMSGTLPYSNINNrdqiIFMVGRGYLSPDLSKLSSNCPKAMKRLLIDCLKFKREER 249

                 .
gi 126215545 497 P 497
Cdd:cd14150  250 P 250
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
348-496 1.29e-06

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: 50.77  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADQHVGLrlpfnsSSVERGGNGSLMAPEVstahsgpSAV 427
Cdd:cd05615  123 GLFFLHKKGIIYRDLKLDNVML--DSEG--HIKIADFGMCKEHMVEGV------TTRTFCGTPDYIAPEI-------IAY 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 428 IDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLeSRSYQEAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05615  186 QPYGRSvDWWAYGVLLYEMLAGQPPFDGEDEDEL-FQSIMEHNV-SYPKSLSKEAVSICKGLMTKHPAKR 253
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
270-461 1.35e-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: 50.80  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpGALADYPDmlpphyypeglghgrtLFLVMKNYPCTLRQYLEEQTPSSRLATMMtLQLLEGV 349
Cdd:cd07876   79 HKNIISLLNVFTPQ-----KSLEEFQD----------------VYLVMELMDANLCQVIHMELDHERMSYLL-YQMLCGI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQHVGLRLPFNSSSVERggngslmAPEVSTAHSGPSAVid 429
Cdd:cd07876  137 KHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTACTNFMMTPYVVTRYYR-------APEVILGMGYKENV-- 203
                        170       180       190
                 ....*....|....*....|....*....|..
gi 126215545 430 yskaDTWAVGAIAYEIFGLANPFygQGSAHLE 461
Cdd:cd07876  204 ----DIWSVGCIMGELVKGSVIF--QGTDHID 229
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
345-496 1.36e-06

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: 50.05  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCClaDQHVGLRLpFNSSSVergGNGSLMAPEVSTahsgP 424
Cdd:cd14118  124 IVLGIEYLHYQKIIHRDIKPSNLLL--GDDG--HVKIADFGVS--NEFEGDDA-LLSSTA---GTPAFMAPEALS----E 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 425 SAVIDYSKA-DTWAVGAIAYE-IFGlANPFYGQGSAHLESR-SYQEAQLPEMPeSVPPEARRLVRSLLQREASKR 496
Cdd:cd14118  190 SRKKFSGKAlDIWAMGVTLYCfVFG-RCPFEDDHILGLHEKiKTDPVVFPDDP-VVSEQLKDLILRMLDKNPSER 262
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
322-507 1.38e-06

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: 50.11  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 322 CTLRQYLEEQTPSSRLATM----MTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLV-ISDFGccLAdqhvglR 396
Cdd:cd05044   88 SYLRAARPTAFTPPLLTLKdllsICVDVAKGCVYLEDMHFVHRDLAARNCLVS-SKDYRERVVkIGDFG--LA------R 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 397 LPFNSSSVERGGNGSL----MAPE-----VSTAHSgpsavidyskaDTWAVGAIAYEIFGLANPFYgQGSAHLESRSY-- 465
Cdd:cd05044  159 DIYKNDYYRKEGEGLLpvrwMAPEslvdgVFTTQS-----------DVWAFGVLMWEILTLGQQPY-PARNNLEVLHFvr 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 126215545 466 QEAQLpEMPESVPPEARRLVRSLLQREASKRPSARLAANVLH 507
Cdd:cd05044  227 AGGRL-DQPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
305-496 1.44e-06

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: 49.99  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 305 EGLGHG-RTLFLVMKnypC-------TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNIL-VEWDSDG 375
Cdd:cd14172   67 ENMHHGkRCLLIIME---CmeggelfSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLyTSKEKDA 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 376 CpwLVISDFGCCL-ADQHVGLRLPFNSSsverggngSLMAPEVstahSGPSaviDYSKA-DTWAVGAIAYEIFGLANPFY 453
Cdd:cd14172  144 V--LKLTDFGFAKeTTVQNALQTPCYTP--------YYVAPEV----LGPE---KYDKScDMWSLGVIMYILLCGFPPFY 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 126215545 454 ---GQGSAHLESRSYQEAQL----PEMPEsVPPEARRLVRSLLQREASKR 496
Cdd:cd14172  207 sntGQAISPGMKRRIRMGQYgfpnPEWAE-VSEEAKQLIRHLLKTDPTER 255
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
344-498 1.55e-06

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: 50.06  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQHVGLRLPFNSSSvergGNGSLMAPEV-STAHS 422
Cdd:cd14151  112 QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT----VKIGDFGLATVKSRWSGSHQFEQLS----GSILWMAPEViRMQDK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPsavidYS-KADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd14151  184 NP-----YSfQSDVYAFGIVLYELMTGQLPYSNINNrdqiIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERP 258

                 .
gi 126215545 498 S 498
Cdd:cd14151  259 L 259
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
342-496 1.65e-06

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: 49.53  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVisDFGCcladqhvglrlpfnSSSVERG-------GNGSLMA 414
Cdd:cd05572   99 TACVVLAFEYLHSRGIIYRDLKPENLLL--DSNGYVKLV--DFGF--------------AKKLGSGrktwtfcGTPEYVA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEVSTAHSgpsavIDYSkADTWAVGAIAYEIFGLANPFygQGSAHLESRSYQE-----AQLpEMPESVPPEARRLVRSLL 489
Cdd:cd05572  161 PEIILNKG-----YDFS-VDYWSLGILLYELLTGRPPF--GGDDEDPMKIYNIilkgiDKI-EFPKYIDKNAKNLIKQLL 231

                 ....*..
gi 126215545 490 QREASKR 496
Cdd:cd05572  232 RRNPEER 238
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
344-502 1.73e-06

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: 49.53  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNIL-VEWDSDGcpwLVISDFGccLADQHV---GLRLPFnsssvergGNGSLMAPEvst 419
Cdd:cd14193  110 QICEGIQYMHQMYILHLDLKPENILcVSREANQ---VKIIDFG--LARRYKpreKLRVNF--------GTPEFLAPE--- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 ahsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGSAHLESR------SYQEAQLPEMPEsvppEARRLVRSLL 489
Cdd:cd14193  174 -------VVNYEfvsfPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNilacqwDFEDEEFADISE----EAKDFISKLL 242
                        170
                 ....*....|...
gi 126215545 490 QREASKRPSARLA 502
Cdd:cd14193  243 IKEKSWRMSASEA 255
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
310-500 1.74e-06

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: 50.11  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCL 388
Cdd:cd06655   88 GDELFVVMEYLAGgSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGS----VKLTDFGFCA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQhvglrlPFNSSSVERGGNGSLMAPEVSTAHS-GPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAH----LESR 463
Cdd:cd06655  164 QIT------PEQSKRSTMVGTPYWMAPEVVTRKAyGP-------KVDIWSLGIMAIEMVEGEPPYLNENPLRalylIATN 230
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126215545 464 SYQEAQlpeMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd06655  231 GTPELQ---NPEKLSPIFRDFLNRCLEMDVEKRGSAK 264
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
338-501 1.77e-06

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: 49.99  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEV 417
Cdd:cd05631  104 AIFYAAELCCGLEDLQRERIVYRDLKPENILL----DDRGHIRISDLG-------LAVQIPEGETVRGRVGTVGYMAPEV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSgpsavidYS-KADTWAVGAIAYEIFGLANPF--YGQGSAHLE-SRSYQEAQlPEMPESVPPEARRLVRSLLqrea 493
Cdd:cd05631  173 INNEK-------YTfSPDWWGLGCLIYEMIQGQSPFrkRKERVKREEvDRRVKEDQ-EEYSEKFSEDAKSICRMLL---- 240

                 ....*...
gi 126215545 494 SKRPSARL 501
Cdd:cd05631  241 TKNPKERL 248
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
312-500 1.77e-06

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: 49.82  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 312 TLFLVMKNYPCtLRQYLEEQT--PSSRlATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGCPWLVISDFGCCLA 389
Cdd:cd13991   74 NIFMDLKEGGS-LGQLIKEQGclPEDR-ALHYLGQALEGLEYLHSRKILHGDVKADNVLL---SSDGSDAFLCDFGHAEC 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 390 DQHVGLrlpfnSSSVERG----GNGSLMAPEVSTAHSGPsavidySKADTWAVGAIAYEIFGLANPF--YGQGSAHLESR 463
Cdd:cd13991  149 LDPDGL-----GKSLFTGdyipGTETHMAPEVVLGKPCD------AKVDVWSSCCMMLHMLNGCHPWtqYYSGPLCLKIA 217
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126215545 464 SyQEAQLPEMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd13991  218 N-EPPPLREIPPSCAPLTAQAIQAGLRKEPVHRASAA 253
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
265-507 1.91e-06

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 49.71  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLApHPNIIRvFRAFTSSvpllpgaladypdmlpphyyPEGlghgrTLFLVMKNYPCTLRQYLEEQT-------PSSRL 337
Cdd:cd14001   60 KSLN-HPNIVG-FRAFTKS--------------------EDG-----SLCLAMEYGGKSLNDLIEERYeaglgpfPAATI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMtLQLLEGVDHLVQQG-IAHRDLKSDNILVEWDSDGCPwlvISDFGccladqhVGLRLPFNSSSVERG-----GNGS 411
Cdd:cd14001  113 LKVA-LSIARALEYLHNEKkILHGDIKSGNVLIKGDFESVK---LCDFG-------VSLPLTENLEVDSDPkaqyvGTEP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 412 LMAPEvstAHSGPSAVIDysKADTWAVGAIAYEIFGLANP--FYGQGSAHLESRSYQE---------AQLPEMP----ES 476
Cdd:cd14001  182 WKAKE---ALEEGGVITD--KADIFAYGLVLWEMMTLSVPhlNLLDIEDDDEDESFDEdeedeeayyGTLGTRPalnlGE 256
                        250       260       270
                 ....*....|....*....|....*....|....
gi 126215545 477 VPPEARRLVR---SLLQREASKRPSARLAANVLH 507
Cdd:cd14001  257 LDDSYQKVIElfyACTQEDPKDRPSAAHIVEALE 290
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
343-498 2.06e-06

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: 49.66  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIA---HRDLKSDNIL----VEWDSDGCPWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSLMAP 415
Cdd:cd14145  111 VQIARGMNYLHCEAIVpviHRDLKSSNILilekVENGDLSNKILKITDFG--LA------REWHRTTKMSAAGTYAWMAP 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQLPeMPESVPPEARRLVRSLLQREA 493
Cdd:cd14145  183 EVIRSSM-------FSKgSDVWSYGVLLWELLTGEVPFRGiDGLAVAYGVAMNKLSLP-IPSTCPEPFARLMEDCWNPDP 254

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd14145  255 HSRPP 259
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
298-496 2.09e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 50.42  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 298 LPPHYYPEGLGHG-RTLFL--VMKNYPCTLRQYLEEQTPSSR-----LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILV 369
Cdd:PTZ00036 124 LKDYYYTECFKKNeKNIFLnvVMEFIPQTVHKYMKHYARNNHalplfLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 370 EWDSDGcpwLVISDFGCC---LADQHvglRLPFNSSSVERggngslmAPEVSTAHSGPSAVIDYskadtWAVGAIAYEIF 446
Cdd:PTZ00036 204 DPNTHT---LKLCDFGSAknlLAGQR---SVSYICSRFYR-------APELMLGATNYTTHIDL-----WSLGCIIAEMI 265
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 447 gLANP-FYGQGSAHLESRSYQ------EAQLPEM---------------------PESVPPEARRLVRSLLQREASKR 496
Cdd:PTZ00036 266 -LGYPiFSGQSSVDQLVRIIQvlgtptEDQLKEMnpnyadikfpdvkpkdlkkvfPKGTPDDAINFISQFLKYEPLKR 342
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
344-496 2.27e-06

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: 50.08  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqHVGLRlpfNSSSVER-GGNGSLMAPEVSTAHs 422
Cdd:cd05593  123 EIVSALDYLHSGKIVYRDLKLENLML--DKDG--HIKITDFGLC----KEGIT---DAATMKTfCGTPEYLAPEVLEDN- 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 423 gpsaviDYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAqlPEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05593  191 ------DYGRAvDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED--IKFPRTLSADAKSLLSGLLIKDPNKR 257
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
344-506 2.28e-06

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: 49.27  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPwlvISDFGCCLA---DQHV---GLRLPFNSSSVERGGNGSLMApev 417
Cdd:cd05072  112 QIAEGMAYIERKNYIHRDLRAANVLVS-ESLMCK---IADFGLARViedNEYTareGAKFPIKWTAPEAINFGSFTI--- 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsavidysKADTWAVGAIAYEIFGLAN-PFYGQGSAHLESRSYQEAQLPEMpESVPPEARRLVRSLLQREASKR 496
Cdd:cd05072  185 --------------KSDVWSFGILLYEIVTYGKiPYPGMSNSDVMSALQRGYRMPRM-ENCPDELYDIMKTCWKEKAEER 249
                        170
                 ....*....|
gi 126215545 497 PSARLAANVL 506
Cdd:cd05072  250 PTFDYLQSVL 259
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
305-445 2.33e-06

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 49.65  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 305 EGLGHGRTLFLVMKNYP-CTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQ--------GIAHRDLKSDNILVEwdsdg 375
Cdd:cd14220   60 KGTGSWTQLYLITDYHEnGSLYDFLKCTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIK----- 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 376 cpwlviSDFGCCLADqhVGLRLPFNSSSVE-------RGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEI 445
Cdd:cd14220  135 ------KNGTCCIAD--LGLAVKFNSDTNEvdvplntRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEM 203
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
344-500 2.46e-06

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: 49.34  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQhvglrlPFNSSSVERGGNGSLMAPEVSTAHS- 422
Cdd:cd06654  124 ECLQALEFLHSNQVIHRDIKSDNILLGMDGS----VKLTDFGFCAQIT------PEQSKRSTMVGTPYWMAPEVVTRKAy 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 423 GPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAH----LESRSYQEAQLPEMPESVppeARRLVRSLLQREASKRPS 498
Cdd:cd06654  194 GP-------KVDIWSLGIMAIEMIEGEPPYLNENPLRalylIATNGTPELQNPEKLSAI---FRDFLNRCLEMDVEKRGS 263

                 ..
gi 126215545 499 AR 500
Cdd:cd06654  264 AK 265
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
334-496 2.62e-06

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: 49.36  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVE-----------WDSDGCPWLV------------------ISDF 384
Cdd:cd14096  104 SEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklRKADDDETKVdegefipgvggggigivkLADF 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GccLAdqhvglRLPFNSSSVERGGNGSLMAPEVSTAHSgpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLE-- 461
Cdd:cd14096  184 G--LS------KQVWDSNTKTPCGTVGYTAPEVVKDER-------YSKKvDMWALGCVLYTLLCGFPPFYDESIETLTek 248
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 126215545 462 -SRSYQEAQLPEMPEsVPPEARRLVRSLLQREASKR 496
Cdd:cd14096  249 iSRGDYTFLSPWWDE-ISKSAKDLISHLLTVDPAKR 283
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
305-445 2.73e-06

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 49.28  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 305 EGLGHGRTLFLVMKNYP-CTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQ--------GIAHRDLKSDNILVEWDSdg 375
Cdd:cd14219   70 KGTGSWTQLYLITDYHEnGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNG-- 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126215545 376 cpwlvisdfGCCLADqhVGLRLPFNSSSVE-------RGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEI 445
Cdd:cd14219  148 ---------TCCIAD--LGLAVKFISDTNEvdippntRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEV 213
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
338-530 2.95e-06

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: 49.08  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGvdhlvQQGIAHRDLKSDNILVewDSDG----CPWLVISDFGCCLADQHVGLRlpfnsssverggngSLM 413
Cdd:cd06622  110 AVVKGLKFLKE-----EHNIIHRDVKPTNVLV--NGNGqvklCDFGVSGNLVASLAKTNIGCQ--------------SYM 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEvSTAHSGPSAVIDYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESR--SYQEAQLPEMPESVPPEARRLVRSLLQ 490
Cdd:cd06622  169 APE-RIKSGGPNQNPTYTvQSDVWSLGLSILEMALGRYPYPPETYANIFAQlsAIVDGDPPTLPSGYSDDAQDFVAKCLN 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 126215545 491 REASKRPS-ARLAanvlhlslwgEH--LLALKNLKLDkMIAWL 530
Cdd:cd06622  248 KIPNRRPTyAQLL----------EHpwLVKYKNADVD-MAEWV 279
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
350-496 2.95e-06

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 49.43  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccladqhvglrlpFNSSSVERG----GNGSLMAPEVSTAHSGPS 425
Cdd:PTZ00263 132 EYLHSKDIIYRDLKPENLLL--DNKGH--VKVTDFG-------------FAKKVPDRTftlcGTPEYLAPEVIQSKGHGK 194
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 426 AVidyskaDTWAVGAIAYEIFGLANPFYGQGSAhlesRSYQ---EAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:PTZ00263 195 AV------DWWTMGVLLYEFIAGYPPFFDDTPF----RIYEkilAGRL-KFPNWFDGRARDLVKGLLQTDHTKR 257
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
317-500 3.06e-06

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: 48.88  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 317 MKNYPCTLRQYLEEQtpssrlATMMTLQLLEGVDHLVQQGIAHRDLK--------SDNILVEWDSdgcpwlvisdfgccL 388
Cdd:cd14022   71 MHSFVRTCKKLREEE------AARLFYQIASAVAHCHDGGLVLRDLKlrkfvfkdEERTRVKLES--------------L 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQHVgLRLPFNSSSvERGGNGSLMAPEV---STAHSGPSAvidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRsY 465
Cdd:cd14022  131 EDAYI-LRGHDDSLS-DKHGCPAYVSPEIlntSGSYSGKAA-------DVWSLGVMLYTMLVGRYPFHDIEPSSLFSK-I 200
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126215545 466 QEAQLpEMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd14022  201 RRGQF-NIPETLSPKAKCLIRSILRREPSERLTSQ 234
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
265-506 3.16e-06

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: 49.05  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSvpllpgaladypdmlpphyyPEGLGHGRTLFLVMKNYpC--TLRQYLEEQTPSSRLATMMT 342
Cdd:cd14036   52 KKLSGHPNIVQFCSAASIG--------------------KEESDQGQAEYLLLTEL-CkgQLVDFVKKVEAPGPFSPDTV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 L----QLLEGVDHLVQQG--IAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVglrlPFNSSSverGGNGSLMAPE 416
Cdd:cd14036  111 LkifyQTCRAVQHMHKQSppIIHRDLKIENLLI--GNQGQ--IKLCDFGSATTEAHY----PDYSWS---AQKRSLVEDE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VST----AHSGPSAVIDYS------KADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYqeaqlpempeSVPPEARR--- 483
Cdd:cd14036  180 ITRnttpMYRTPEMIDLYSnypigeKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKY----------TIPPNDTQytv 249
                        250       260
                 ....*....|....*....|....*.
gi 126215545 484 ---LVRSLLQREASKRPSARLAANVL 506
Cdd:cd14036  250 fhdLIRSTLKVNPEERLSITEIVEQL 275
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
311-518 3.46e-06

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: 49.23  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPCTLRQYLEEQTPSSRL--ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCL 388
Cdd:cd07873   73 KSLTLVFEYLDKDLKQYLDDCGNSINMhnVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE----LKLADFGLAR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQhvglrLPFNSSSverggngslmaPEVSTAHSGPSAVI----DYS-KADTWAVGAIAYE------------------- 444
Cdd:cd07873  149 AKS-----IPTKTYS-----------NEVVTLWYRPPDILlgstDYStQIDMWGVGCIFYEmstgrplfpgstveeqlhf 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 445 IFG-LANPFYGQGSAHLESRSYQEAQLPEM-PESVPPEARR-------LVRSLLQREASKRPSARLAANVLHLSLWGEHL 515
Cdd:cd07873  213 IFRiLGTPTEETWPGILSNEEFKSYNYPKYrADALHNHAPRldsdgadLLSKLLQFEGRKRISAEEAMKHPYFHSLGERI 292

                 ...
gi 126215545 516 LAL 518
Cdd:cd07873  293 HKL 295
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
311-489 3.65e-06

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: 49.62  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGCCLA 389
Cdd:cd05622  146 RYLYMVMEYMPGgDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMK 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 390 DQHVGL-RLpfnSSSVergGNGSLMAPEVSTAHSGPSAvidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQE 467
Cdd:cd05622  222 MNKEGMvRC---DTAV---GTPDYISPEVLKSQGGDGY---YGReCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH 292
                        170       180
                 ....*....|....*....|....
gi 126215545 468 AQLPEMPE--SVPPEARRLVRSLL 489
Cdd:cd05622  293 KNSLTFPDdnDISKEAKNLICAFL 316
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
344-499 3.75e-06

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: 48.58  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwDSDgcpwLV-ISDFGCC--------LADQHVGlrLPFnsssverggngsLMA 414
Cdd:cd08221  109 QIVSAVSHIHKAGILHRDIKTLNIFLT-KAD----LVkLGDFGISkvldsessMAESIVG--TPY------------YMS 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEVSTAHSgpsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQeAQLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd08221  170 PELVQGVK-------YNfKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ-GEYEDIDEQYSEEIIQLVHDCLHQDP 241

                 ....*.
gi 126215545 494 SKRPSA 499
Cdd:cd08221  242 EDRPTA 247
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
306-417 3.80e-06

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 48.91  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 306 GLGHGRTLFLVMKNYP-CTLRQYLeeqtpSSRLATMMTLQLL-----EGVDHL----VQQG-----IAHRDLKSDNILVE 370
Cdd:cd14055   67 GVGLDRQYWLITAYHEnGSLQDYL-----TRHILSWEDLCKMagslaRGLAHLhsdrTPCGrpkipIAHRDLKSSNILVK 141
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 126215545 371 WDSDgcpwlvisdfgCCLADQHVGLRLPfNSSSVERGGNGS------LMAPEV 417
Cdd:cd14055  142 NDGT-----------CVLADFGLALRLD-PSLSVDELANSGqvgtarYMAPEA 182
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
324-452 4.31e-06

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: 48.87  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLADQHvglrlpfnsss 403
Cdd:cd14175   83 LDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPESLRICDFG--FAKQL----------- 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 126215545 404 veRGGNGSLMAPEVSTAHSGPSAVI--DYSKA-DTWAVGAIAYEIFGLANPF 452
Cdd:cd14175  150 --RAENGLLMTPCYTANFVAPEVLKrqGYDEGcDIWSLGILLYTMLAGYTPF 199
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
324-498 4.99e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 49.24  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRL-ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsdgCPWLVIS--DFGccLADQHVglrlpfN 400
Cdd:PTZ00267 156 IKQRLKEHLPFQEYeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL------MPTGIIKlgDFG--FSKQYS------D 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 401 SSSVERG----GNGSLMAPEVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPeMPE 475
Cdd:PTZ00267 222 SVSLDVAssfcGTPYYLAPELWERKR-------YSKkADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDP-FPC 293
                        170       180
                 ....*....|....*....|...
gi 126215545 476 SVPPEARRLVRSLLQREASKRPS 498
Cdd:PTZ00267 294 PVSSGMKALLDPLLSKNPALRPT 316
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
277-498 5.02e-06

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 49.07  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 277 FRAFTSSVPLLPGALADYPDMLPPHYYPEG----LGHGRTLFLVMKNYPCTLRQYL----EEQTPSSRLATM-----MTL 343
Cdd:cd05106  140 FLNFVMALPEISETSSDYKNITLEKKYIRSdsgfSSQGSDTYVEMRPVSSSSSQSSdskdEEDTEDSWPLDLddllrFSS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewdSDGcPWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MAPE--- 416
Cdd:cd05106  220 QVAQGMDFLASKNCIHRDVAARNVLL---TDG-RVAKICDFG--LA------RDIMNDSNYVVKGNARLpvkwMAPEsif 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 --VSTAHSgpsavidyskaDTWAVGAIAYEIFGLA----------NPFYgqgsaHLESRSYQEAQlpemPESVPPEARRL 484
Cdd:cd05106  288 dcVYTVQS-----------DVWSYGILLWEIFSLGkspypgilvnSKFY-----KMVKRGYQMSR----PDFAPPEIYSI 347
                        250
                 ....*....|....
gi 126215545 485 VRSLLQREASKRPS 498
Cdd:cd05106  348 MKMCWNLEPTERPT 361
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
315-444 5.27e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 49.12  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 315 LVMKNYPCTLRQYLEEQT-PSSRL-ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCpwlvISDFG-CCLADq 391
Cdd:PHA03211 237 LVLPKYRSDLYTYLGARLrPLGLAqVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDIC----LGDFGaACFAR- 311
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 392 hvGLRlpfnSSSVERGGNGSL--MAPEVSTAHSGPSAVidyskaDTWAVGAIAYE 444
Cdd:PHA03211 312 --GSW----STPFHYGIAGTVdtNAPEVLAGDPYTPSV------DIWSAGLVIFE 354
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
342-502 5.60e-06

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: 48.34  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLADQHVGLRLPFNSSSVERGgngsLMAPEV--ST 419
Cdd:cd07841  108 MLMTLRGLEYLHSNWILHRDLKPNNLLI--ASDGV--LKLADFG--LARSFGSPNRKMTHQVVTRW----YRAPELlfGA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPSavidyskADTWAVGAIAYEIFgLANPFYgQGSAHLE--SRSYQ------EAQLPEM--------PESVPP---- 479
Cdd:cd07841  178 RHYGVG-------VDMWSVGCIFAELL-LRVPFL-PGDSDIDqlGKIFEalgtptEENWPGVtslpdyveFKPFPPtplk 248
                        170       180       190
                 ....*....|....*....|....*....|.
gi 126215545 480 --------EARRLVRSLLQREASKRPSARLA 502
Cdd:cd07841  249 qifpaasdDALDLLQRLLTLNPNKRITARQA 279
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
357-498 5.92e-06

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: 48.03  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 357 IAHRDLKSDNILVEwdSDGCpwLVISDFGcclADQHVGlrlpfNSSSVERGGNGSLMAPEVstAHSGPSAvidySKADTW 436
Cdd:cd14060  108 VIHRDLKSRNVVIA--ADGV--LKICDFG---ASRFHS-----HTTHMSLVGTFPWMAPEV--IQSLPVS----ETCDTY 169
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 437 AVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14060  170 SYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKERPS 231
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
343-499 6.02e-06

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: 48.09  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQ-QGIAHRDLKSDNILVewDSDGcPWlVISDFGCCLADQHVGLRLPFNSSSVERGG-----NGSLMAPE 416
Cdd:cd14011  121 LQISEALSFLHNdVKLVHGNICPESVVI--NSNG-EW-KLAGFDFCISSEQATDQFPYFREYDPNLPplaqpNLNYLAPE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VSTAHS-GPSAvidyskaDTWAVGAIAYEIFGLANPFYGQGSAHL--ESRSYQEAQLP-EMPESVPPEARRLVRSLLQRE 492
Cdd:cd14011  197 YILSKTcDPAS-------DMFSLGVLIYAIYNKGKPLFDCVNNLLsyKKNSNQLRQLSlSLLEKVPEELRDHVKTLLNVT 269

                 ....*..
gi 126215545 493 ASKRPSA 499
Cdd:cd14011  270 PEVRPDA 276
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
270-498 6.03e-06

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: 48.10  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFtssvpllpgaladypdmlpphyypEGLGHgrtLFLVMKnYPC--TLRQYLEEQTP-SSRLATMMTLQLL 346
Cdd:cd14075   60 HPNIIRLYEVV------------------------ETLSK---LHLVME-YASggELYTKISTEGKlSESEAKPLFAQIV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILveWDSDGCpwLVISDFGccladqhvglrlpFnSSSVERG-------GNGSLMAPEV-- 417
Cdd:cd14075  112 SAVKHMHENNIIHRDLKAENVF--YASNNC--VKVGDFG-------------F-STHAKRGetlntfcGSPPYAAPELfk 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSGPSavidyskADTWAVGAIAYEIFGLANPFYGQGSAHLESR----SYQeaqlpeMPESVPPEARRLVRSLLQREA 493
Cdd:cd14075  174 DEHYIGIY-------VDIWALGVLLYFMVTGVMPFRAETVAKLKKCilegTYT------IPSYVSEPCQELIRGILQPVP 240

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd14075  241 SDRYS 245
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
342-497 6.27e-06

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: 48.46  E-value: 6.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MAPEv 417
Cdd:cd14207  186 SFQVARGMEFLSSRKCIHRDLAARNILLSENN----VVKICDFG--LA------RDIYKNPDYVRKGDARLplkwMAPE- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsAVID--YS-KADTWAVGAIAYEIFGL-ANPFYG-QGSAHLESRsYQEAQLPEMPESVPPEARRLVRSLLQRE 492
Cdd:cd14207  253 --------SIFDkiYStKSDVWSYGVLLWEIFSLgASPYPGvQIDEDFCSK-LKEGIRMRAPEFATSEIYQIMLDCWQGD 323

                 ....*
gi 126215545 493 ASKRP 497
Cdd:cd14207  324 PNERP 328
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
265-498 6.29e-06

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: 48.08  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSVPLLpgALADYPDMlpphyypeglGHGRTlFLVMKNYPCTLRQYLEEQTPSSRLATM---- 340
Cdd:cd05098   73 KMIGKHKNIINLLGACTQDGPLY--VIVEYASK----------GNLRE-YLQARRPPGMEYCYNPSHNPEEQLSSKdlvs 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGCCLADQHVglrlpfnsSSVERGGNGSL----MAPE 416
Cdd:cd05098  140 CAYQVARGMEYLASKKCIHRDLAARNVLVTEDN----VMKIADFGLARDIHHI--------DYYKKTTNGRLpvkwMAPE 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 vstahsgpsAVID--YS-KADTWAVGAIAYEIFGL-ANPFYGQGSAHLeSRSYQEAQLPEMPESVPPEARRLVRSLLQRE 492
Cdd:cd05098  208 ---------ALFDriYThQSDVWSFGVLLWEIFTLgGSPYPGVPVEEL-FKLLKEGHRMDKPSNCTNELYMMMRDCWHAV 277

                 ....*.
gi 126215545 493 ASKRPS 498
Cdd:cd05098  278 PSQRPT 283
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
308-500 6.34e-06

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: 47.97  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 308 GHGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwLV-ISDFG 385
Cdd:cd05080   78 QGGKSLQLIMEYVPLgSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDR-----LVkIGDFG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 CCLA--DQHVGLRlpfnsssVERGGNGSLM--APEVSTAHSGpsavidYSKADTWAVGAIAYEIFGLANPFYGQGSAHLE 461
Cdd:cd05080  153 LAKAvpEGHEYYR-------VREDGDSPVFwyAPECLKEYKF------YYASDVWSFGVTLYELLTHCDSSQSPPTKFLE 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 126215545 462 ---SRSYQEAQLPEM-----------PESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd05080  220 migIAQGQMTVVRLIellergerlpcPDKCPQEVYHLMKNCWETEASFRPTFE 272
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
344-499 6.60e-06

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 48.28  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGccladqhVGLRL-----PFNSSSvergGNGSLMAPEVS 418
Cdd:PLN00034 176 QILSGIAYLHRRHIVHRDIKPSNLLI----NSAKNVKIADFG-------VSRILaqtmdPCNSSV----GTIAYMSPERI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHSGPSAVIDYSkADTWAVGAIAYEIFGLANPF----YGQGSAHLESRSYqeAQLPEMPESVPPEARRLVRSLLQREAS 494
Cdd:PLN00034 241 NTDLNHGAYDGYA-GDIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAICM--SQPPEAPATASREFRHFISCCLQREPA 317

                 ....*
gi 126215545 495 KRPSA 499
Cdd:PLN00034 318 KRWSA 322
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
357-529 7.13e-06

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: 48.42  E-value: 7.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 357 IAHRDLKSDNILVewDSDGcpWLVISDFGCCLADqhvglrLPFNSSSVERGGNGSLMAPEVSTAHSGPSAVidyskaDTW 436
Cdd:cd05604  118 IVYRDLKPENILL--DSQG--HIVLTDFGLCKEG------ISNSDTTTTFCGTPEYLAPEVIRKQPYDNTV------DWW 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 437 AVGAIAYE-IFGLAnPFYGQGSAHLesrsYQeaQLPEMPESVPPEARRLVRSLLQREASKRPSARLAANvlhlslwgEHL 515
Cdd:cd05604  182 CLGSVLYEmLYGLP-PFYCRDTAEM----YE--NILHKPLVLRPGISLTAWSILEELLEKDRQLRLGAK--------EDF 246
                        170
                 ....*....|....
gi 126215545 516 LALKNLKLDKMIAW 529
Cdd:cd05604  247 LEIKNHPFFESINW 260
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
310-452 7.18e-06

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: 48.48  E-value: 7.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLV---MKNYPcTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGc 386
Cdd:cd14176   85 GKYVYVVtelMKGGE-LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFG- 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 387 cLADQHvglrlpfnsssveRGGNGSLMAPEVSTAHSGPSAVID--YSKA-DTWAVGAIAYEIFGLANPF 452
Cdd:cd14176  163 -FAKQL-------------RAENGLLMTPCYTANFVAPEVLERqgYDAAcDIWSLGVLLYTMLTGYTPF 217
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
270-445 8.06e-06

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: 48.16  E-value: 8.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpGALADYPDmlpphyypeglghgrtLFLVMKNYPCTLRQYLEEQTPSSRLATMMtLQLLEGV 349
Cdd:cd07874   75 HKNIISLLNVFTPQ-----KSLEEFQD----------------VYLVMELMDANLCQVIQMELDHERMSYLL-YQMLCGI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCcladqhvglrlpfnsssVERGGNGSLMAPEVSTA-HSGPSAVI 428
Cdd:cd07874  133 KHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGL-----------------ARTAGTSFMMTPYVVTRyYRAPEVIL 191
                        170       180
                 ....*....|....*....|
gi 126215545 429 DY---SKADTWAVGAIAYEI 445
Cdd:cd07874  192 GMgykENVDIWSVGCIMGEM 211
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
341-498 8.08e-06

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: 47.43  E-value: 8.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPwlvISDFGccLADQhvgLRLPFNSSSverggngSLMAPEVSTA 420
Cdd:cd05148  109 MACQVAEGMAYLEEQNSIHRDLAARNILVG-EDLVCK---VADFG--LARL---IKEDVYLSS-------DKKIPYKWTA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 hsgPSAVI--DYS-KADTWAVGAIAYEIFGlanpfYGQgsAHLESRSYQEA--------QLPEmPESVPPEARRLVRSLL 489
Cdd:cd05148  173 ---PEAAShgTFStKSDVWSFGILLYEMFT-----YGQ--VPYPGMNNHEVydqitagyRMPC-PAKCPQEIYKIMLECW 241

                 ....*....
gi 126215545 490 QREASKRPS 498
Cdd:cd05148  242 AAEPEDRPS 250
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
341-496 8.14e-06

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: 47.85  E-value: 8.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsdGCPWLV-ISDFGCCladqhvglRLPFNSSSVERGGNGSL----MAP 415
Cdd:cd05049  127 IAVQIASGMVYLASQHFVHRDLATRNCLV-----GTNLVVkIGDFGMS--------RDIYSTDYYRVGGHTMLpirwMPP 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVstahsgpsavIDYSK----ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQR 491
Cdd:cd05049  194 ES----------ILYRKftteSDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKR 263

                 ....*
gi 126215545 492 EASKR 496
Cdd:cd05049  264 EPQQR 268
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
314-385 8.54e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 48.64  E-value: 8.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 314 FLVMKnY--PCTLRQYLEEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpwLV-ISDFG 385
Cdd:NF033483  83 YIVME-YvdGRTLKDYIREHGPlSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI--TKDG---RVkVTDFG 152
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
343-496 8.88e-06

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: 47.31  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVIsDFGCCLADQHVG-LRLPFnsssvergGNGSLMAPEVSTAH 421
Cdd:cd14191  107 RQISEGVEYIHKQGIVHLDLKPENIMCV-NKTGTKIKLI-DFGLARRLENAGsLKVLF--------GTPEFVAPEVINYE 176
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 422 SgpsavIDYSkADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAQlpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14191  177 P-----IGYA-TDMWSIGVICYILVSGLSPFMGDNDnetlANVTSATWDFDD--EAFDEISDDAKDFISNLLKKDMKAR 247
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
305-498 9.72e-06

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: 47.66  E-value: 9.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 305 EGLGHGRtlflvMKNYPCTLRQYLEEQT----PSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLV 380
Cdd:cd05061   89 ELMAHGD-----LKSYLRSLRPEAENNPgrppPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFT----VK 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 381 ISDFGCCladqhvglRLPFNSSSVERGGNGSL----MAPE-----VSTAHSgpsavidyskaDTWAVGAIAYEIFGLANP 451
Cdd:cd05061  160 IGDFGMT--------RDIYETDYYRKGGKGLLpvrwMAPEslkdgVFTTSS-----------DMWSFGVVLWEITSLAEQ 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 126215545 452 FYgQGSAHLESRSY-QEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05061  221 PY-QGLSNEQVLKFvMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPT 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
344-499 9.90e-06

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: 47.30  E-value: 9.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLviSDFGccladqhVGLRLpfNSSSVERG---GNGSLMAPEVsta 420
Cdd:cd06613  105 ETLKGLAYLHSTGKIHRDIKGANILL--TEDGDVKL--ADFG-------VSAQL--TATIAKRKsfiGTPYWMAPEV--- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 hsgpSAVID---Y-SKADTWAVGAIAYEIFGLANPFYGqgsAH-------LESRSYQEAQLPEmPESVPPEARRLVRSLL 489
Cdd:cd06613  169 ----AAVERkggYdGKCDIWALGITAIELAELQPPMFD---LHpmralflIPKSNFDPPKLKD-KEKWSPDFHDFIKKCL 240
                        170
                 ....*....|
gi 126215545 490 QREASKRPSA 499
Cdd:cd06613  241 TKNPKKRPTA 250
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
311-489 1.03e-05

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: 48.07  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGCCLA 389
Cdd:cd05621  125 KYLYMVMEYMPGgDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL----DKYGHLKLADFGTCMK 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 390 DQHVGlrLPFNSSSVergGNGSLMAPEVSTAHSGPSAvidYSK-ADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEA 468
Cdd:cd05621  201 MDETG--MVHCDTAV---GTPDYISPEVLKSQGGDGY---YGReCDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHK 272
                        170       180
                 ....*....|....*....|...
gi 126215545 469 QLPEMPESV--PPEARRLVRSLL 489
Cdd:cd05621  273 NSLNFPDDVeiSKHAKNLICAFL 295
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
341-385 1.07e-05

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: 47.69  E-value: 1.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG 385
Cdd:cd07866  120 YMLQLLEGINYLHENHILHRDIKAANILI--DNQGI--LKIADFG 160
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
344-497 1.15e-05

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: 47.00  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADqhvgLRLPFNSSSVERGGNGSL--MAPEVSTAH 421
Cdd:cd14062   97 QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLT----VKIGDFG--LAT----VKTRWSGSQQFEQPTGSIlwMAPEVIRMQ 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SG-PsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSA----HLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd14062  167 DEnP-----YSfQSDVYAFGIVLYELLTGQLPYSHINNRdqilFMVGRGYLRPDLSKVRSDTPKALRRLMEDCIKFQRDE 241

                 ..
gi 126215545 496 RP 497
Cdd:cd14062  242 RP 243
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
270-447 1.21e-05

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: 47.36  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIrvfraftssvpllpgALADYpdMLPPHYYPEGlghgRTLFLVMKNYPCTLRQYLEEQTP-SSRLATMMTLQLLEG 348
Cdd:cd07855   63 HDNII---------------AIRDI--LRPKVPYADF----KDVYVVLDLMESDLHHIIHSDQPlTLEHIRYFLYQLLRG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 349 VDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGC--CLAdqhvglrlpfnSSSVErggNGSLMAPEVSTA-HSGPS 425
Cdd:cd07855  122 LKYIHSANVIHRDLKPSNLLVNENCE----LKIGDFGMarGLC-----------TSPEE---HKYFMTEYVATRwYRAPE 183
                        170       180
                 ....*....|....*....|....*.
gi 126215545 426 AVI---DYSKA-DTWAVGAIAYEIFG 447
Cdd:cd07855  184 LMLslpEYTQAiDMWSVGCIFAEMLG 209
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
348-496 1.22e-05

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: 47.72  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqHVGLRlPFNSSSVeRGGNGSLMAPEVSTAHsgpsav 427
Cdd:cd05618  133 ALNYLHERGIIYRDLKLDNVLL--DSEG--HIKLTDYGMC----KEGLR-PGDTTST-FCGTPNYIAPEILRGE------ 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 428 iDYS-KADTWAVGAIAYEIFGLANPFYGQGSA-----HLESRSYQ---EAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05618  197 -DYGfSVDWWALGVLMFEMMAGRSPFDIVGSSdnpdqNTEDYLFQvilEKQI-RIPRSLSVKAASVLKSFLNKDPKER 272
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
341-497 1.33e-05

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: 47.37  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHL-VQQGIAHRDLKSDNILVewDSDGCPWLVisDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVST 419
Cdd:cd06618  119 MTVSIVKALHYLkEKHGVIHRDVKPSNILL--DESGNVKLC--DFG-------ISGRLVDSKAKTRSAGCAAYMAPERID 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPSAVIdysKADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAqLPEMP--ESVPPEARRLVRSLLQREASKR 496
Cdd:cd06618  188 PPDNPKYDI---RADVWSLGISLVELATGQFPYRNcKTEFEVLTKILNEE-PPSLPpnEGFSPDFCSFVDLCLTKDHRYR 263

                 .
gi 126215545 497 P 497
Cdd:cd06618  264 P 264
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
329-499 1.34e-05

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: 47.32  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 329 EEQTPSSRLATMMTLQLLEGvdhlvqQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladQHVGLRLPFNSSSVergG 408
Cdd:cd06657  115 EEQIAAVCLAVLKALSVLHA------QGVIHRDIKSDSILLTHDGR----VKLSDFGFC---AQVSKEVPRRKSLV---G 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 NGSLMAPE-VSTAHSGPsavidysKADTWAVGAIAYEIFGLANPFYGQGSahLESRSYQEAQLP---EMPESVPPEARRL 484
Cdd:cd06657  179 TPYWMAPElISRLPYGP-------EVDIWSLGIMVIEMVDGEPPYFNEPP--LKAMKMIRDNLPpklKNLHKVSPSLKGF 249
                        170
                 ....*....|....*
gi 126215545 485 VRSLLQREASKRPSA 499
Cdd:cd06657  250 LDRLLVRDPAQRATA 264
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
342-504 1.35e-05

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: 46.88  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPWLVIsDFG-CCLADQHVglrlpfnSSSVErggNGSLMAPEVSTA 420
Cdd:cd14133  108 AQQILEALVFLHSLGLIHCDLKPENILLA-SYSRCQIKII-DFGsSCFLTQRL-------YSYIQ---SRYYRAPEVILG 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 hsgpsavIDYSKA-DTWAVGAIAYEIFgLANPF------YGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd14133  176 -------LPYDEKiDMWSLGCILAELY-TGEPLfpgaseVDQLARIIGTIGIPPAHMLDQGKADDELFVDFLKKLLEIDP 247
                        170
                 ....*....|.
gi 126215545 494 SKRPSARLAAN 504
Cdd:cd14133  248 KERPTASQALS 258
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
346-445 1.49e-05

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: 46.91  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVisDFG-CCLADQHVGLRlpfNSSSvergGNGSLMAPEVSTAHSGP 424
Cdd:cd06608  123 LRGLAYLHENKVIHRDIKGQNILL--TEEAEVKLV--DFGvSAQLDSTLGRR---NTFI----GTPYWMAPEVIACDQQP 191
                         90       100
                 ....*....|....*....|.
gi 126215545 425 SAVIDySKADTWAVGAIAYEI 445
Cdd:cd06608  192 DASYD-ARCDVWSLGITAIEL 211
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
342-498 1.58e-05

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 47.28  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MAPEv 417
Cdd:cd05102  178 SFQVARGMEFLASRKCIHRDLAARNILLSENN----VVKICDFG--LA------RDIYKDPDYVRKGSARLplkwMAPE- 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsAVID---YSKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd05102  245 --------SIFDkvyTTQSDVWSFGVLLWEIFSLgASPYPGVQINEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDP 316

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd05102  317 KERPT 321
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
328-504 1.71e-05

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: 46.56  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 328 LEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNiLVEWDSDGCPWLVISDFGccLADQHVGLrlpfnssSVERG 407
Cdd:cd14088   91 LDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLEN-LVYYNRLKNSKIVISDFH--LAKLENGL-------IKEPC 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 408 GNGSLMAPEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQgsahLESRSYQ---------------EAQLPE 472
Cdd:cd14088  161 GTPEYLAPEVVGRQRYGRPV------DCWAIGVIMYILLSGNPPFYDE----AEEDDYEnhdknlfrkilagdyEFDSPY 230
                        170       180       190
                 ....*....|....*....|....*....|..
gi 126215545 473 MPEsVPPEARRLVRSLLQREASKRPSARLAAN 504
Cdd:cd14088  231 WDD-ISQAAKDLVTRLMEVEQDQRITAEEAIS 261
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
334-496 1.77e-05

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: 46.66  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGccladqhvglrlpFNSSSVERG----GN 409
Cdd:cd05612   99 SNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL--DKEG--HIKLTDFG-------------FAKKLRDRTwtlcGT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 410 GSLMAPEV--STAHSgpSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLesrsYQE--AQLPEMPESVPPEARRLV 485
Cdd:cd05612  162 PEYLAPEViqSKGHN--KAV------DWWALGILIYEMLVGYPPFFDDNPFGI----YEKilAGKLEFPRHLDLYAKDLI 229
                        170
                 ....*....|.
gi 126215545 486 RSLLQREASKR 496
Cdd:cd05612  230 KKLLVVDRTRR 240
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
342-499 1.99e-05

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: 46.56  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCLADQHVGLRlpfNSSSVERGGNGSLMAPEVSTAH 421
Cdd:cd06653  112 TRQILQGVSYLHSNMIVHRDIKGANILR--DSAGN--VKLGDFGASKRIQTICMS---GTGIKSVTGTPYWMSPEVISGE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SgpsavidYS-KADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQlPEMPESVPPEARRLVRSLLQREaSKRPSA 499
Cdd:cd06653  185 G-------YGrKADVWSVACTVVEMLTEKPPWAEyEAMAAIFKIATQPTK-PQLPDGVSDACRDFLRQIFVEE-KRRPTA 255
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
323-500 2.14e-05

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: 46.45  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 323 TLRQYLEE-QTPSSRLATMMTLQLLEGVD--HLVQQGIAHRDLKSDNILVewdsDGCPWLV-ISDFGccLADQhvgLRLP 398
Cdd:cd13983   88 TLKQYLKRfKRLKLKVIKSWCRQILEGLNylHTRDPPIIHRDLKCDNIFI----NGNTGEVkIGDLG--LATL---LRQS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 399 FNSSSVergGNGSLMAPEVSTAHSGPsavidysKADTWAVGAIAYEIFGLANPfygqgsahlesrsYQEAQLP------- 471
Cdd:cd13983  159 FAKSVI---GTPEFMAPEMYEEHYDE-------KVDIYAFGMCLLEMATGEYP-------------YSECTNAaqiykkv 215
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 126215545 472 ---EMPES----VPPEARRLVRSLLqREASKRPSAR 500
Cdd:cd13983  216 tsgIKPESlskvKDPELKDFIEKCL-KPPDERPSAR 250
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
324-445 2.29e-05

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: 46.26  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLATM----MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhVGLRLPF 399
Cdd:cd14052   90 LDVFLSELGLLGRLDEFrvwkILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT----LKIGDFG-------MATVWPL 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 126215545 400 nSSSVERGGNGSLMAPEVSTAHSgpsavIDYsKADTWAVGAIAYEI 445
Cdd:cd14052  159 -IRGIEREGDREYIAPEILSEHM-----YDK-PADIFSLGLILLEA 197
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
324-498 2.51e-05

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: 46.10  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTP-SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFgccladqhvGLRLPFNSS 402
Cdd:cd14161   89 LYDYISERQRlSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN----IKIADF---------GLSNLYNQD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 403 SVERGGNGSLM--APEVSTA--HSGPsavidysKADTWAVGAIAYEIFGLANPFYGQGS----AHLESRSYQEAqlpemp 474
Cdd:cd14161  156 KFLQTYCGSPLyaSPEIVNGrpYIGP-------EVDSWSLGVLLYILVHGTMPFDGHDYkilvKQISSGAYREP------ 222
                        170       180
                 ....*....|....*....|....
gi 126215545 475 eSVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14161  223 -TKPSDACGLIRWLLMVNPERRAT 245
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
324-453 2.55e-05

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: 46.03  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLAtmMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGC---CLADQH---VGLRL 397
Cdd:cd05113   90 LREMRKRFQTQQLLE--MCKDVCEAMEYLESKQFLHRDLAARNCLV--NDQGV--VKVSDFGLsryVLDDEYtssVGSKF 163
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 398 PFNSSsverggngslmAPEVsTAHSGPSavidySKADTWAVGAIAYEIFGLANPFY 453
Cdd:cd05113  164 PVRWS-----------PPEV-LMYSKFS-----SKSDVWAFGVLMWEVYSLGKMPY 202
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
344-496 2.69e-05

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: 45.84  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCClADQHVGLRLPFNSSSvergGNGSLMAPEV--STAH 421
Cdd:cd14078  109 QIVSAVAYVHSQGYAHRDLKPENLLLDEDQN----LKLIDFGLC-AKPKGGMDHHLETCC----GSPAYAAPELiqGKPY 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 422 SGpsavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLeSRSYQEAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14078  180 IG-------SEADVWSMGVLLYALLCGFLPFDDDNVMAL-YRKIQSGKY-EEPEWLSPSSKLLLDQMLQVDPKKR 245
pknD PRK13184
serine/threonine-protein kinase PknD;
270-452 2.94e-05

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 47.07  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLlpgaladypdmlpphYYPEGLGHGRTLFLVMKN-YPC-TLRQYLEEQTpssRLATMMTL--QL 345
Cdd:PRK13184  61 HPGIVPVYSICSDGDPV---------------YYTMPYIEGYTLKSLLKSvWQKeSLSKELAEKT---SVGAFLSIfhKI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCC---------LADQHVGLRLPFNSSSVERG---GNGSLM 413
Cdd:PRK13184 123 CATIEYVHSKGVLHRDLKPDNILLGLFGE----VVILDWGAAifkkleeedLLDIDVDERNICYSSMTIPGkivGTPDYM 198
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126215545 414 APEVSTAHsgPSAVidysKADTWAVGAIAYEIFGLANPF 452
Cdd:PRK13184 199 APERLLGV--PASE----STDIYALGVILYQMLTLSFPY 231
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
265-500 3.31e-05

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: 46.17  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSVPLLpgALADYPDMLPPHYY-----PEGLghgrtlflvmkNYPCTLRQYLEEQTPSSRLAT 339
Cdd:cd05100   72 KMIGKHKNIINLLGACTQDGPLY--VLVEYASKGNLREYlrarrPPGM-----------DYSFDTCKLPEEQLTFKDLVS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 340 MmTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGCClADQHvglrlpfNSSSVERGGNGSL----MAP 415
Cdd:cd05100  139 C-AYQVARGMEYLASQKCIHRDLAARNVLVTEDN----VMKIADFGLA-RDVH-------NIDYYKKTTNGRLpvkwMAP 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EvstahsgpsAVID--YS-KADTWAVGAIAYEIFGLA-NPFYGQGSAHLeSRSYQEAQLPEMPESVPPEARRLVRSLLQR 491
Cdd:cd05100  206 E---------ALFDrvYThQSDVWSFGVLLWEIFTLGgSPYPGIPVEEL-FKLLKEGHRMDKPANCTHELYMIMRECWHA 275

                 ....*....
gi 126215545 492 EASKRPSAR 500
Cdd:cd05100  276 VPSQRPTFK 284
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
331-498 3.34e-05

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: 45.69  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 331 QTPSSRLATMMTLQLLE----GVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQhvglrlpfnsSSVER 406
Cdd:cd05084   86 RTEGPRLKVKELIRMVEnaaaGMEYLESKHCIHRDLAARNCLVTEKNV----LKISDFGMSREEE----------DGVYA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 407 GGNGSLMAPEVSTAhsgPSAvIDY----SKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSYQEAQLPeMPESVPPEA 481
Cdd:cd05084  152 ATGGMKQIPVKWTA---PEA-LNYgrysSESDVWSFGILLWETFSLgAVPYANLSNQQTREAVEQGVRLP-CPENCPDEV 226
                        170
                 ....*....|....*..
gi 126215545 482 RRLVRSLLQREASKRPS 498
Cdd:cd05084  227 YRLMEQCWEYDPRKRPS 243
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
344-496 3.55e-05

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: 46.21  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwlVISDfgccladqhVGLRLPFNSSSVERG-GNGSLMAPEV---ST 419
Cdd:cd05633  116 EIILGLEHMHNRFVVYRDLKPANILLDEHGHV----RISD---------LGLACDFSKKKPHASvGTHGYMAPEVlqkGT 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 420 AHSgpsavidySKADTWAVGAIAYEIFGLANPF--YGQGSAHLESRSYQEAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05633  183 AYD--------SSADWFSLGCMLFKLLRGHSPFrqHKTKDKHEIDRMTLTVNV-ELPDSFSPELKSLLEGLLQRDVSKR 252
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
270-499 3.84e-05

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: 45.59  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLL-------PGALADYPDMLPPHYYPEgLGHGRTLFLVMKNYPCTLrqyleeqTPSSRLAtmMT 342
Cdd:cd05050   67 HPNIVKLLGVCAVGKPMCllfeymaYGDLNEFLRHRSPRAQCS-LSHSTSSARKCGLNPLPL-------SCTEQLC--IA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhvgLRLPFNSSSVERGGNGSL-----MAPEV 417
Cdd:cd05050  137 KQVAAGMAYLSERKFVHRDLATRNCLVGENMV----VKIADFG---------LSRNIYSADYYKASENDAipirwMPPES 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsavIDYSK----ADTWAVGAIAYEIFGLA-NPFYGQgsAHLESRSY-QEAQLPEMPESVPPEARRLVRSLLQR 491
Cdd:cd05050  204 ----------IFYNRytteSDVWAYGVVLWEIFSYGmQPYYGM--AHEEVIYYvRDGNVLSCPDNCPLELYNLMRLCWSK 271

                 ....*...
gi 126215545 492 EASKRPSA 499
Cdd:cd05050  272 LPSDRPSF 279
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
343-498 3.92e-05

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: 45.33  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGCPWLVISDFGCCladqhvglRLPFNSSSVERGGNGS--LMAPEVstA 420
Cdd:cd08225  108 VQISLGLKHIHDRKILHRDIKSQNIFL---SKNGMVAKLGDFGIA--------RQLNDSMELAYTCVGTpyYLSPEI--C 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 421 HSGPSAvidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPeSVPPEARRLVRSLLQREASKRPS 498
Cdd:cd08225  175 QNRPYN----NKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISP-NFSRDLRSLISQLFKVSPRDRPS 247
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
344-499 4.03e-05

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: 45.34  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWdSDGCPWLVISDFGCCL---ADQHVGLRLpfnsssvergGNGSLMAPEVstA 420
Cdd:cd14115   97 DIMEALQYLHNCRVAHLDIKPENLLIDL-RIPVPRVKLIDLEDAVqisGHRHVHHLL----------GNPEFAAPEV--I 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPSAVidysKADTWAVGAIAYEIFGLANPFYGqgsahlESRSYQEAQLPEMPESVPPE--------ARRLVRSLLQRE 492
Cdd:cd14115  164 QGTPVSL----ATDIWSIGVLTYVMLSGVSPFLD------ESKEETCINVCRVDFSFPDEyfgdvsqaARDFINVILQED 233

                 ....*..
gi 126215545 493 ASKRPSA 499
Cdd:cd14115  234 PRRRPTA 240
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
270-454 4.07e-05

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: 45.58  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllPGALADYPDMlpphyypeglghGRTLFLVMKNYPCTLRQYLEEQtpssrLATMMTlQLLEGV 349
Cdd:cd14109   55 HPNIVQMHDAYDDE----KLAVTVIDNL------------ASTIELVRDNLLPGKDYYTERQ-----VAVFVR-QLLLAL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSdgcpwLVISDFGccladqhVGLRLPFNSSSVERGGNGSLMAPEVstAHSGPSAVid 429
Cdd:cd14109  113 KHMHDLGIAHLDLRPEDILLQDDK-----LKLADFG-------QSRRLLRGKLTTLIYGSPEFVSPEI--VNSYPVTL-- 176
                        170       180
                 ....*....|....*....|....*
gi 126215545 430 ysKADTWAVGAIAYEIFGLANPFYG 454
Cdd:cd14109  177 --ATDMWSVGVLTYVLLGGISPFLG 199
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
309-447 4.14e-05

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: 45.82  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 309 HGRTLFLVMknypctlrQYLEeQTPSSRLATMMT-----------LQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCp 377
Cdd:cd07845   79 HLDSIFLVM--------EYCE-QDLASLLDNMPTpfsesqvkclmLQLLRGLQYLHENFIIHRDLKVSNLLL--TDKGC- 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 378 wLVISDFGccLADQHvglRLPFNSssverggngslMAPEVSTA-HSGPSAVI---DYSKA-DTWAVGAIAYEIFG 447
Cdd:cd07845  147 -LKIADFG--LARTY---GLPAKP-----------MTPKVVTLwYRAPELLLgctTYTTAiDMWAVGCILAELLA 204
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
265-498 4.29e-05

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: 45.78  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSVPLL-------PGALADYPDMLPPhyyPEglghgrtlflvmKNYPCTLRQYLEEQTPSSRL 337
Cdd:cd05101   84 KMIGKHKNIINLLGACTQDGPLYviveyasKGNLREYLRARRP---PG------------MEYSYDINRVPEEQMTFKDL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMmTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----M 413
Cdd:cd05101  149 VSC-TYQLARGMEYLASQKCIHRDLAARNVLVTENN----VMKIADFG--LA------RDINNIDYYKKTTNGRLpvkwM 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEvstahsgpsAVID--YS-KADTWAVGAIAYEIFGL-ANPFYGQGSAHLeSRSYQEAQLPEMPESVPPEARRLVRSLL 489
Cdd:cd05101  216 APE---------ALFDrvYThQSDVWSFGVLMWEIFTLgGSPYPGIPVEEL-FKLLKEGHRMDKPANCTNELYMMMRDCW 285

                 ....*....
gi 126215545 490 QREASKRPS 498
Cdd:cd05101  286 HAVPSQRPT 294
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
328-499 4.60e-05

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: 45.30  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 328 LEEQTPSSRLATMMTL-QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpWLVISDFGccLADQH---VGLRLPFnsss 403
Cdd:cd14190   93 VDEDYHLTEVDAMVFVrQICEGIQFMHQMRVLHLDLKPENILCVNRTGH--QVKIIDFG--LARRYnprEKLKVNF---- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 404 vergGNGSLMAPEvstahsgpsaVIDYS----KADTWAVGAIAYEIFGLANPFYGQGSAH-----LESRSYQEAqlpEMP 474
Cdd:cd14190  165 ----GTPEFLSPE----------VVNYDqvsfPTDMWSMGVITYMLLSGLSPFLGDDDTEtlnnvLMGNWYFDE---ETF 227
                        170       180
                 ....*....|....*....|....*
gi 126215545 475 ESVPPEARRLVRSLLQREASKRPSA 499
Cdd:cd14190  228 EHVSDEAKDFVSNLIIKERSARMSA 252
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
341-506 5.34e-05

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: 45.26  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPwlvISDFGccLAdqhvglRLPFNSSSVERGGngslmaPEVSTA 420
Cdd:cd05067  108 MAAQIAEGMAFIEERNYIHRDLRAANILVS-DTLSCK---IADFG--LA------RLIEDNEYTAREG------AKFPIK 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPSAvIDYS----KADTWAVGAIAYEIF--------GLANPfygQGSAHLEsRSYQEAQlpemPESVPPEARRLVRSL 488
Cdd:cd05067  170 WTAPEA-INYGtftiKSDVWSFGILLTEIVthgripypGMTNP---EVIQNLE-RGYRMPR----PDNCPEELYQLMRLC 240
                        170
                 ....*....|....*...
gi 126215545 489 LQREASKRPSARLAANVL 506
Cdd:cd05067  241 WKERPEDRPTFEYLRSVL 258
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
333-498 5.49e-05

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: 44.83  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 333 PSSRLatMMTLQLLEGVDHL--VQQGIAHRDLKSDNILVewDSDGCPwlVISDFG-----CCLADQHVglrlpfnsssVE 405
Cdd:cd14064   92 LQSKL--IIAVDVAKGMEYLhnLTQPIIHRDLNSHNILL--YEDGHA--VVADFGesrflQSLDEDNM----------TK 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 406 RGGNGSLMAPEVSTAHSgpsaviDYS-KADTWAVGAIAYEIFGLANPFygqgsAHLE------SRSYQEAQlPEMPESVP 478
Cdd:cd14064  156 QPGNLRWMAPEVFTQCT------RYSiKADVFSYALCLWELLTGEIPF-----AHLKpaaaaaDMAYHHIR-PPIGYSIP 223
                        170       180
                 ....*....|....*....|....
gi 126215545 479 pearRLVRSLLQR----EASKRPS 498
Cdd:cd14064  224 ----KPISSLLMRgwnaEPESRPS 243
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
334-499 5.56e-05

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: 45.02  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 334 SSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGccLADQHVGlrlPFNSSSvergGNGSLM 413
Cdd:cd14184   97 TERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFG--LATVVEG---PLYTVC----GTPTYV 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVsTAHSGpsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSahLESRSYQEAQLP--EMP----ESVPPEARRLVR 486
Cdd:cd14184  168 APEI-IAETG------YGlKVDIWAAGVITYILLCGFPPFRSENN--LQEDLFDQILLGklEFPspywDNITDSAKELIS 238
                        170
                 ....*....|...
gi 126215545 487 SLLQREASKRPSA 499
Cdd:cd14184  239 HMLQVNVEARYTA 251
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
344-385 5.60e-05

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: 44.98  E-value: 5.60e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILV-EWDSdgcpwLVISDFG 385
Cdd:cd14162  108 QLVAGVEYCHSKGVVHRDLKCENLLLdKNNN-----LKITDFG 145
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
335-500 5.61e-05

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: 45.06  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 335 SRLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQhvglrlpFNSSSVERG---GNGS 411
Cdd:cd06641  101 TQIATILR-EILKGLDYLHSEKKIHRDIKAANVLLSEHGE----VKLADFG--VAGQ-------LTDTQIKRN*fvGTPF 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 412 LMAPEV--STAHSgpsavidySKADTWAVGAIAYEIFGLANPfygqgsahlESRSYQEAQLPEMPESVPP--------EA 481
Cdd:cd06641  167 WMAPEVikQSAYD--------SKADIWSLGITAIELARGEPP---------HSELHPMKVLFLIPKNNPPtlegnyskPL 229
                        170
                 ....*....|....*....
gi 126215545 482 RRLVRSLLQREASKRPSAR 500
Cdd:cd06641  230 KEFVEACLNKEPSFRPTAK 248
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
342-498 6.25e-05

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: 45.36  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MAPEv 417
Cdd:cd05103  185 SFQVAKGMEFLASRKCIHRDLAARNILLSENN----VVKICDFG--LA------RDIYKDPDYVRKGDARLplkwMAPE- 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsAVID--YS-KADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd05103  252 --------TIFDrvYTiQSDVWSFGVLLWEIFSLgASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEP 323

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd05103  324 SQRPT 328
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
344-511 6.39e-05

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: 45.09  E-value: 6.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGccLAdqhvglrlpfNSSSVERGGNGSLM---------- 413
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLV--NADCE--LKICDFG--LA----------RGFSENPGENAGFMteyvatrwyr 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEVSTAHSGpsavidYSKA-DTWAVGAIAYEIFGLANPFYGQGS-------------------AHLESRSYQE--AQLP 471
Cdd:cd07857  177 APEIMLSFQS------YTKAiDVWSVGCILAELLGRKPVFKGKDYvdqlnqilqvlgtpdeetlSRIGSPKAQNyiRSLP 250
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 126215545 472 EMPE-----SVP---PEARRLVRSLLQREASKRPSARLAANVLHLSLW 511
Cdd:cd07857  251 NIPKkpfesIFPnanPLALDLLEKLLAFDPTKRISVEEALEHPYLAIW 298
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
313-504 6.61e-05

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: 45.21  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYPCTLRQYLE-------EQTPSSRLATMMtLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCpwLVISDFG 385
Cdd:cd07837   80 LYLVFEYLDTDLKKFIDsygrgphNPLPAKTIQSFM-YQLCKGVAHCHSHGVMHRDLKPQNLLVD-KQKGL--LKIADLG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 CCLAdqhvgLRLPFNSSSVE------RggngslmAPEV---STAHSGPsavidyskADTWAVGAIAYEIFGLANPFYGQ- 455
Cdd:cd07837  156 LGRA-----FTIPIKSYTHEivtlwyR-------APEVllgSTHYSTP--------VDMWSVGCIFAEMSRKQPLFPGDs 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 456 ------------GSAHLES----------RSYQEAQLPEMPESVP---PEARRLVRSLLQREASKRPSARLAAN 504
Cdd:cd07837  216 elqqllhifrllGTPNEEVwpgvsklrdwHEYPQWKPQDLSRAVPdlePEGVDLLTKMLAYDPAKRISAKAALQ 289
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
311-511 6.78e-05

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: 44.88  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPC-TLRQYLeeQTPSSRLATMMTL----QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFG 385
Cdd:cd05081   80 RSLRLVMEYLPSgCLRDFL--QRHRARLDASRLLlyssQICKGMEYLGSRRCVHRDLAARNILVESEAH----VKIADFG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 ccladqhVGLRLPFNSSS--VERGGNGSLM--APEvSTAHSgpsavIDYSKADTWAVGAIAYEIFGLANpfygqgsahlE 461
Cdd:cd05081  154 -------LAKLLPLDKDYyvVREPGQSPIFwyAPE-SLSDN-----IFSRQSDVWSFGVVLYELFTYCD----------K 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 462 SRSYQEAQLPEM-PESVPPEARRLVRSLlqrEASKR----PSARLAANVLHLSLW 511
Cdd:cd05081  211 SCSPSAEFLRMMgCERDVPALCRLLELL---EEGQRlpapPACPAEVHELMKLCW 262
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
317-498 6.82e-05

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: 44.70  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 317 MKNypCTLRQYLEEQTPSSRLATM--MTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSDGCPwlvISDFGccLA----- 389
Cdd:cd05068   85 MKH--GSLLEYLQGKGRSLQLPQLidMAAQVASGMAYLESQNYIHRDLAARNVLVG-ENNICK---VADFG--LArvikv 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 390 ----DQHVGLRLPFNSSsverggngslmAPEVSTAHSgpsavidYS-KADTWAVGAIAYEIFGLAN-PFYGQGSAHLESR 463
Cdd:cd05068  157 edeyEAREGAKFPIKWT-----------APEAANYNR-------FSiKSDVWSFGILLTEIVTYGRiPYPGMTNAEVLQQ 218
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126215545 464 SYQEAQLPEmPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05068  219 VERGYRMPC-PPNCPPQLYDIMLECWKADPMERPT 252
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
344-498 7.01e-05

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: 44.96  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGCCLADQHVglrlpfnsSSVERGGNGSL----MAPEvst 419
Cdd:cd05099  142 QVARGMEYLESRRCIHRDLAARNVLVTEDN----VMKIADFGLARGVHDI--------DYYKKTSNGRLpvkwMAPE--- 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 ahsgpsAVID--YS-KADTWAVGAIAYEIFGL-ANPFYGQGSAHLeSRSYQEAQLPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd05099  207 ------ALFDrvYThQSDVWSFGILMWEIFTLgGSPYPGIPVEEL-FKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQ 279

                 ...
gi 126215545 496 RPS 498
Cdd:cd05099  280 RPT 282
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
344-496 7.08e-05

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: 45.04  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDfgccladqhVGLRLPFNSSSVERG-GNGSLMAPEVSTahs 422
Cdd:cd14223  111 EIILGLEHMHSRFVVYRDLKPANILL--DEFG--HVRISD---------LGLACDFSKKKPHASvGTHGYMAPEVLQ--- 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126215545 423 gpSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLP-EMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd14223  175 --KGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAvELPDSFSPELRSLLEGLLQRDVNRR 247
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
310-385 7.19e-05

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: 45.17  E-value: 7.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMMTLQLLE----GVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDF 384
Cdd:cd13988   65 TRHKVLVMELCPCgSLYTVLEEPSNAYGLPESEFLIVLRdvvaGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDF 144

                 .
gi 126215545 385 G 385
Cdd:cd13988  145 G 145
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
270-496 7.36e-05

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: 45.03  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTssvpllpgaladypDMLPPHYYPEGLGHGRTLFLVMKnypctlRQYLEEqTPSSRLATmmtlQLLEGV 349
Cdd:cd14179   61 HPNIVKLHEVYH--------------DQLHTFLVMELLKGGELLERIKK------KQHFSE-TEASHIMR----KLVSAV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSDGCPWLVIsDFGccladqHVGLRLPfnsssvergGNGSLMAPEVSTAHSGPSaVID 429
Cdd:cd14179  116 SHMHDVGVVHRDLKPENLLFTDESDNSEIKII-DFG------FARLKPP---------DNQPLKTPCFTLHYAAPE-LLN 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 430 YS----KADTWAVGAIAYEIFGLANPFYGQGSAhLESRSYQEAQLP----------EMPESVPPEARRLVRSLLQREASK 495
Cdd:cd14179  179 YNgydeSCDLWSLGVILYTMLSGQVPFQCHDKS-LTCTSAEEIMKKikqgdfsfegEAWKNVSQEAKDLIQGLLTVDPNK 257

                 .
gi 126215545 496 R 496
Cdd:cd14179  258 R 258
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
266-498 7.78e-05

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: 44.65  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSSvpllpGALadypdMLPPHYYPeglgHGRTL-FL----VMKNYPCTLRQYLEEQTPSSRLATM 340
Cdd:cd05047   51 KLGHHPNIINLLGACEHR-----GYL-----YLAIEYAP----HGNLLdFLrksrVLETDPAFAIANSTASTLSSQQLLH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVewdsdGCPWLV-ISDFGCCLADQ-----HVGlRLPFNSSSVErggngslma 414
Cdd:cd05047  117 FAADVARGMDYLSQKQFIHRDLAARNILV-----GENYVAkIADFGLSRGQEvyvkkTMG-RLPVRWMAIE--------- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 pevSTAHSgpsavIDYSKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSYQEAQLpEMPESVPPEARRLVRSLLQREA 493
Cdd:cd05047  182 ---SLNYS-----VYTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRL-EKPLNCDDEVYDLMRQCWREKP 252

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd05047  253 YERPS 257
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
311-445 7.86e-05

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: 44.62  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPCTLRQYLEE--QTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCL 388
Cdd:cd07871   76 RCLTLVFEYLDSDLKQYLDNcgNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE----LKLADFGLAR 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 389 ADQhvglrLPFNSSSverggngslmaPEVSTAHSGPSAVI----DYSKA-DTWAVGAIAYEI 445
Cdd:cd07871  152 AKS-----VPTKTYS-----------NEVVTLWYRPPDVLlgstEYSTPiDMWGVGCILYEM 197
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
261-455 8.02e-05

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 44.61  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 261 RDGPKQLAPHPNIIRVFRAFT-SSVPLLPGALadypdMLPPHY-YPEGLGHGRTLFLVMKNYPCTLRQYLEEQtpssrla 338
Cdd:cd14153   34 RDNEEQLKAFKREVMAYRQTRhENVVLFMGAC-----MSPPHLaIITSLCKGRTLYSVVRDAKVVLDVNKTRQ------- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 339 tmMTLQLLEGVDHLVQQGIAHRDLKSDNILveWDSDGcpwLVISDFGCcladqhvglrlpFNSSSVERGG---------N 409
Cdd:cd14153  102 --IAQEIVKGMGYLHAKGILHKDLKSKNVF--YDNGK---VVITDFGL------------FTISGVLQAGrredklriqS 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 126215545 410 GSL--MAPEVSTAHSGPSA--VIDYSK-ADTWAVGAIAYEIFGLANPFYGQ 455
Cdd:cd14153  163 GWLchLAPEIIRQLSPETEedKLPFSKhSDVFAFGTIWYELHAREWPFKTQ 213
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
344-496 8.14e-05

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: 44.59  E-value: 8.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVISDFGccladqhvglrlpFNSSSVERG------GNGSLMAPEV 417
Cdd:cd14665  104 QLISGVSYCHSMQICHRDLKLENTLL--DGSPAPRLKICDFG-------------YSKSSVLHSqpkstvGTPAYIAPEV 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 STAHSgpsavIDYSKADTWAVGAIAYEIFGLANPFYGQGsahlESRSYQEA--QLPEMPESVP------PEARRLVRSLL 489
Cdd:cd14665  169 LLKKE-----YDGKIADVWSCGVTLYVMLVGAYPFEDPE----EPRNFRKTiqRILSVQYSIPdyvhisPECRHLISRIF 239

                 ....*..
gi 126215545 490 QREASKR 496
Cdd:cd14665  240 VADPATR 246
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
357-417 8.30e-05

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 44.63  E-value: 8.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 357 IAHRDLKSDNILVEwdsdgcpwlviSDFGCCLADqhVGLRLPFNSSSVERGGNGSL-----MAPEV 417
Cdd:cd14053  123 IAHRDFKSKNVLLK-----------SDLTACIAD--FGLALKFEPGKSCGDTHGQVgtrryMAPEV 175
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
317-498 8.40e-05

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: 44.64  E-value: 8.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 317 MKNYPCTLRQYLEEQT----PSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladqh 392
Cdd:cd05062   96 LKSYLRSLRPEMENNPvqapPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFT----VKIGDFGMT----- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 393 vglRLPFNSSSVERGGNGSL----MAPE-----VSTAHSgpsavidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESR 463
Cdd:cd05062  167 ---RDIYETDYYRKGGKGLLpvrwMSPEslkdgVFTTYS-----------DVWSFGVVLWEIATLAEQPYQGMSNEQVLR 232
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126215545 464 SYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05062  233 FVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPS 267
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
348-505 8.42e-05

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: 45.01  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqHVGLRlPFNSSSVeRGGNGSLMAPEVSTAHsgpsav 427
Cdd:cd05617  128 ALNFLHERGIIYRDLKLDNVLL--DADG--HIKLTDYGMC----KEGLG-PGDTTST-FCGTPNYIAPEILRGE------ 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 428 iDYS-KADTWAVGAIAYEIFGLANPF-YGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSARLAANV 505
Cdd:cd05617  192 -EYGfSVDWWALGVLMFEMMAGRSPFdIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQP 270
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
342-499 8.53e-05

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: 44.69  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILvewdSDGCPWLVISDFGCCLADQHVGLrlpfnSSSVERGGNGS--LMAPEVST 419
Cdd:cd06651  117 TRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGASKRLQTICM-----SGTGIRSVTGTpyWMSPEVIS 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPsavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQrEASKRPSA 499
Cdd:cd06651  188 GEGYG------RKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHARDFLGCIFV-EARHRPSA 260
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
315-489 8.64e-05

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: 44.57  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 315 LVMKNYPCTLRQYLEEQT----PSSRLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCpwLVISDFG----- 385
Cdd:cd07863   84 LVFEHVDQDLRTYLDKVPppglPAETIKDLMR-QFLRGLDFLHANCIVHRDLKPENILVT--SGGQ--VKLADFGlariy 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 386 -CCLADQHVGLRLPFNsssverggngslmAPEVSTAHSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRS 464
Cdd:cd07863  159 sCQMALTPVVVTLWYR-------------APEVLLQSTYATPV------DMWSVGCIFAEMFRRKPLFCGNSEADQLGKI 219
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126215545 465 YQEAQLP---EMPESV-------PPEARRLVRSLL 489
Cdd:cd07863  220 FDLIGLPpedDWPRDVtlprgafSPRGPRPVQSVV 254
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
270-498 8.65e-05

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: 44.35  E-value: 8.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPLlpgaladypdmlpphyypeglghgrtlFLVMKNYPC-TLRQYL--EEQTPSSRLATMMT--LQ 344
Cdd:cd14058   45 HPNIIKLYGACSNQKPV---------------------------CLVMEYAEGgSLYNVLhgKEPKPIYTAAHAMSwaLQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHL---VQQGIAHRDLKSDNILVewdSDGCPWLVISDFGCClADQHvglrlpfNSSSVERgGNGSLMAPEVsTAH 421
Cdd:cd14058   98 CAKGVAYLhsmKPKALIHRDLKPPNLLL---TNGGTVLKICDFGTA-CDIS-------THMTNNK-GSAAWMAPEV-FEG 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 422 SGPSAvidysKADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14058  165 SKYSE-----KCDVFSWGIILWEVITRRKPFDHiGGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSKDPEKRPS 237
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
299-498 9.29e-05

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: 44.33  E-value: 9.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 299 PPHY-YPEGLGHGRTLflvmkNYpctLRQYLEEQTPSSRLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcp 377
Cdd:cd05052   75 PPFYiITEFMPYGNLL-----DY---LRECNREELNAVVLLYMAT-QIASAMEYLEKKNFIHRDLAARNCLVGENH---- 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 378 wLV-ISDFGccLAdqhvglrlpfnsssverggngSLMAPEVSTAHSGPSAVIDY------------SKADTWAVGAIAYE 444
Cdd:cd05052  142 -LVkVADFG--LS---------------------RLMTGDTYTAHAGAKFPIKWtapeslaynkfsIKSDVWAFGVLLWE 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 445 I--FGLAnPFYG---QGSAHLESRSYQEaqlpEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05052  198 IatYGMS-PYPGidlSQVYELLEKGYRM----ERPEGCPPKVYELMRACWQWNPSDRPS 251
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
270-496 9.77e-05

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: 44.30  E-value: 9.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSvpllpgaladypdmlpphyypeglghgRTLFLVMKnYPC--TLRQYLEE-QTPSSRLATMMTLQLL 346
Cdd:cd14073   60 HPHIIRIYEVFENK---------------------------DKIVIVME-YASggELYDYISErRRLPEREARRIFRQIV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 347 EGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLADQHVGLRLPFNSSSVerggngsLMAPEV--STAHSGP 424
Cdd:cd14073  112 SAVHYCHKNGVVHRDLKLENILLDQNGN----AKIADFGLSNLYSKDKLLQTFCGSPL-------YASPEIvnGTPYQGP 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 425 savidysKADTWAVGAIAYEIFGLANPFYGQGSAHLeSRSYQEAQLPEMPEsvPPEARRLVRSLLQREASKR 496
Cdd:cd14073  181 -------EVDCWSLGVLLYTLVYGTMPFDGSDFKRL-VKQISSGDYREPTQ--PSDASGLIRWMLTVNPKRR 242
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
265-508 1.04e-04

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: 44.60  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 265 KQLAPHPNIIRVFRAFTSSVPLLPGALadypdmlppHYYPEGLGHGRTLFLVMKNYPCTlrQYLEEQTPSSRLATMmtlq 344
Cdd:cd06639   73 RSLPNHPNVVKFYGMFYKADQYVGGQL---------WLVLELCNGGSVTELVKGLLKCG--QRLDEAMISYILYGA---- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 lLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCPWLVisDFGccLADQHVGLRLPFNSSSvergGNGSLMAPEVSTAHSGp 424
Cdd:cd06639  138 -LLGLQHLHNNRIIHRDVKGNNILLT--TEGGVKLV--DFG--VSAQLTSARLRRNTSV----GTPFWMAPEVIACEQQ- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 425 savIDYS---KADTWAVGAIAYEIfglanpfyGQGSAHLeSRSYQEAQLPEMPESVPPEAR----------RLVRSLLQR 491
Cdd:cd06639  206 ---YDYSydaRCDVWSLGITAIEL--------ADGDPPL-FDMHPVKALFKIPRNPPPTLLnpekwcrgfsHFISQCLIK 273
                        250
                 ....*....|....*..
gi 126215545 492 EASKRPSarlaanVLHL 508
Cdd:cd06639  274 DFEKRPS------VTHL 284
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
324-467 1.06e-04

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: 44.17  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 324 LRQYLEEQTPSSRLATM--MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGC---CLADQHV---GL 395
Cdd:cd05112   86 LSDYLRTQRGLFSAETLlgMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQ----VVKVSDFGMtrfVLDDQYTsstGT 161
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 396 RLPFNSSSverggngslmaPEVsTAHSGPSavidySKADTWAVGAIAYEIFglanpfyGQGSAHLESRSYQE 467
Cdd:cd05112  162 KFPVKWSS-----------PEV-FSFSRYS-----SKSDVWSFGVLMWEVF-------SEGKIPYENRSNSE 209
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
340-501 1.09e-04

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: 44.35  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 340 MMTLQLLEGVDHLV-QQGIAHRDLKSDNILVewDSDGcpWLVISDFGccladqhVGLRLpFNSSSVERGGNGSLMAPEVS 418
Cdd:cd06620  108 KIAVAVLEGLTYLYnVHRIIHRDIKPSNILV--NSKG--QIKLCDFG-------VSGEL-INSIADTFVGTSTYMSPERI 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHsgpsaviDYS-KADTWAVGAIAYEIFGLANPFYG-----QGSAHLES------RSYQEAQlPEMPESV--PPEARRL 484
Cdd:cd06620  176 QGG-------KYSvKSDVWSLGLSIIELALGEFPFAGsndddDGYNGPMGildllqRIVNEPP-PRLPKDRifPKDLRDF 247
                        170
                 ....*....|....*..
gi 126215545 485 VRSLLQREASKRPSARL 501
Cdd:cd06620  248 VDRCLLKDPRERPSPQL 264
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
313-503 1.13e-04

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: 44.39  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYPCTLRQYLEEQTPSSRLATMM----TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCL 388
Cdd:cd07836   73 LMLVFEYMDKDLKKYMDTHGVRGALDPNTvksfTYQLLKGIAFCHENRVLHRDLKPQNLLI--NKRG--ELKLADFGLAR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 AdqhvgLRLPFNSSSVE------RggngslmAPEVSTAHSGPSAVIdyskaDTWAVGAIAYEIFGLANPFYGQGSAH--- 459
Cdd:cd07836  149 A-----FGIPVNTFSNEvvtlwyR-------APDVLLGSRTYSTSI-----DIWSVGCIMAEMITGRPLFPGTNNEDqll 211
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 460 ---------LESRSYQEAQLPEMPESVP-----------PEARRLVRSLLQREASKRPSARLAA 503
Cdd:cd07836  212 kifrimgtpTESTWPGISQLPEYKPTFPryppqdlqqlfPHADPLGIDLLHRLLQLNPELRISA 275
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
322-496 1.16e-04

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: 44.28  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 322 CTLRQYLE----------EQTPSSRLATMMTLQLLEGVDHL--VQQGIAHRDLKSDNILVEwDSDGCPWLVISDFGCC-- 387
Cdd:cd14041   87 CTVLEYCEgndldfylkqHKLMSEKEARSIIMQIVNALKYLneIKPPIIHYDLKPGNILLV-NGTACGEIKITDFGLSki 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 388 LADQHVGlrlPFNSSSVERGGNGSL--MAPEVSTAHSGPSAVIDysKADTWAVGAIAYEIFGLANPFYGQGSAH--LESR 463
Cdd:cd14041  166 MDDDSYN---SVDGMELTSQGAGTYwyLPPECFVVGKEPPKISN--KVDVWSVGVIFYQCLYGRKPFGHNQSQQdiLQEN 240
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 126215545 464 SY---QEAQLPEMPeSVPPEARRLVRSLLQREASKR 496
Cdd:cd14041  241 TIlkaTEVQFPPKP-VVTPEAKAFIRRCLAYRKEDR 275
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
341-499 1.16e-04

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: 43.98  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEwdSDGCPWLviSDFG----CCLADQHVGlrLPFnsssverggngsLMAPE 416
Cdd:cd06607  106 ICHGALQGLAYLHSHNRIHRDVKAGNILLT--EPGTVKL--ADFGsaslVCPANSFVG--TPY------------WMAPE 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VSTA-HSGPsavidYS-KADTWAVGAIAYEIFGLANPFYGQGSAhleSRSYQEAQ-----LPEMPESVppEARRLVRSLL 489
Cdd:cd06607  168 VILAmDEGQ-----YDgKVDVWSLGITCIELAERKPPLFNMNAM---SALYHIAQndsptLSSGEWSD--DFRNFVDSCL 237
                        170
                 ....*....|
gi 126215545 490 QREASKRPSA 499
Cdd:cd06607  238 QKIPQDRPSA 247
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
330-496 1.18e-04

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: 44.25  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 330 EQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCpWLVISDFGCCL-ADQHVGLRLPFNSSSvergg 408
Cdd:cd14170   95 DQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNA-ILKLTDFGFAKeTTSHNSLTTPCYTPY----- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 ngsLMAPEVStahsGPSaviDYSKA-DTWAVGAIAYEIFGLANPFYGQG----SAHLESR---SYQEAQLPEMPEsVPPE 480
Cdd:cd14170  169 ---YVAPEVL----GPE---KYDKScDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRirmGQYEFPNPEWSE-VSEE 237
                        170
                 ....*....|....*.
gi 126215545 481 ARRLVRSLLQREASKR 496
Cdd:cd14170  238 VKMLIRNLLKTEPTQR 253
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
344-488 1.22e-04

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 44.28  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLAdqhvglrlpfNSSSVerggNGSLMAPEVSTA-HS 422
Cdd:cd07858  116 QLLRGLKYIHSANVLHRDLKPSNLLLNANCD----LKICDFG--LA----------RTTSE----KGDFMTEYVVTRwYR 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 423 GPSAVI---DYSKA-DTWAVGAIAYEIFGLANPFYGQGSAH--------LESRSyqEAQLPEMPEsvpPEARRLVRSL 488
Cdd:cd07858  176 APELLLncsEYTTAiDVWSVGCIFAELLGRKPLFPGKDYVHqlklitelLGSPS--EEDLGFIRN---EKARRYIRSL 248
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
338-489 1.34e-04

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: 44.29  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 338 ATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCLADQHVGL-RlpfNSSSVergGNGSLMAPE 416
Cdd:cd05596  127 ARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL--DASG--HLKLADFGTCMKMDKDGLvR---SDTAV---GTPDYISPE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 417 VSTAHSGPSAvidYSK-ADTWAVGAIAYEIFGLANPFYGQGSA--------HLESRSYqeaqlPEMPEsVPPEARRLVRS 487
Cdd:cd05596  197 VLKSQGGDGV---YGReCDWWSVGVFLYEMLVGDTPFYADSLVgtygkimnHKNSLQF-----PDDVE-ISKDAKSLICA 267

                 ..
gi 126215545 488 LL 489
Cdd:cd05596  268 FL 269
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
352-514 1.38e-04

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: 44.13  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 352 LVQQGIAHRDLKSDNILVewDSDG-CPwlvISDFGCCLADQHVGLrlpfnsSSVERGGNGSLMAPEV-STAHSGPSavid 429
Cdd:cd05590  112 LHDKGIIYRDLKLDNVLL--DHEGhCK---LADFGMCKEGIFNGK------TTSTFCGTPDYIAPEIlQEMLYGPS---- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 430 yskADTWAVGAIAYEIFGLANPFYGQGSAHLesrsyQEAQLPE---MPESVPPEARRLVRSLLqreaSKRPSARLAAnvl 506
Cdd:cd05590  177 ---VDWWAMGVLLYEMLCGHAPFEAENEDDL-----FEAILNDevvYPTWLSQDAVDILKAFM----TKNPTMRLGS--- 241

                 ....*...
gi 126215545 507 hLSLWGEH 514
Cdd:cd05590  242 -LTLGGEE 248
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
312-498 1.52e-04

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: 43.74  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 312 TLFLVMKNYPCTLRQYLEEQTPS--SRLATMMTL-QLLEGVDHLVQQGIAHRDLKSDN-ILVewdsDGCpwLVISDFGcc 387
Cdd:cd14131   76 YLYMVMECGEIDLATILKKKRPKpiDPNFIRYYWkQMLEAVHTIHEEGIVHSDLKPANfLLV----KGR--LKLIDFG-- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 388 LADQhvglrLPFNSSSVERG---GNGSLMAPEV-----STAHSGPSAVIDYsKADTWAVGAIAYE-IFGLAnPFygqgsA 458
Cdd:cd14131  148 IAKA-----IQNDTTSIVRDsqvGTLNYMSPEAikdtsASGEGKPKSKIGR-PSDVWSLGCILYQmVYGKT-PF-----Q 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 126215545 459 HLES--RSYQEAQLP----EMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14131  216 HITNpiAKLQAIIDPnheiEFPDIPNPDLIDVMKRCLQRDPKKRPS 261
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
342-504 1.60e-04

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: 43.70  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILveWDSDGCPWLVISDFG-CCLADQHVGLRLPFNSSSverggngsLMAPEVSTA 420
Cdd:cd14104  103 VRQVCEALEFLHSKNIGHFDIRPENII--YCTRRGSYIKIIEFGqSRQLKPGDKFRLQYTSAE--------FYAPEVHQH 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPSAVidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLES--RSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14104  173 ESVSTAT------DMWSLGCLVYVLLSGINPFEAETNQQTIEniRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRMT 246

                 ....*.
gi 126215545 499 ARLAAN 504
Cdd:cd14104  247 AQEALN 252
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
344-498 1.64e-04

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: 43.41  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwLVISDFgccladqhvglrlpfnsssvergGNGSLMAPEVSTAHSG 423
Cdd:cd14102  113 QVLEAVRHCYSCGVVHRDIKDENLLVDLRTGE---LKLIDF-----------------------GSGALLKDTVYTDFDG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 -----PSAVIDYSK-----ADTWAVGAIAYEIFGLANPFYgQGSAHLESRSYqeaqlpeMPESVPPEARRLVRSLLQREA 493
Cdd:cd14102  167 trvysPPEWIRYHRyhgrsATVWSLGVLLYDMVCGDIPFE-QDEEILRGRLY-------FRRRVSPECQQLIKWCLSLRP 238

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd14102  239 SDRPT 243
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
344-500 1.83e-04

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 44.12  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwlVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MAPEvst 419
Cdd:cd05104  222 QVAKGMEFLASKNCIHRDLAARNILLTHGRIT----KICDFG--LA------RDIRNDSNYVVKGNARLpvkwMAPE--- 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 ahSGPSAVIDYsKADTWAVGAIAYEIFGLAN-PFYGQGsahLESRSY---QEAQLPEMPESVPPEARRLVRSLLQREASK 495
Cdd:cd05104  287 --SIFECVYTF-ESDVWSYGILLWEIFSLGSsPYPGMP---VDSKFYkmiKEGYRMDSPEFAPSEMYDIMRSCWDADPLK 360

                 ....*
gi 126215545 496 RPSAR 500
Cdd:cd05104  361 RPTFK 365
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
308-498 1.89e-04

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: 43.38  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 308 GHGRTLFLVMKNYPC-TLRQYLEEQTPSSRLATMM--TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDF 384
Cdd:cd05079   78 DGGNGIKLIMEFLPSgSLKEYLPRNKNKINLKQQLkyAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ----VKIGDF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GCCLAdqhVGLRLPFNSSSVERGGNGSLMAPEVsTAHSGpsaviDYSKADTWAVGAIAYEIFGLAN-------------- 450
Cdd:cd05079  154 GLTKA---IETDKEYYTVKDDLDSPVFWYAPEC-LIQSK-----FYIASDVWSFGVTLYELLTYCDsesspmtlflkmig 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 126215545 451 PFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05079  225 PTHGQMTVTRLVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTT 272
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
344-499 2.17e-04

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: 43.19  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNilvewdsdgcpwLVISDfgcclaDQHVGLRL-PFNSSSVERGGNGSL---------M 413
Cdd:cd13976   92 QIASAVAHCHRNGIVLRDLKLRK------------FVFAD------EERTKLRLeSLEDAVILEGEDDSLsdkhgcpayV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 APEV---STAHSGPSAvidyskaDTWAVGAIAYEIFGLANPFYGQGSAHLESRsYQEAQLpEMPESVPPEARRLVRSLLQ 490
Cdd:cd13976  154 SPEIlnsGATYSGKAA-------DVWSLGVILYTMLVGRYPFHDSEPASLFAK-IRRGQF-AIPETLSPRARCLIRSLLR 224

                 ....*....
gi 126215545 491 REASKRPSA 499
Cdd:cd13976  225 REPSERLTA 233
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
344-446 2.26e-04

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: 43.45  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLAdqhvglrlpfnSSSVERGGNGSLM---------- 413
Cdd:cd07849  114 QILRGLKYIHSANVLHRDLKPSNLLLNTNCD----LKICDFG--LA-----------RIADPEHDHTGFLteyvatrwyr 176
                         90       100       110
                 ....*....|....*....|....*....|....
gi 126215545 414 APEVSTAHSGpsavidYSKA-DTWAVGAIAYEIF 446
Cdd:cd07849  177 APEIMLNSKG------YTKAiDIWSVGCILAEML 204
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
344-445 2.59e-04

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: 43.19  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccladqhVGLRlpfNSSSVERG----GNGSLMAPEVST 419
Cdd:cd06611  111 QMLEALNFLHSHKVIHRDLKAGNILLTLDGD----VKLADFG-------VSAK---NKSTLQKRdtfiGTPYWMAPEVVA 176
                         90       100
                 ....*....|....*....|....*.
gi 126215545 420 AHSGPSAVIDYsKADTWAVGAIAYEI 445
Cdd:cd06611  177 CETFKDNPYDY-KADIWSLGITLIEL 201
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
311-446 3.05e-04

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: 42.75  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 311 RTLFLVMKNYPCTLRQYLEeQTPSS---RLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdSDgCPWLVISDFGCC 387
Cdd:cd07844   71 KTLTLVFEYLDTDLKQYMD-DCGGGlsmHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLI---SE-RGELKLADFGLA 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126215545 388 LADQhvglrLPFNSSSverggngslmaPEVSTAHSGPSAVI----DYSKA-DTWAVGAIAYEIF 446
Cdd:cd07844  146 RAKS-----VPSKTYS-----------NEVVTLWYRPPDVLlgstEYSTSlDMWGVGCIFYEMA 193
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
297-460 3.13e-04

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 43.03  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 297 MLPPHY-YPEGLGHGRTLFLVMKNYPCTL-----RQYLEEqtpssrlatmmtlqLLEGVDHLVQQGIAHRDLKSDNILve 370
Cdd:cd14152   66 MHPPHLaIITSFCKGRTLYSFVRDPKTSLdinktRQIAQE--------------IIKGMGYLHAKGIVHKDLKSKNVF-- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 371 WDSDGcpwLVISDFGCcladqhvglrlpFNSSSVERGGNGS-----------LMAPEVsTAHSGPSAVID---YSK-ADT 435
Cdd:cd14152  130 YDNGK---VVITDFGL------------FGISGVVQEGRREnelklphdwlcYLAPEI-VREMTPGKDEDclpFSKaADV 193
                        170       180
                 ....*....|....*....|....*
gi 126215545 436 WAVGAIAYEIFGLANPFYGQGSAHL 460
Cdd:cd14152  194 YAFGTIWYELQARDWPLKNQPAEAL 218
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
266-504 3.37e-04

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: 42.82  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSsvpllpgaladypdmlPPHYYpeglghgrTLFLVMKNypctlRQYLEEQTPSSRL----ATMM 341
Cdd:cd14077   68 SLLNHPHICRLRDFLRT----------------PNHYY--------MLFEYVDG-----GQLLDYIISHGKLkekqARKF 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFgccladqhvGLRLPFNSSSVERGGNGSL--MAPEVST 419
Cdd:cd14077  119 ARQIASALDYLHRNSIVHRDLKIENILISKSGN----IKIIDF---------GLSNLYDPRRLLRTFCGSLyfAAPELLQ 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 A--HSGPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQlpEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd14077  186 AqpYTGP-------EVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKV--EYPSYLSSECKSLISRMLVVDPKKRA 256

                 ....*..
gi 126215545 498 SARLAAN 504
Cdd:cd14077  257 TLEQVLN 263
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
344-496 4.15e-04

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: 42.26  E-value: 4.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewdsDGCPWLVISDFGCcladqhvglrlpfnsSSVERGGN------GS--LMAP 415
Cdd:cd14079  110 QIISGVEYCHRHMVVHRDLKPENLLL----DSNMNVKIADFGL---------------SNIMRDGEflktscGSpnYAAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAH--SGPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAHL----ESRSYQeaqlpeMPESVPPEARRLVRSLL 489
Cdd:cd14079  171 EVISGKlyAGP-------EVDVWSCGVILYALLCGSLPFDDEHIPNLfkkiKSGIYT------IPSHLSPGARDLIKRML 237

                 ....*..
gi 126215545 490 QREASKR 496
Cdd:cd14079  238 VVDPLKR 244
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
322-504 4.15e-04

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: 42.74  E-value: 4.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 322 CTLRQYLE----------EQTPSSRLATMMTLQLLEGVDHL--VQQGIAHRDLKSDNILVEwDSDGCPWLVISDFGCC-- 387
Cdd:cd14040   87 CTVLEYCEgndldfylkqHKLMSEKEARSIVMQIVNALRYLneIKPPIIHYDLKPGNILLV-DGTACGEIKITDFGLSki 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 388 LADQHVGLrlpfNSSSVERGGNGSL--MAPEVSTAHSGPSAVIDysKADTWAVGAIAYEIFGLANPFYGQGSAH--LESR 463
Cdd:cd14040  166 MDDDSYGV----DGMDLTSQGAGTYwyLPPECFVVGKEPPKISN--KVDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQEN 239
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 126215545 464 SY---QEAQLPEMPeSVPPEARRLVRSLLQREASKRPSARLAAN 504
Cdd:cd14040  240 TIlkaTEVQFPVKP-VVSNEAKAFIRRCLAYRKEDRFDVHQLAS 282
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
346-500 4.21e-04

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: 42.41  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVisDFGccLADQHVglrlpfNSSSVERGGNGSLMAPEVSTAHSgps 425
Cdd:cd06621  115 LKGLSYLHSRKIIHRDIKPSNILL--TRKGQVKLC--DFG--VSGELV------NSLAGTFTGTSYYMAPERIQGGP--- 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 426 avidYS-KADTWAVGAIAYEIFGLANPFYGQGSAHL---ESRSY-QEAQLPEMPESvPPEARRLVRSL-------LQREA 493
Cdd:cd06621  180 ----YSiTSDVWSLGLTLLEVAQNRFPFPPEGEPPLgpiELLSYiVNMPNPELKDE-PENGIKWSESFkdfiekcLEKDG 254

                 ....*..
gi 126215545 494 SKRPSAR 500
Cdd:cd06621  255 TRRPGPW 261
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
344-497 4.27e-04

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: 42.33  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwdsDGCPwLVISDFGCCLadqhVGLRLPFNSSSVERGGNGSLMAPEV-STAHS 422
Cdd:cd14149  116 QTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLT-VKIGDFGLAT----VKSRWSGSQQVEQPTGSILWMAPEViRMQDN 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 423 GPSAVidysKADTWAVGAIAYEIFGLANPFYGQGSAH----LESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd14149  188 NPFSF----QSDVYSYGIVLYELMTGELPYSHINNRDqiifMVGRGYASPDLSKLYKNCPKAMKRLVADCIKKVKEERP 262
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
344-496 4.82e-04

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: 42.26  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDsdgcpwLV--ISDFGccladqhvgLRLPFNSSSVERGGnGSLMAPevstAH 421
Cdd:cd05092  130 QIASGMVYLASLHFVHRDLATRNCLVGQG------LVvkIGDFG---------MSRDIYSTDYYRVG-GRTMLP----IR 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGPSAVIDYSK----ADTWAVGAIAYEIFGLA-NPFYGQGSAHLESRSYQEAQLpEMPESVPPEARRLVRSLLQREASKR 496
Cdd:cd05092  190 WMPPESILYRKftteSDIWSFGVVLWEIFTYGkQPWYQLSNTEAIECITQGREL-ERPRTCPPEVYAIMQGCWQREPQQR 268
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
336-500 4.95e-04

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: 42.35  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 336 RLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQHVGLRLPFNSSSvergGNGSLMAP 415
Cdd:cd06640  102 QIATMLK-EILKGLDYLHSEKKIHRDIKAANVLLSEQGD----VKLADFG--VAGQLTDTQIKRNTFV----GTPFWMAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EV--STAHSgpsavidySKADTWAVGAIAYEIFGLANPfygqgsahlESRSYQEAQLPEMPESVPPEA--------RRLV 485
Cdd:cd06640  171 EViqQSAYD--------SKADIWSLGITAIELAKGEPP---------NSDMHPMRVLFLIPKNNPPTLvgdfskpfKEFI 233
                        170
                 ....*....|....*
gi 126215545 486 RSLLQREASKRPSAR 500
Cdd:cd06640  234 DACLNKDPSFRPTAK 248
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
342-498 5.37e-04

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 42.09  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MAPEv 417
Cdd:cd05054  144 SFQVARGMEFLASRKCIHRDLAARNILLSENN----VVKICDFG--LA------RDIYKDPDYVRKGDARLplkwMAPE- 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 stahsgpsAVID--YS-KADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREA 493
Cdd:cd05054  211 --------SIFDkvYTtQSDVWSFGVLLWEIFSLgASPYPGVQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEP 282

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd05054  283 KERPT 287
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
341-499 5.37e-04

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: 41.92  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwLVISDFGCCLA---DQHVGLRLPfnsssvergGNGSLMAPEV 417
Cdd:cd13995  101 VTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTK-----AVLVDFGLSVQmteDVYVPKDLR---------GTEIYMSPEV 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 418 --STAHSgpsavidySKADTWAVGAIAYEIFGLANPF---YGQGS--AHLESRSYQEAQLPEMPESVPPEARRLVRSLLQ 490
Cdd:cd13995  167 ilCRGHN--------TKADIYSLGATIIHMQTGSPPWvrrYPRSAypSYLYIIHKQAPPLEDIAQDCSPAMRELLEAALE 238

                 ....*....
gi 126215545 491 REASKRPSA 499
Cdd:cd13995  239 RNPNHRSSA 247
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
266-498 5.41e-04

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 42.09  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSSVPLLP-------GALADYpdmlpphyypegLGHGRTLFLvmknypcTLRQYLEeqtpssrla 338
Cdd:cd05055   94 HLGNHENIVNLLGACTIGGPILViteyccyGDLLNF------------LRRKRESFL-------TLEDLLS--------- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 339 tmMTLQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGcPWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSL----MA 414
Cdd:cd05055  146 --FSYQVAKGMAFLASKNCIHRDLAARNVLL---THG-KIVKICDFG--LA------RDIMNDSNYVVKGNARLpvkwMA 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 415 PEvSTAHSgpsavIDYSKADTWAVGAIAYEIFGLA-NPFYG----QGSAHLESRSYQEAQlpemPESVPPEARRLVRSLL 489
Cdd:cd05055  212 PE-SIFNC-----VYTFESDVWSYGILLWEIFSLGsNPYPGmpvdSKFYKLIKEGYRMAQ----PEHAPAEIYDIMKTCW 281

                 ....*....
gi 126215545 490 QREASKRPS 498
Cdd:cd05055  282 DADPLKRPT 290
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
312-506 5.82e-04

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: 41.87  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 312 TLFLVMKNYPCTLRQYLEeQTPS---SRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCL 388
Cdd:cd07870   72 TLTFVFEYMHTDLAQYMI-QHPGglhPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE----LKLADFGLAR 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 ADQhvglrLPFNSSSVErggngslmapEVSTAHSGPSAVI---DYSKA-DTWAVGAIAYEIFGLANPFYGQGSAHLESRS 464
Cdd:cd07870  147 AKS-----IPSQTYSSE----------VVTLWYRPPDVLLgatDYSSAlDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEK 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 126215545 465 YQE-------------AQLPEM-PESVPPEARRLVRSLLQREASKRPSARLAANVL 506
Cdd:cd07870  212 IWTvlgvptedtwpgvSKLPNYkPEWFLPCKPQQLRVVWKRLSRPPKAEDLASQML 267
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
336-505 5.93e-04

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: 41.76  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 336 RLATMMTLQLlegvDHLVQQGIAHRDLKSDNILVewDSDG-------CPWLVISDfGCCladqhvglrlpfnSSSVERgg 408
Cdd:cd05576  117 RWAAEMVVAL----DALHREGIVCRDLNPNNILL--NDRGhiqltyfSRWSEVED-SCD-------------SDAIEN-- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 409 ngSLMAPEVStahsgpsAVIDYSKA-DTWAVGAIAYEIFglanpfygQGSAHLESR--SYQEAQLPEMPESVPPEARRLV 485
Cdd:cd05576  175 --MYCAPEVG-------GISEETEAcDWWSLGALLFELL--------TGKALVECHpaGINTHTTLNIPEWVSEEARSLL 237
                        170       180
                 ....*....|....*....|
gi 126215545 486 RSLLQREaskrPSARLAANV 505
Cdd:cd05576  238 QQLLQFN----PTERLGAGV 253
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
270-444 6.20e-04

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: 42.28  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTssvpllpgaladyPDmlpphyypEGLGHGRTLFLVMKNYPCTLRQYLEEQTPSSRLATMMTLQLLEGV 349
Cdd:cd07851   73 HENVIGLLDVFT-------------PA--------SSLEDFQDVYLVTHLMGADLNNIVKCQKLSDDHIQFLVYQILRGL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 350 DHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGccLADQ-------HVGLRLpfnsssverggngsLMAPEV--STA 420
Cdd:cd07851  132 KYIHSAGIIHRDLKPSNLAVNEDCE----LKILDFG--LARHtddemtgYVATRW--------------YRAPEImlNWM 191
                        170       180
                 ....*....|....*....|....*
gi 126215545 421 HsgpsavidYSKA-DTWAVGAIAYE 444
Cdd:cd07851  192 H--------YNQTvDIWSVGCIMAE 208
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
342-459 6.23e-04

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: 42.24  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 342 TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVISDFG-CCLADQHVglrLPFNSSSVERggngslmAPEVSTA 420
Cdd:cd14212  109 LQQLLDALSVLKDARIIHCDLKPENILL--VNLDSPEIKLIDFGsACFENYTL---YTYIQSRFYR-------SPEVLLG 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 126215545 421 HSgpsavidYSKA-DTWAVGAIAYEIFgLANPFYGQGSAH 459
Cdd:cd14212  177 LP-------YSTAiDMWSLGCIAAELF-LGLPLFPGNSEY 208
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
305-500 7.30e-04

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: 41.58  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 305 EGLGHGRTLFLvMKNYPctlrqyLEEqtpsSRLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDF 384
Cdd:cd06642   82 EYLGGGSALDL-LKPGP------LEE----TYIATILR-EILKGLDYLHSERKIHRDIKAANVLLSEQGD----VKLADF 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GccLADQHVGLRLPFNSSSvergGNGSLMAPEVSTahsgpSAVIDYsKADTWAVGAIAYEIFGLANPFygqgsahleSRS 464
Cdd:cd06642  146 G--VAGQLTDTQIKRNTFV----GTPFWMAPEVIK-----QSAYDF-KADIWSLGITAIELAKGEPPN---------SDL 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 126215545 465 YQEAQLPEMPESVPPEA--------RRLVRSLLQREASKRPSAR 500
Cdd:cd06642  205 HPMRVLFLIPKNSPPTLegqhskpfKEFVEACLNKDPRFRPTAK 248
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
344-507 8.65e-04

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: 41.53  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewdsdGCPWLV-ISDFGCCladqhvglRLPFNSSSVERGGNGSL----MAPEvS 418
Cdd:cd05094  131 QIASGMVYLASQHFVHRDLATRNCLV-----GANLLVkIGDFGMS--------RDVYSTDYYRVGGHTMLpirwMPPE-S 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHSGPSavidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05094  197 IMYRKFT-----TESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLN 271

                 ....*....
gi 126215545 499 ARLAANVLH 507
Cdd:cd05094  272 IKEIYKILH 280
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
341-499 8.68e-04

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: 41.56  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQ-GIAHRDLKSDNILVewDSDGcpWLVISDFGccladqhVGLRLpFNSSSVERGGNGSLMAPEvst 419
Cdd:cd06605  104 IAVAVVKGLIYLHEKhKIIHRDVKPSNILV--NSRG--QVKLCDFG-------VSGQL-VDSLAKTFVGTRSYMAPE--- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPsaviDYS-KADTWAVGAIAYEI----FGLANPFYGQGSAHLESRSY--QEAQlPEMPESV-PPEARRLVRSLLQR 491
Cdd:cd06605  169 RISGG----KYTvKSDIWSLGLSLVELatgrFPYPPPNAKPSMMIFELLSYivDEPP-PLLPSGKfSPDFQDFVSQCLQK 243

                 ....*...
gi 126215545 492 EASKRPSA 499
Cdd:cd06605  244 DPTERPSY 251
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
337-388 8.93e-04

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 41.57  E-value: 8.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126215545 337 LATMMTLQLLEGVDHLVQQGIAHRDLKSDNILV------EWDSDGC-----PWLVISDFGCCL 388
Cdd:cd13981  107 LAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicaDWPGEGEngwlsKGLKLIDFGRSI 169
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
336-488 9.53e-04

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: 41.54  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 336 RLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladqhVGLRLPFNSSSVERGGN--GSLM 413
Cdd:cd05626  101 VLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGH----IKLTDFGLC-----TGFRWTHNSKYYQKGSHirQDSM 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 414 AP-----EVST----------------------AHS--------GPSAVI--DYSK-ADTWAVGAIAYEIFGLANPFYGQ 455
Cdd:cd05626  172 EPsdlwdDVSNcrcgdrlktleqratkqhqrclAHSlvgtpnyiAPEVLLrkGYTQlCDWWSVGVILFEMLVGQPPFLAP 251
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126215545 456 GSAHLESRSYQEAQLPEMPESV--PPEARRLVRSL 488
Cdd:cd05626  252 TPTETQLKVINWENTLHIPPQVklSPEAVDLITKL 286
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
270-500 9.76e-04

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: 41.39  E-value: 9.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFtssvpllpgaladypdmlpphyypeglgHGRTLFLVMKNYPCTLRQYLEEQT----PSSRLATMMTlQL 345
Cdd:cd14117   65 HPNILRLYNYF----------------------------HDRKRIYLILEYAPRGELYKELQKhgrfDEQRTATFME-EL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 346 LEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCLadqhvglrlpfNSSSVERG---GNGSLMAPEVSTAHS 422
Cdd:cd14117  116 ADALHYCHEKKVIHRDIKPENLLMGYKGE----LKIADFGWSV-----------HAPSLRRRtmcGTLDYLPPEMIEGRT 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 423 GPSavidysKADTWAVGAIAYEIFgLANPFYGQGSaHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSAR 500
Cdd:cd14117  181 HDE------KVDLWCIGVLCYELL-VGMPPFESAS-HTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHPSERLPLK 250
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
344-500 1.00e-03

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: 41.31  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSD--GCPWLVISDFG---CCLADQHVGLRLPFnsssverggngslMAPEVs 418
Cdd:cd05037  110 QLASALHYLEDKKLIHGNVRGRNILLAREGLdgYPPFIKLSDPGvpiTVLSREERVDRIPW-------------IAPEC- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 taHSGPSAVIDYSkADTWAVGAIAYEIF-GLANPFYGQGSAHLESRSYQEAQLPeMPESvpPEARRLVRSLLQREASKRP 497
Cdd:cd05037  176 --LRNLQANLTIA-ADKWSFGTTLWEICsGGEEPLSALSSQEKLQFYEDQHQLP-APDC--AELAELIMQCWTYEPTKRP 249

                 ...
gi 126215545 498 SAR 500
Cdd:cd05037  250 SFR 252
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
343-452 1.04e-03

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: 41.13  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQG---IAHRDLKSDNIL----VEWDSDGCPWLVISDFGccLAdqhvglRLPFNSSSVERGGNGSLMAP 415
Cdd:cd14148   99 VQIARGMNYLHNEAivpIIHRDLKSSNILilepIENDDLSGKTLKITDFG--LA------REWHKTTKMSAAGTYAWMAP 170
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 126215545 416 EVsTAHSgpsaviDYSK-ADTWAVGAIAYEIFGLANPF 452
Cdd:cd14148  171 EV-IRLS------LFSKsSDVWSFGVLLWELLTGEVPY 201
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
344-511 1.09e-03

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: 41.02  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNiLVEWDSDGCPWLVISDFGCCLADQHvglrlpfNSSSVERGGNGSLMAPEVSTAHSG 423
Cdd:cd14024   92 QMARAVAHCHQHGVILRDLKLRR-FVFTDELRTKLVLVNLEDSCPLNGD-------DDSLTDKHGCPAYVGPEILSSRRS 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 424 PSAvidySKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQlpEMPESVPPEARRLVRSLLQREaskrPSARLAA 503
Cdd:cd14024  164 YSG----KAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAF--SLPAWLSPGARCLVSCMLRRS----PAERLKA 233

                 ....*...
gi 126215545 504 NVLHLSLW 511
Cdd:cd14024  234 SEILLHPW 241
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
344-452 1.11e-03

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: 40.91  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCPWLVISDFGccladqhvglrlpFNSSSVERG------GNGSLMAPEV 417
Cdd:cd14662  104 QLISGVSYCHSMQICHRDLKLENTLL--DGSPAPRLKICDFG-------------YSKSSVLHSqpkstvGTPAYIAPEV 168
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 126215545 418 STAHSgpsavIDYSKADTWAVGAIAYEIFGLANPF 452
Cdd:cd14662  169 LSRKE-----YDGKVADVWSCGVTLYVMLVGAYPF 198
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
270-498 1.13e-03

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: 41.21  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFRAFTSSVPL------LP-GALADYPDMLPPHYYPEGLGHGRTLFLVMknypctlrqyleEQTPSSRLATmmt 342
Cdd:cd05048   67 HPNIVCLLGVCTKEQPQcmlfeyMAhGDLHEFLVRHSPHSDVGVSSDDDGTASSL------------DQSDFLHIAI--- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 lQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGcpwLV--ISDFGccLAdqhvglRLPFnSSSVERGGNGSL-----MAP 415
Cdd:cd05048  132 -QIAAGMEYLSSHHYVHRDLAARNCLV---GDG---LTvkISDFG--LS------RDIY-SSDYYRVQSKSLlpvrwMPP 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EvstahsgpsaVIDYSK----ADTWAVGAIAYEIF--GLaNPFYGQgsahlesrSYQEA-------QLPEMPESVPPEAR 482
Cdd:cd05048  196 E----------AILYGKftteSDVWSFGVVLWEIFsyGL-QPYYGY--------SNQEViemirsrQLLPCPEDCPARVY 256
                        250
                 ....*....|....*.
gi 126215545 483 RLVRSLLQREASKRPS 498
Cdd:cd05048  257 SLMVECWHEIPSRRPR 272
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
344-446 1.14e-03

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: 41.44  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVewdSDGCPWLVISDFGccladqhvglrlpfnsSSVERGGNGsLMAPEVSTAHSG 423
Cdd:cd14135  113 QLFLALKHLKKCNILHADIKPDNILV---NEKKNTLKLCDFG----------------SASDIGENE-ITPYLVSRFYRA 172
                         90       100
                 ....*....|....*....|....*.
gi 126215545 424 PSAVI--DYSKA-DTWAVGAIAYEIF 446
Cdd:cd14135  173 PEIILglPYDYPiDMWSVGCTLYELY 198
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
333-452 1.19e-03

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: 41.32  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 333 PSSRL-ATMMTLQLLegvdHLVQQGIAHRDLKSDNILVewDSDG-CPwlvISDFGCC---LADqhvglrlpfNSSSVERG 407
Cdd:cd05591   96 PRARFyAAEVTLALM----FLHRHGVIYRDLKLDNILL--DAEGhCK---LADFGMCkegILN---------GKTTTTFC 157
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 126215545 408 GNGSLMAPEV-STAHSGPSavidyskADTWAVGAIAYEIFGLANPF 452
Cdd:cd05591  158 GTPDYIAPEIlQELEYGPS-------VDWWALGVLMYEMMAGQPPF 196
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
341-499 1.21e-03

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: 40.78  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCCladQHVGLRLPFNSSSVergGNGSLMAPEVSTA 420
Cdd:cd06646  111 VCRETLQGLAYLHSKGKMHRDIKGANILLTDNGD----VKLADFGVA---AKITATIAKRKSFI---GTPYWMAPEVAAV 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 421 HSGPSavidYSK-ADTWAVGAIAYEIFGLANPFYG---QGSAHLESRSyqEAQLPEMPESV--PPEARRLVRSLLQREAS 494
Cdd:cd06646  181 EKNGG----YNQlCDIWAVGITAIELAELQPPMFDlhpMRALFLMSKS--NFQPPKLKDKTkwSSTFHNFVKISLTKNPK 254

                 ....*
gi 126215545 495 KRPSA 499
Cdd:cd06646  255 KRPTA 259
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
306-454 1.21e-03

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: 40.80  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 306 GLGHGRTLFLVMKNYPC-TLRQYLEE--QTPSSRLATMMtLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpWLVIS 382
Cdd:cd05060   63 GVCKGEPLMLVMELAPLgPLLKYLKKrrEIPVSDLKELA-HQVAMGMAYLESKHFVHRDLAARNVLLVNRH----QAKIS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 383 DFGCCLAdqhvglrLPFNSS--SVERGGNGSL--MAPEvstahsgpsaVIDY----SKADTWAVGAIAYEIFGLANPFYG 454
Cdd:cd05060  138 DFGMSRA-------LGAGSDyyRATTAGRWPLkwYAPE----------CINYgkfsSKSDVWSYGVTLWEAFSYGAKPYG 200
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
313-504 1.26e-03

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: 41.12  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 313 LFLVMKNYPCTLRQYLEeQTPSSRLATMM----TLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFGCCL 388
Cdd:cd07835   73 LYLVFEFLDLDLKKYMD-SSPLTGLDPPLiksyLYQLLQGIAFCHSHRVLHRDLKPQNLLI--DTEGA--LKLADFGLAR 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 389 AdqhvgLRLPFNSSSVE------RggngslmAPEV---STAHSGPsavidyskADTWAVGAIAYE--------------- 444
Cdd:cd07835  148 A-----FGVPVRTYTHEvvtlwyR-------APEIllgSKHYSTP--------VDIWSVGCIFAEmvtrrplfpgdseid 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126215545 445 ----IF---GLANPFYGQGSAHLES--RSYQEAQLPEMPESVP---PEARRLVRSLLQREASKRPSARLAAN 504
Cdd:cd07835  208 qlfrIFrtlGTPDEDVWPGVTSLPDykPTFPKWARQDLSKVVPsldEDGLDLLSQMLVYDPAKRISAKAALQ 279
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
343-498 1.34e-03

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: 40.78  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIA---HRDLKSDNILVEWDSDGCPW----LVISDFGccLAdqhvglRLPFNSSSVERGGNGSLMAP 415
Cdd:cd14147  108 VQIARGMHYLHCEALVpviHRDLKSNNILLLQPIENDDMehktLKITDFG--LA------REWHKTTQMSAAGTYAWMAP 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EVSTAHSgpsavidYSK-ADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQLPeMPESVPPEARRLVRSLLQREA 493
Cdd:cd14147  180 EVIKAST-------FSKgSDVWSFGVLLWELLTGEVPYRGiDCLAVAYGVAVNKLTLP-IPSTCPEPFAQLMADCWAQDP 251

                 ....*
gi 126215545 494 SKRPS 498
Cdd:cd14147  252 HRRPD 256
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
343-497 1.43e-03

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: 40.78  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwlVISdfgccLADqhVGLRLPFNSSSVERG---GNGSLMAPEvST 419
Cdd:cd08229  135 VQLCSALEHMHSRRVMHRDIKPANVFITATG------VVK-----LGD--LGLGRFFSSKTTAAHslvGTPYYMSPE-RI 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AHSGPSAvidysKADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQLPEMP-ESVPPEARRLVRSLLQREASKRP 497
Cdd:cd08229  201 HENGYNF-----KSDIWSLGCLLYEMAALQSPFYGdKMNLYSLCKKIEQCDYPPLPsDHYSEELRQLVNMCINPDPEKRP 275
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
352-458 1.51e-03

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: 40.87  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 352 LVQQGIAHRDLKSDNILVewDSDGcpWLVISDFGCCladqHVGLRlPFNSSSVeRGGNGSLMAPEVSTAHsgpsaviDYS 431
Cdd:cd05588  112 LHEKGIIYRDLKLDNVLL--DSEG--HIKLTDYGMC----KEGLR-PGDTTST-FCGTPNYIAPEILRGE-------DYG 174
                         90       100
                 ....*....|....*....|....*...
gi 126215545 432 -KADTWAVGAIAYEIFGLANPFYGQGSA 458
Cdd:cd05588  175 fSVDWWALGVLMFEMLAGRSPFDIVGSS 202
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
348-505 1.78e-03

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: 40.44  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVEwDSDGCPwlvISDFGCclaDQHVGLRLPFNSSSVERGGNGSLMAPEVSTAhSGPSAv 427
Cdd:cd13979  115 ALRFCHSHGIVHLDVKPANILIS-EQGVCK---LCDFGC---SVKLGEGNEVGTPRSHIGGTYTYRAPELLKG-ERVTP- 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 428 idysKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQlPEMPESVPPEARRLVRSLLQREASKRPSARLAANV 505
Cdd:cd13979  186 ----KADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLR-PDLSGLEDSEFGQRLRSLISRCWSAQPAERPNADE 258
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
344-505 2.08e-03

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: 40.63  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEWDSDgcpwLVISDFGCC-LADQHvglrlpfnsssverggngslMAPEVSTA-H 421
Cdd:cd07856  116 QILRGLKYVHSAGVIHRDLKPSNILVNENCD----LKICDFGLArIQDPQ--------------------MTGYVSTRyY 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 422 SGPSAVIDYSK----ADTWAVGAIAYEIFgLANPFYgQGSAHLESRSYQEAQLPEMPESV-----PPEARRLVRSLLQRE 492
Cdd:cd07856  172 RAPEIMLTWQKydveVDIWSAGCIFAEML-EGKPLF-PGKDHVNQFSIITELLGTPPDDVinticSENTLRFVQSLPKRE 249
                        170
                 ....*....|...
gi 126215545 493 asKRPSARLAANV 505
Cdd:cd07856  250 --RVPFSEKFKNA 260
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
343-499 2.47e-03

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: 39.91  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILV-----------EWDSDGCPWLVISDFGCCLADqhVGLRLPFNSSSVERgGNGS 411
Cdd:cd14139  111 LQVSMGLKYIHNSGLVHLDIKPSNIFIchkmqsssgvgEEVSNEEDEFLSANVVYKIGD--LGHVTSINKPQVEE-GDSR 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 412 LMAPEVSTAhsgpsaviDYS---KADTWAVGAIAYEIFGlANPFYGQGSAHLESRsyqEAQLPEMPESVPPEARRLVRSL 488
Cdd:cd14139  188 FLANEILQE--------DYRhlpKADIFALGLTVALAAG-AEPLPTNGAAWHHIR---KGNFPDVPQELPESFSSLLKNM 255
                        170
                 ....*....|.
gi 126215545 489 LQREASKRPSA 499
Cdd:cd14139  256 IQPDPEQRPSA 266
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
344-499 2.89e-03

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: 39.90  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 344 QLLEGVDHLVQQGIAHRDLKSDNILVEwdsdGCPWLVISDFGCCladqhvglrLPFNSSSV----ERGGNGSLMAPEVST 419
Cdd:cd14110  107 QILSAVDYLHSRRILHLDLRSENMIIT----EKNLLKIVDLGNA---------QPFNQGKVlmtdKKGDYVETMAPELLE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 420 AH-SGPsavidysKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQ-EAQLPEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd14110  174 GQgAGP-------QTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKgKVQLSRCYAGLSGGAVNFLKSTLCAKPWGRP 246

                 ..
gi 126215545 498 SA 499
Cdd:cd14110  247 TA 248
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
266-497 2.93e-03

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: 39.98  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 266 QLAPHPNIIRVFRAFTSSVPL-LPGALADYPDMLpphyypEGLGHGRtlflVMKNYPCTLRQYLEEQTPSSRLATMMTLQ 344
Cdd:cd05089   58 KLGHHPNIINLLGACENRGYLyIAIEYAPYGNLL------DFLRKSR----VLETDPAFAKEHGTASTLTSQQLLQFASD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVEWDsdgcpwLV--ISDFGCCLADQ----HVGLRLPFNSSSVErggngslmapevS 418
Cdd:cd05089  128 VAKGMQYLSEKQFIHRDLAARNVLVGEN------LVskIADFGLSRGEEvyvkKTMGRLPVRWMAIE------------S 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 419 TAHSgpsavIDYSKADTWAVGAIAYEIFGL-ANPFYGQGSAHLESRSYQEAQLpEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd05089  190 LNYS-----VYTTKSDVWSFGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRM-EKPRNCDDEVYELMRQCWRDRPYERP 263
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
310-498 2.96e-03

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 39.91  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 310 GRTLFLVMKNYP-----CTLRQYlEEQTPSSRLATMMTlQLLEGVDHLVQQGIAHRDLKSDNILVEWDSdGCPwlvISDF 384
Cdd:cd05064   78 GNTMMIVTEYMSngaldSFLRKH-EGQLVAGQLMGMLP-GLASGMKYLSEMGYVHKGLAAHKVLVNSDL-VCK---ISGF 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 385 GccladqhvglRLPFNSS----SVERGGNGSL-MAPEVSTAHSGPSAvidyskADTWAVGAIAYEIFGLAN-PFYGQGSA 458
Cdd:cd05064  152 R----------RLQEDKSeaiyTTMSGKSPVLwAAPEAIQYHHFSSA------SDVWSFGIVMWEVMSYGErPYWDMSGQ 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 126215545 459 HLESRSYQEAQLPEmPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd05064  216 DVIKAVEDGFRLPA-PRNCPNLLHQLMLDCWQKERGERPR 254
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
340-502 3.03e-03

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: 39.86  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 340 MMTLQLLEGVDHLVQQGIAHRDLKSDNILVEwDSD-----------------GCPWLVIsDFG-CCLADQHvglrlpfnS 401
Cdd:cd14134  119 HIAKQLLEAVAFLHDLKLTHTDLKPENILLV-DSDyvkvynpkkkrqirvpkSTDIKLI-DFGsATFDDEY--------H 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 402 SSVerggngslmapeVSTAHSGPSAVI-----DYSkADTWAVGAIAYE----------------------IFG------- 447
Cdd:cd14134  189 SSI------------VSTRHYRAPEVIlglgwSYP-CDVWSIGCILVElytgellfqthdnlehlammerILGplpkrmi 255
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126215545 448 -----LANPFY--------GQGSAHLESRSYQEAQLPEMPESVPPEARR---LVRSLLQREASKRPSARLA 502
Cdd:cd14134  256 rrakkGAKYFYfyhgrldwPEGSSSGRSIKRVCKPLKRLMLLVDPEHRLlfdLIRKMLEYDPSKRITAKEA 326
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
323-500 3.07e-03

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: 39.70  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 323 TLRQYLEE-QTPSSRLATMMTLQLLEGVD--HLVQQGIAHRDLKSDNILVEWDSDGcpwLVISDFGCCLAdqhvgLRLPF 399
Cdd:cd14031   99 TLKTYLKRfKVMKPKVLRSWCRQILKGLQflHTRTPPIIHRDLKCDNIFITGPTGS---VKIGDLGLATL-----MRTSF 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 400 NSSSVergGNGSLMAPEVSTAHSGPSavidyskADTWAVGAIAYEIFGLANPFYG-QGSAHLESRSYQEAQLPEMPESVP 478
Cdd:cd14031  171 AKSVI---GTPEFMAPEMYEEHYDES-------VDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSGIKPASFNKVTD 240
                        170       180
                 ....*....|....*....|..
gi 126215545 479 PEARRLVRSLLQREASKRPSAR 500
Cdd:cd14031  241 PEVKEIIEGCIRQNKSERLSIK 262
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
341-446 3.21e-03

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: 39.46  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 341 MTLQLLEGVDHLVQQGIAHRDLKSDNILVewdSDGCPwLVISDFGCC---LADQHV---GLRLPFNSSSverggngslma 414
Cdd:cd05114  105 MCQDVCEGMEYLERNNFIHRDLAARNCLV---NDTGV-VKVSDFGMTryvLDDQYTsssGAKFPVKWSP----------- 169
                         90       100       110
                 ....*....|....*....|....*....|..
gi 126215545 415 PEVSTaHSGPSavidySKADTWAVGAIAYEIF 446
Cdd:cd05114  170 PEVFN-YSKFS-----SKSDVWSFGVLMWEVF 195
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
313-385 3.62e-03

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: 39.71  E-value: 3.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 313 LFLVMKNYPCTLRQYLEeQTPSSRLATMMTL-----QLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFG 385
Cdd:cd07861   74 LYLVFEFLSMDLKKYLD-SLPKGKYMDAELVksylyQILQGILFCHSRRVLHRDLKPQNLLI--DNKGV--IKLADFG 146
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
270-498 3.82e-03

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: 39.25  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 270 HPNIIRVFraftssvpllpGALADYPDMLPPHYYPEG-----LGHGRTLFLVMknypcTLRQYleeqtpssrlatmmTLQ 344
Cdd:cd05040   57 HPNLIRLY-----------GVVLSSPLMMVTELAPLGslldrLRKDQGHFLIS-----TLCDY--------------AVQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 345 LLEGVDHLVQQGIAHRDLKSDNILVEWDSdgcpwLV-ISDFGCCLA----DQHV----GLRLPFnsssverggngSLMAP 415
Cdd:cd05040  107 IANGMAYLESKRFIHRDLAARNILLASKD-----KVkIGDFGLMRAlpqnEDHYvmqeHRKVPF-----------AWCAP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 416 EvSTAHSGPSavidySKADTWAVGAIAYEIFGLAN-PFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREAS 494
Cdd:cd05040  171 E-SLKTRKFS-----HASDVWMFGVTLWEMFTYGEePWLGLNGSQILEKIDKEGERLERPDDCPQDIYNVMLQCWAHKPA 244

                 ....
gi 126215545 495 KRPS 498
Cdd:cd05040  245 DRPT 248
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
343-497 5.83e-03

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: 38.63  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 343 LQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGcpwlVISDFGCCLADQHVglrlpfNSSSVergGNGSLMAPEVSTAHS 422
Cdd:cd13975  109 LDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA----KITDLGFCKPEAMM------SGSIV---GTPIHMAPELFSGKY 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126215545 423 GPSavidyskADTWAVGAIAYEIFG----LANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRP 497
Cdd:cd13975  176 DNS-------VDVYAFGILFWYLCAghvkLPEAFEQCASKDHLWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQRP 247
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
348-498 6.26e-03

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: 38.65  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 348 GVDHLVQQGIAHRDLKSDNILVEWDSDGCPwLVISDFGccLAdQHVGlRLPFNSSSVERGGNGSL--MAPEVSTAHsgps 425
Cdd:cd14156  101 GMVYLHSKNIYHRDLNSKNCLIRVTPRGRE-AVVTDFG--LA-REVG-EMPANDPERKLSLVGSAfwMAPEMLRGE---- 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126215545 426 aviDYS-KADTWAVGAIAYEIFGL--ANP--FYGQGSAHLESRSYQeaqlpEMPESVPPEARRLVRSLLQREASKRPS 498
Cdd:cd14156  172 ---PYDrKVDVFSFGIVLCEILARipADPevLPRTGDFGLDVQAFK-----EMVPGCPEPFLDLAASCCRMDAFKRPS 241
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
335-444 7.18e-03

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: 38.89  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126215545 335 SRLATMMtLQLLEGVDHLVQQGIAHRDLKSDNILVewDSDGCpwLVISDFgccladqhvGLRLPFnssSVERGGNGSLMA 414
Cdd:cd07865  119 SEIKKVM-KMLLNGLYYIHRNKILHRDMKAANILI--TKDGV--LKLADF---------GLARAF---SLAKNSQPNRYT 181
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 126215545 415 PEVSTAHSGPSAVI----DYSKA-DTWAVGAIAYE 444
Cdd:cd07865  182 NRVVTLWYRPPELLlgerDYGPPiDMWGAGCIMAE 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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