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Conserved domains on  [gi|327284948|ref|XP_003227197|]
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PREDICTED: casein kinase I [Anolis carolinensis]

Protein Classification

STKc_CK1_delta_epsilon domain-containing protein (domain architecture ID 10197527)

STKc_CK1_delta_epsilon domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-282 0e+00

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 648.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRTHQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14125  161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 327284948 248 FSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGF 282
Cdd:cd14125  241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
8-285 8.99e-36

Serine/threonine protein kinase [Signal transduction mechanisms];


:

Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 135.64  E-value: 8.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIatgEEVAIK-----LECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVM 82
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDR---KLVALKvlakkLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  83 ELL-GPSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDA 159
Cdd:COG0515   78 EYVdGGSLEDLLKKIGRkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 160 RTHQHIPYRENKNLtGTARYASINTHLGIEQ---SRRDDLESLGYVLMYFNLGSLPWQGLKAA-TKRQKYERISEKKMST 235
Cdd:COG0515  156 GSTSSIPALPSTSV-GTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsATSQTLKIILELPTPS 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 327284948 236 PIEVLCKGYPSEFSTYLN--FCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYD 285
Cdd:COG0515  235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
 
Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-282 0e+00

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 648.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRTHQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14125  161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 327284948 248 FSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGF 282
Cdd:cd14125  241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-273 6.82e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 96.56  E-value: 6.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   6 GNKYRLGRKIGSGSFGDIY---LGANIATGEEVAIKLECVKTKhpQLHIESKFYKMMQ--------------GGVGIPSI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLENE--TIVMETLVYNNIYdidkialwknihniDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  69 KWCGA----EGDYNVMVMELLGPSLEDLFN--FCSRKFSLKTVLLladQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 143 nlvYIIDFGLAKKYrdARTHQHIPY-RENKNL-TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA-- 218
Cdd:PHA02882 166 ---YIIDYGIASHF--IIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHng 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 327284948 219 ----ATKRQKYERISEKKMStpIEVLCKGypseFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:PHA02882 241 nlihAAKCDFIKRLHEGKIK--IKNANKF----IYDFIECVTKLSYEEKPDYDALIKIF 293
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
119-155 2.09e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749  Cd Length: 199  Bit Score: 37.96  E-value: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 327284948  119 IHSKNFIHRDVKPDNFLMGLGKkgnlVYIIDFGLAKK 155
Cdd:TIGR03724 106 LHKAGIVHGDLTTSNIIVRDDK----VYLIDFGLGKY 138
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
3-201 2.62e-03

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 225023  Cd Length: 201  Bit Score: 37.77  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   3 LRVGNKYRLG--RKIGSGSFGDIYLGAniATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGaegdYNVM 80
Cdd:COG2112   16 NVEEGKYELRveKELAKGTTSVVYLGE--WRGGEVALKVRRRDSPRRNLEKEAKILEILAGEGVTPEVYFYG----EDFI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  81 VME-LLGPSLEDLFNFCSRKFSLKTV---LLLADQMISRIEyihsknfIHRdvkPDNFLMGLGKKgnlVYIIDFGLAKKY 156
Cdd:COG2112   90 RMEyIDGRPLGKLEIGGDRKHLLRVLekaYKLDRLGIEHGE-------LSR---PWKNVLVNDRD---VYIIDFDSATFK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 327284948 157 RDARthqhipyrenkNLTGTARYasinthLGIEQSRRDDLESLGY 201
Cdd:COG2112  157 KKPR-----------NVTQALSL------LFREGLRIEKTILRGY 184
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
8-285 8.99e-36

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 135.64  E-value: 8.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIatgEEVAIK-----LECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVM 82
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDR---KLVALKvlakkLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  83 ELL-GPSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDA 159
Cdd:COG0515   78 EYVdGGSLEDLLKKIGRkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 160 RTHQHIPYRENKNLtGTARYASINTHLGIEQ---SRRDDLESLGYVLMYFNLGSLPWQGLKAA-TKRQKYERISEKKMST 235
Cdd:COG0515  156 GSTSSIPALPSTSV-GTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsATSQTLKIILELPTPS 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 327284948 236 PIEVLCKGYPSEFSTYLN--FCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYD 285
Cdd:COG0515  235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-238 1.02e-27

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 109.54  E-value: 1.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948     9 YRLGRKIGSGSFGDIYLGANIATGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948    86 -GPSLEDLFNFCsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYRDARTHqh 164
Cdd:smart00220  80 eGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL--LDEDGH-VKLADFGLARQLDPGEKL-- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327284948   165 ipyrenKNLTGTARYASINTHLGIEQSRRDDLESLGyVLMY-FNLGSLPWQGlkAATKRQKYERISEKKMSTPIE 238
Cdd:smart00220 154 ------TTFVGTPEYMAPEVLLGKGYGKAVDIWSLG-VILYeLLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219
Pkinase pfam00069
Protein kinase domain;
9-215 2.85e-24

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 99.59  E-value: 2.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948    9 YRLGRKIGSGSFGDIYLGANIATGEEVAIKleCVKT---------------------KHPqlHIeSKFYKMMQggvgips 67
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAVK--KIKKekikkkkdknvlreikilkklNHP--NI-VRLYDVFE------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   68 ikwcgaEGDYNVMVMELLGPSleDLFNFCSRK--FSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLv 145
Cdd:pfam00069  69 ------DKDHLYLVLEYVEGG--SLFDLLSEKgaFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENIL--IDEDGNL- 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327284948  146 YIIDFGLAKKYrdartHQHIPYrenKNLTGTARYAS----INTHLGIEQsrrdDLESLGYVLMYFNLGSLPWQG 215
Cdd:pfam00069 138 KITDFGLAKQL-----SSGSKL---TTFVGTPWYMApevlRGNPYGPKV----DVWSLGCILYELLTGKPPFPG 199
pknD PRK13184
serine/threonine-protein kinase; Reviewed
8-239 9.86e-14

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 71.73  E-value: 9.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIK-----LECVKTKHPQLHIESKFY-KMMQGGVgIPSIKWCgAEGDYNVMV 81
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKkiredLSENPLLKKRFLREAKIAaDLIHPGI-VPVYSIC-SDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  82 MELL-GPSLEDLFNFCSRKFSL----------KTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKgnlVYIIDF 150
Cdd:PRK13184  81 MPYIeGYTLKSLLKSVWQKESLskelaektsvGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGE---VVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 151 GLAK---KYRDARTHQHIPYREN--KNLT------GTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWqglkaa 219
Cdd:PRK13184 158 GAAIfkkLEEEDLLDIDVDERNIcySSMTipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY------ 231
                        250       260
                 ....*....|....*....|.
gi 327284948 220 tKRQKYERISEK-KMSTPIEV 239
Cdd:PRK13184 232 -RRKKGRKISYRdVILSPIEV 251
 
Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-282 0e+00

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 648.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRTHQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14125  161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 327284948 248 FSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGF 282
Cdd:cd14125  241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
8-273 0e+00

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 542.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14016   81 SLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAKKYRDPRTGKHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14016  161 REGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKEKYEKIGEKKMNTSPEELCKGLPKE 240
                        250       260
                 ....*....|....*....|....*.
gi 327284948 248 FSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14016  241 FAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
8-273 4.95e-179

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 502.81  E-value: 4.95e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14128    1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14128   81 SLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDSRTRQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14128  161 REDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAE 240
                        250       260
                 ....*....|....*....|....*.
gi 327284948 248 FSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14128  241 FAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
9-290 2.25e-149

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 428.38  E-value: 2.25e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   9 YRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPS 88
Cdd:cd14126    2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  89 LEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGL--GKKGNLVYIIDFGLAKKYRDARTHQHIP 166
Cdd:cd14126   82 LEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRqsTKKQHVIHIIDFGLAKEYIDPETNKHIP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 167 YRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPS 246
Cdd:cd14126  162 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 327284948 247 EFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDW 290
Cdd:cd14126  242 EMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDW 285
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
9-281 2.84e-136

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 394.55  E-value: 2.84e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   9 YRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPS 88
Cdd:cd14127    2 YKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  89 LEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGL--GKKGNLVYIIDFGLAKKYRDARTHQHIP 166
Cdd:cd14127   82 LEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRpgTKNANVIHVVDFGMAKQYRDPKTKQHIP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 167 YRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPS 246
Cdd:cd14127  162 YREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQSTPIRDLCEGFPE 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 327284948 247 EFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQG 281
Cdd:cd14127  242 EFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
8-274 2.94e-77

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 242.93  E-value: 2.94e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLF-NFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLG-KKGNLVYIIDFGLAKKYRDARTHQHI 165
Cdd:cd14017   81 NLAELRrSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGpSDERTVYILDFGLARQYTNKDGEVER 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 166 PYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKaatkrqKYERISEKKMSTPIEVLCKGYP 245
Cdd:cd14017  161 PPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLK------DKEEVGKMKEKIDHEELLKGLP 234
                        250       260
                 ....*....|....*....|....*....
gi 327284948 246 SEFSTYLNFCRSLRFDDKPDYSYLRQLFR 274
Cdd:cd14017  235 KEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
5-273 7.32e-55

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 185.56  E-value: 7.32e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   5 VGNKYRLGRKIGSGSFGDIYLGANiATGEEVAIKLECVKTKHPQ----LHIESKFY----------KMMQGG----VGIP 66
Cdd:cd14015    8 TKRQWKLGKSIGQGGFGEIYLASD-DSTLSVGKDAKYVVKIEPHsngpLFVEMNFYqrvakpemikKWMKAKklkhLGIP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  67 SikwCGAEG-------DYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLG 139
Cdd:cd14015   87 R---YIGSGsheykgeKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLGFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 140 KKGNLVYIIDFGLAKKYRDarTHQHIPYREN--KNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLK 217
Cdd:cd14015  164 KNKDQVYLVDYGLASRYCP--NGKHKEYKEDprKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWEDNL 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327284948 218 AAT---KRQKyerisEKKMSTPIEVL--C---KGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14015  242 KNPeyvQKQK-----EKYMDDIPLLLkkCfpgKDVPEELQKYLKYVASLEYEEKPDYEKLRKIL 300
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
8-273 5.15e-46

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 160.99  E-value: 5.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14129    1 RWKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMG-LGKKGNLVYIIDFGLAKKYRDARTHQHI 165
Cdd:cd14129   81 NLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRKCYMLDFGLARQFTNSCGDVRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 166 PyRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAAtkrqkyERISEKKMSTPIEVLCKGYP 245
Cdd:cd14129  161 P-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQVGSIKERYEHRLMLKHLP 233
                        250       260
                 ....*....|....*....|....*...
gi 327284948 246 SEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14129  234 PEFSVFLDHISGLDYFTKPDYQLLVSVF 261
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
8-273 1.13e-45

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 159.81  E-value: 1.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14130    1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  88 SLEDLFNFCSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMG-LGKKGNLVYIIDFGLAKKYRDArTHQHI 165
Cdd:cd14130   81 NLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrLPSTYRKCYMLDFGLARQYTNT-TGEVR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 166 PYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMstpievLCKGYP 245
Cdd:cd14130  160 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRM------LLKHMP 233
                        250       260
                 ....*....|....*....|....*...
gi 327284948 246 SEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14130  234 SEFHLFLDHIASLDYFTKPDYQLIMSVF 261
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
6-272 3.77e-38

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025  Cd Length: 302  Bit Score: 140.75  E-value: 3.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   6 GNKYRLGRKIGSGSFGDIYLGA---NIATGEEV--AIKLEcvKTKHPQLHIESKFY----------KMMQ----GGVGIP 66
Cdd:cd14123   11 KKNWRLGKMIGKGGFGLIYLASpqvNVPVEDDAvhVIKVE--YHENGPLFSELKFYqraakpdtisKWMKskqlDYLGIP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  67 SIkWCGAEGDYN-----VMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgKK 141
Cdd:cd14123   89 TY-WGSGLTEFNgtsyrFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY-RN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 142 GNLVYIIDFGLAkkYRDARTHQHIPYREN--KNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPW-QGLK- 217
Cdd:cd14123  167 PNEVYLADYGLS--YRYCPNGNHKEYKENprKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeQNLKn 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327284948 218 -AATKRQKYERISE-----KKMSTPIEVLCkgypsEFSTYLNFCRSLRFDDKPDYSYLRQL 272
Cdd:cd14123  245 pVAVQEAKAKLLSNlpdsvLKWSTGGSSSM-----EIAQFLSRVKDLAYDEKPDYQALKKI 300
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
15-207 3.99e-34

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: 127.00  E-value: 3.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  15 IGSGSFGDIYLGANIATGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL-GPSLE 90
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKvipKEKLKKLLEELLREIEILKKLNH-PNIVKLYDVFETENFLYLVMEYCeGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  91 DLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAKKYRDARTHQHIPYRen 170
Cdd:cd00180   80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL---DSDGTVKLADFGLAKDLDSDDSLLKTTGG-- 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 327284948 171 knlTGTARYASINTHLGIEQSRRDDLESLGYVLMYFN 207
Cdd:cd00180  155 ---TTPPYYAPPELLGGRYYGPKVDIWSLGVILYELE 188
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
8-273 4.59e-34

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271024  Cd Length: 301  Bit Score: 129.24  E-value: 4.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLgANIATGEEVAIKLECVKTKHPQ----LHIESKFY------KMMQGGVGIPSIKWCGAE--- 74
Cdd:cd14122   11 EWKLGLPIGQGGFGRLYL-ADENSSESVGSDAPYVVKVEPSdngpLFTELKFYmraakpDQIQKWIKSHKLKYLGVPkyw 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  75 ---------GDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgKKGNLV 145
Cdd:cd14122   90 gsglhekngKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLSY-KNPDQV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 146 YIIDFGLAkkYRDARTHQHIPYREN--KNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGlkaATKRQ 223
Cdd:cd14122  169 YLVDYGLA--YRYCPEGVHKEYKEDpkRCHDGTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWED---NLKDP 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 327284948 224 KYERISEKKMSTPIEVL---C---KGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14122  244 NYVRDSKIRYRDNISELmekCfpgKNKPGEIRKYMETVKLLGYTEKPLYPHLREIL 299
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
8-215 1.39e-27

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: 109.21  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIKLecvktKHPQLHIESKFYKMMQ---------GGVGIPSIKWCGAEGDYN 78
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKV-----LRPELAEDEEFRERFLrearalarlSHPNIVRVYDVGEDDGRP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  79 VMVMELL-GPSLEDLFNFcSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYR 157
Cdd:cd14014   76 YIVMEYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIL--LTEDGR-VKLTDFGIARALG 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 158 DAR-THQHIPYrenknltGTARYASINTHLGIEQSRRDDLESLGyVLMYFNL-GSLPWQG 215
Cdd:cd14014  152 DSGlTQTGSVL-------GTPAYMAPEQARGGPVDPRSDIYSLG-VVLYELLtGRPPFDG 203
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
8-236 2.64e-26

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: 105.68  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIK------LECVKTK-------------HPqlHIeSKFYKMMQggvgipsi 68
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidkskLKEEIEEkikreieimkllnHP--NI-IKLYEVIE-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  69 kwcgaEGDYNVMVMELLgpSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVy 146
Cdd:cd14003   70 -----TENKIYLVMEYA--SGGELFDYIVNngRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL--LDKNGNLK- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 147 IIDFGLAKKYRDARTHQhipyrenknlT--GTARYASINTHLGIE-QSRRDDLESLGyVLMYFNL-GSLPWQGlkaATKR 222
Cdd:cd14003  140 IIDFGLSNEFRGGSLLK----------TfcGTPAYAAPEVLLGRKyDGPKADVWSLG-VILYAMLtGYLPFDD---DNDS 205
                        250
                 ....*....|....
gi 327284948 223 QKYERISEKKMSTP 236
Cdd:cd14003  206 KLFRKILKGKYPIP 219
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
63-270 7.77e-26

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026  Cd Length: 298  Bit Score: 104.92  E-value: 7.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  63 VGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:cd14124   82 LGIPSCVGFGVHDSYRFLVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAENIFVDPEDQS 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 143 NlVYIIDFGLAkkYRDARTHQHIPYRENKNLT--GTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAAT 220
Cdd:cd14124  162 E-VYLAGYGFA--FRYCPGGKHVEYREGSRSPheGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLHNT 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 327284948 221 KRQKYERisEKKMSTPIEVLCKGY-----PSEFSTYLNFCRSLRFDDKPDYSYLR 270
Cdd:cd14124  239 EDIMKQK--ERFMDDVPGFLGPCFhqkkvSEALQKYLKVVMALQYEEKPDYAMLR 291
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
8-232 2.32e-25

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: 102.94  E-value: 2.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIK-----------LECVKT--------KHPqlHIeSKFYKMMQggvgipsi 68
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidkkklksedEEMLRReieilkrlDHP--NI-VKLYEVFE-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  69 kwcgaEGDYNVMVMELL--GpsleDLFNF-CSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNL 144
Cdd:cd05117   70 -----DDKNLYLVMELCtgG----ELFDRiVKKgSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 145 VYIIDFGLAKKYRDARTHQHipyrenknLTGTARYAS--INTHLGIeqSRRDDLESLGyVLMYFNL-GSLPWQGlkaATK 221
Cdd:cd05117  141 IKIIDFGLAKIFEEGEKLKT--------VCGTPYYVApeVLKGKGY--GKKCDIWSLG-VILYILLcGYPPFYG---ETE 206
                        250
                 ....*....|.
gi 327284948 222 RQKYERISEKK 232
Cdd:cd05117  207 QELFEKILKGK 217
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-273 6.82e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 96.56  E-value: 6.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   6 GNKYRLGRKIGSGSFGDIY---LGANIATGEEVAIKLECVKTKhpQLHIESKFYKMMQ--------------GGVGIPSI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLENE--TIVMETLVYNNIYdidkialwknihniDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  69 KWCGA----EGDYNVMVMELLGPSLEDLFN--FCSRKFSLKTVLLladQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948 143 nlvYIIDFGLAKKYrdARTHQHIPY-RENKNL-TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA-- 218
Cdd:PHA02882 166 ---YIIDYGIASHF--IIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHng 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 327284948 219 ----ATKRQKYERISEKKMStpIEVLCKGypseFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:PHA02882 241 nlihAAKCDFIKRLHEGKIK--IKNANKF----IYDFIECVTKLSYEEKPDYDALIKIF 293
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
8-167 9.94e-23

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: 95.35  E-value: 9.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIK---LEcVKTKHPQLHIESKFYKMMQGgvgiPSI-KWCGA--EGDYNVMV 81
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKkinLE-SKEKKESILNEIAILKKCKH----PNIvKYYGSylKKDELWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  82 MELL-GPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgkKGnLVYIIDFGLAKKYRDAR 160
Cdd:cd05122   76 MEFCsGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTS--DG-EVKLIDFGLSAQLSDGK 152
                        170
                 ....*....|
gi 327284948 161 THQHI---PY 167
Cdd:cd05122  153 TRNTFvgtPY 162
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
8-200 5.20e-22

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: 93.35  E-value: 5.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   8 KYRLGRKIGSGSFGDIYLGANIATGEEVAIK---LECVKTKH-PQLHIESKFYKMMQGgvgiPSI-KWCGAEGD---YNV 79
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEElEALEREIRILSSLKH----PNIvRYLGTERTentLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  80 mVMELL-GPSLEDLF-NFcsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYR 157
Cdd:cd06606   77 -FLEYVpGGSLASLLkKF--GKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL--VDSDGV-VKLADFGCAKRLA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 327284948 158 DARTHQhipyrENKNLTGTARYAS---INthlGIEQSRRDDLESLG 200
Cdd:cd06606  151 EIATGE-----GTKSLRGTPYWMApevIR---GEGYGRAADIWSLG 188
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
9-168 1.41e-20

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: 89.22  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948   9 YRLGRKIGSGSFGDIYLGANIATGEEVAIK-LECVKTKHPQLHIESKFYKMMQGGVGIP-------SIKWcgAEGDYNVM 80
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKkIKNDFRHPKAALREIKLLKHLNDVEGHPnivklldVFEH--RGGNHLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327284948  81 VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgkKGNLVYIIDFGLAKKY-RDA 159
Cdd:cd05118   79 VFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFL