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Conserved domains on  [gi|153281169|ref|NP_006473|]
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dual specificity tyrosine-phosphorylation-regulated kinase 2 isoform 2 [Homo sapiens]

Protein Classification

dual specificity tyrosine-phosphorylation-regulated kinase( domain architecture ID 10197781)

dual specificity tyrosine-phosphorylation-regulated kinase (DYRK) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates; it autophosphorylates itself on tyrosine residues and phosphorylates its substrates exclusively on S/T residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
156-535 0e+00

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 857.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 156 PEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQ 235
Cdd:cd14224    1 PEQAMKQYMHKLTAYEHHEIFNYPEIYFVGPNAKKRQGVIGGPNNGGYDDEQGSYIHVPHDHIAYRYEVLKVIGKGSFGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 236 VVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKN 315
Cdd:cd14224   81 VVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMTFELLSMNLYELIKKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 316 KFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVIL 395
Cdd:cd14224  161 KFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 396 GARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSV 475
Cdd:cd14224  241 GARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLLETSKRAKNFISSKGYPRYCTVTTLPDGSV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 476 VLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14224  321 VLNGGRSRRGKMRGPPGSKDWVTALKGCDDPLFLDFLKRCLEWDPAARMTPSQALRHPWL 380
 
Name Accession Description Interval E-value
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
156-535 0e+00

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 857.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 156 PEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQ 235
Cdd:cd14224    1 PEQAMKQYMHKLTAYEHHEIFNYPEIYFVGPNAKKRQGVIGGPNNGGYDDEQGSYIHVPHDHIAYRYEVLKVIGKGSFGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 236 VVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKN 315
Cdd:cd14224   81 VVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMTFELLSMNLYELIKKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 316 KFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVIL 395
Cdd:cd14224  161 KFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 396 GARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSV 475
Cdd:cd14224  241 GARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLLETSKRAKNFISSKGYPRYCTVTTLPDGSV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 476 VLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14224  321 VLNGGRSRRGKMRGPPGSKDWVTALKGCDDPLFLDFLKRCLEWDPAARMTPSQALRHPWL 380
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
222-535 6.94e-87

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 270.56  E-value: 6.94e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK--RFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKikKDRERILREIKILKKLKHP------NIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   300 TFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH-- 376
Cdd:smart00220  75 VMEYCEGgDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH--VKLADFGLARQLDpg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIellgmpsqklldaskraknfv 456
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI--------------------- 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169   457 sskgypryctvttlsdgsvvlnggrsRRGKLRGPPESREWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:smart00220 210 --------------------------GKPKPPFPPPEWDI--------SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
222-535 2.28e-62

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 206.31  E-value: 2.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR---FHRQAAEEIRILEHLRKqdkdntMNVIHMLENFTFRNHIC 298
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLNH------PNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  299 MTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH- 376
Cdd:pfam00069  75 LVLEYVEGgSLFDLLSEKG--AFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGN--LKITDFGLARQLNs 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  377 -QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIellgmpsqklldaskraknf 455
Cdd:pfam00069 151 gSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-------------------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  456 vsskgypryctvttlsdgsvvlnggrsrRGKLRGPPESREWGNALKgcddplflDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:pfam00069 211 ----------------------------DQPYAFPELPSNLSEEAK--------DLLKKLLKKDPSKRLTATEALQHPWF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
222-579 1.44e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 160.29  E-value: 1.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVhqhVALKMVR----NEKRFHRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHI 297
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAkkleSKSKEVERFLREIQILASLNHPP-----NIVKLYDFFQDEGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLS-MNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSC-- 373
Cdd:COG0515   74 YLVMEYVDgGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV-VKLIDFGLAKll 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 -------YEHQRVYTYIQSRFYRAPEVILG---ARYGMPIDMWSLGCILAELLTGYPLLPGEDEG---DQLACMIELLGM 440
Cdd:COG0515  153 pdpgstsSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSsatSQTLKIILELPT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 441 PSQKlldaskraknfvsskgypryctvttlsdgsvvlnggrsrrgklrgppesREWGNALKGCDDPLFLDFLKQCLEWDP 520
Cdd:COG0515  233 PSLA-------------------------------------------------SPLSPSNPELISKAASDLLKKLLAKDP 263
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 521 AVRMTPGQALRHPWLRRR--------LPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTN 579
Cdd:COG0515  264 KNRLSSSSDLSHDLLAHLklkesdlsDLLKPDDSAPLRLSLPPSLEALISSLNSLAISGSDLKLDDS 330
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
221-542 5.18e-42

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 154.53  E-value: 5.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVL-KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK---------------RFHRQAAEEIRILEHLRKQdkdntmNV 284
Cdd:PTZ00024   9 RYIQKgAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrqlvgmcGIHFTTLRELKIMNEIKHE------NI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 285 IHMLENFTFRNHICMTFELLSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgI 364
Cdd:PTZ00024  83 MGLVDVYVEGDFINLVMDIMASDLKKVVDRKIR--LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI--C 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 365 KVIDFG-SSCYEHQRVY------TYIQSR----------FYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:PTZ00024 159 KIADFGlARRYGYPPYSdtlskdETMQRReemtskvvtlWYRAPELLMGAeKYHFAVDMWSVGCIFAELLTGKPLFPGEN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 427 EGDQLACMIELLGMPSQklldaskraKNFVSSKGYPRYCTVTtlsdgsvvlnggrsrrgklrgPPESREWGNALKGCDDP 506
Cdd:PTZ00024 239 EIDQLGRIFELLGTPNE---------DNWPQAKKLPLYTEFT---------------------PRKPKDLKTIFPNASDD 288
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 153281169 507 LfLDFLKQCLEWDPAVRMTPGQALRHPWLRRRlPKP 542
Cdd:PTZ00024 289 A-IDLLQSLLKLNPLERISAKEALKHEYFKSD-PLP 322
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
221-418 3.11e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 91.39  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE--------KRFHR--QAAEEiriLEH-----LRKQDKDNTMNVI 285
Cdd:NF033483   8 RYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDlardpefvARFRReaQSAAS---LSHpnivsVYDVGEDGGIPYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 286 HMlenftfrnhicmtfELLS-MNLYELIKKNKfqgfslPL-VRK---FAHSILQCLDALHKNRIIHCDLKPENILLKQQG 360
Cdd:NF033483  85 VM--------------EYVDgRTLKDYIREHG------PLsPEEaveIMIQILSALEHAHRNGIVHRDIKPQNILITKDG 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 361 RsgIKVIDFG-------SSCYEHQRVytyIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:NF033483 145 R--VKVTDFGiaralssTTMTQTNSV---LGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTG 204
 
Name Accession Description Interval E-value
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
156-535 0e+00

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 857.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 156 PEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQ 235
Cdd:cd14224    1 PEQAMKQYMHKLTAYEHHEIFNYPEIYFVGPNAKKRQGVIGGPNNGGYDDEQGSYIHVPHDHIAYRYEVLKVIGKGSFGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 236 VVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKN 315
Cdd:cd14224   81 VVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMTFELLSMNLYELIKKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 316 KFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVIL 395
Cdd:cd14224  161 KFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 396 GARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSV 475
Cdd:cd14224  241 GARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLLETSKRAKNFISSKGYPRYCTVTTLPDGSV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 476 VLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14224  321 VLNGGRSRRGKMRGPPGSKDWVTALKGCDDPLFLDFLKRCLEWDPAARMTPSQALRHPWL 380
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
178-535 0e+00

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 610.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 178 YPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK 257
Cdd:cd14225    1 YPEIWFLGLEAKKIEGVPGAPQNNGYDDENGSYLKVLHDHIAYRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 258 RFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLD 337
Cdd:cd14225   81 RFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 338 ALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd14225  161 LLYRERIIHCDLKPENILLRQRGQSSIKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 418 GYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRyctvttlsdgSVVLNGGRSRRgklrgpPESREWG 497
Cdd:cd14225  241 GYPLFPGENEVEQLACIMEVLGLPPPELIENAQRRRLFFDSKGNPR----------CITNSKGKKRR------PNSKDLA 304
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 153281169 498 NALKgCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14225  305 SALK-TSDPLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
208-535 0e+00

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 593.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 208 GSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHM 287
Cdd:cd14210    1 GDYKVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLNDNDPDDKHNIVRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 288 LENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVI 367
Cdd:cd14210   81 KDSFIFRGHLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLD 447
Cdd:cd14210  161 DFGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPPKSLID 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 448 ASKRAKNFVSSKGYPRYCTvttlsdgsvvlnggrSRRGKLRgPPESREWGNALKgCDDPLFLDFLKQCLEWDPAVRMTPG 527
Cdd:cd14210  241 KASRRKKFFDSNGKPRPTT---------------NSKGKKR-RPGSKSLAQVLK-CDDPSFLDFLKKCLRWDPSERMTPE 303

                 ....*...
gi 153281169 528 QALRHPWL 535
Cdd:cd14210  304 EALQHPWI 311
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
222-535 5.91e-158

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: 452.88  E-value: 5.91e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKADKYHIVRLKDVFYFKNHLCIVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYT 381
Cdd:cd14133   81 ELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFLTQRLYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 382 YIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKraknfvsskgy 461
Cdd:cd14133  161 YIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGK----------- 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 462 pryctvttlsdgsvvlnggrsrrgklrgppesrewgnalkgCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14133  230 -----------------------------------------ADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
221-537 1.08e-130

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 386.29  E-value: 1.08e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd14226   14 RYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLKRHFMFRNHLCLV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKN--RIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQR 378
Cdd:cd14226   94 FELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKRSAIKIIDFGSSCQLGQR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSS 458
Cdd:cd14226  174 IYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVHMLDQAPKARKFFEK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 459 KGYPRYCTVTTLSDGSVVLNGGRSRRGKL---RGPPESREWGNALKGCDDPL-FLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd14226  254 LPDGTYYLKKTKDGKKYKPPGSRKLHEILgveTGGPGGRRAGEPGHTVEDYLkFKDLILRMLDYDPKTRITPAEALQHSF 333

                 ...
gi 153281169 535 LRR 537
Cdd:cd14226  334 FKR 336
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
222-535 1.60e-125

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: 372.74  E-value: 1.60e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQ-DKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNTKyDPEDKHHIVRLLDHFMHHGHLCIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVY 380
Cdd:cd14212   81 FELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFGSACFENYTLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNF--VSS 458
Cdd:cd14212  161 TYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPPDWMLEKGKNTNKFfkKVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 459 KGYPR------------------------YCTVTTLSDgsVVLNGGRsrrgKLRGPPESREWGNALKgcddpLFLDFLKQ 514
Cdd:cd14212  241 KSGGRstyrlktpeefeaenncklepgkrYFKYKTLED--IIMNYPM----KKSKKEQIDKEMETRL-----AFIDFLKG 309
                        330       340
                 ....*....|....*....|.
gi 153281169 515 CLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14212  310 LLEYDPKKRWTPDQALNHPFI 330
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
222-535 7.02e-112

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: 334.59  E-value: 7.02e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkDNTMNVIHMLENFTFR--NHICM 299
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLNDV--EGHPNIVKLLDVFEHRggNHLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFGSSCYEHQRV 379
Cdd:cd05118   79 VFELMGMNLYELIKDYP-RGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLE-LGQLKLADFGLARSFTSPP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YT-YIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMpsqklldaskraknfvs 457
Cdd:cd05118  157 YTpYVATRWYRAPEVLLGAKpYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGT----------------- 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 458 skgypryctvttlsdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd05118  220 ------------------------------------------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
221-535 6.25e-98

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: 301.79  E-value: 6.25e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd14134   13 RYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKDPNGKSHCVQLRDWFDYRGHMCIV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-------------KQQGR----SG 363
Cdd:cd14134   93 FELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynpkkKRQIRvpksTD 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 364 IKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLG-MPS 442
Cdd:cd14134  173 IKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLAMMERILGpLPK 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 443 QKLLDASKRAKNFVSSKGYPRYCTVTTLsdgsvvlngGRSRRgklRGPPESREWgNALKGCDDPLFLDFLKQCLEWDPAV 522
Cdd:cd14134  253 RMIRRAKKGAKYFYFYHGRLDWPEGSSS---------GRSIK---RVCKPLKRL-MLLVDPEHRLLFDLIRKMLEYDPSK 319
                        330
                 ....*....|...
gi 153281169 523 RMTPGQALRHPWL 535
Cdd:cd14134  320 RITAKEALKHPFF 332
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
222-535 6.94e-87

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 270.56  E-value: 6.94e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK--RFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKikKDRERILREIKILKKLKHP------NIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   300 TFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH-- 376
Cdd:smart00220  75 VMEYCEGgDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH--VKLADFGLARQLDpg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIellgmpsqklldaskraknfv 456
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI--------------------- 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169   457 sskgypryctvttlsdgsvvlnggrsRRGKLRGPPESREWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:smart00220 210 --------------------------GKPKPPFPPPEWDI--------SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
222-535 6.08e-77

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 247.36  E-value: 6.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNtMNVIHMLENFTFRNHICMTF 301
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADE-FNFVRAYECFQHKNHTCLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG--IKVIDFGSSCYEHQRV 379
Cdd:cd14211   80 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyrVKVIDFGSASHVSKAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 -YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSS 458
Cdd:cd14211  160 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEHLLNAATKTSRFFNR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 459 KGYPRYCTVTTLSDGSVVLNGGRSrrgklrgPPESREW-------------GNALKGC-------DDPLFLDFLKQCLEW 518
Cdd:cd14211  240 DPDSPYPLWRLKTPEEHEAETGIK-------SKEARKYifnclddmaqvngPSDLEGSellaekaDRREFIDLLKRMLTI 312
                        330
                 ....*....|....*..
gi 153281169 519 DPAVRMTPGQALRHPWL 535
Cdd:cd14211  313 DQERRITPGEALNHPFV 329
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
221-535 8.45e-77

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: 246.37  E-value: 8.45e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHK-VHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd14135    1 RYRVYGYLGKGVFSNVVRARDLArGNQEVAIKIIRNNELMHKAGLKELEILKKLNDADPDDKKHCIRLLRHFEHKNHLCL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKK-NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFGSSCYEHQR 378
Cdd:cd14135   81 VFESLSMNLREVLKKyGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEK-KNTLKLCDFGSASDIGEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYT-YIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLdasKRAK---- 453
Cdd:cd14135  160 EITpYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFPKKML---RKGQfkdq 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 ------NF-------VSSKGYpryctVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKgcddplflDFLKQCLEWDP 520
Cdd:cd14135  237 hfdenlNFiyrevdkVTKKEV-----RRVMSDIKPTKDLKTLLIGKQRLPDEDRKKLLQLK--------DLLDKCLMLDP 303
                        330
                 ....*....|....*
gi 153281169 521 AVRMTPGQALRHPWL 535
Cdd:cd14135  304 EKRITPNEALQHPFI 318
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
221-535 2.32e-75

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 242.87  E-value: 2.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKD--NTMNVIHMLENFTFR---- 294
Cdd:cd14136   11 RYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPKdpGREHVVQLLDDFKHTgpng 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILLKQQgRSGIKVIDFGSSC 373
Cdd:cd14136   91 THVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHtKCGIIHTDIKPENVLLCIS-KIEVKIADLGNAC 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLL---PGED---EGDQLACMIELLGMPSQKLLD 447
Cdd:cd14136  170 WTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALIIELLGRIPRSIIL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 448 ASKRAKNFVSskgypryctvttlsdgsvvlnggrsRRGKLRGPPESREWG--NAL--KGC----DDPLFLDFLKQCLEWD 519
Cdd:cd14136  250 SGKYSREFFN-------------------------RKGELRHISKLKPWPleDVLveKYKwskeEAKEFASFLLPMLEYD 304
                        330
                 ....*....|....*.
gi 153281169 520 PAVRMTPGQALRHPWL 535
Cdd:cd14136  305 PEKRATAAQCLQHPWL 320
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
217-533 2.40e-68

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: 223.53  E-value: 2.40e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 217 HVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRF-HRqaaeEIRILEHLRKQdkdntmNVIHMLENFTFR- 294
Cdd:cd14137    1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYkNR----ELQIMRRLKHP------NIVKLKYFFYSSg 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 ---NHIC--MTFELLSMNLYELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGI-KV 366
Cdd:cd14137   71 ekkDEVYlnLVMEYMPETLYRVIRHYSKNKQTIPiiYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV--DPETGVlKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 367 IDFGSSCY--EHQRVYTYIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQ 443
Cdd:cd14137  149 CDFGSAKRlvPGEPNVSYICSRYYRAPELIFGAtDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 444 KLLDASKRAK---NFVSSKGYPryctvttlsdgsvvlnggrsrrgklrgppesreWGNALKGCDDPLFLDFLKQCLEWDP 520
Cdd:cd14137  229 EQIKAMNPNYtefKFPQIKPHP---------------------------------WEKVFPKRTPPDAIDLLSKILVYNP 275
                        330
                 ....*....|...
gi 153281169 521 AVRMTPGQALRHP 533
Cdd:cd14137  276 SKRLTALEALAHP 288
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
222-535 4.39e-68

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: 222.36  E-value: 4.39e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR---FHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEeegIPSTALREISLLKELKHP------NIVKLLDVIHTENKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRSG-IKVIDFG-SSCYEH 376
Cdd:cd07829   75 LVFEYCDQDLKKYLDKRP-GPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLI---NRDGvLKLADFGlARAFGI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 Q-RVYTY-IQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLldaskrak 453
Cdd:cd07829  151 PlRTYTHeVVTLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEES-------- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgYPRyctVTTLSDGSVVLNggrsrrgklRGPPESreWGNALKGCdDPLFLDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd07829  223 -------WPG---VTKLPDYKPTFP---------KWPKND--LEKVLPRL-DPEGIDLLSKMLQYNPAKRISAKEALKHP 280

                 ..
gi 153281169 534 WL 535
Cdd:cd07829  281 YF 282
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
222-535 5.33e-66

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 218.74  E-value: 5.33e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNtMNVIHMLENFTFRNHICMTF 301
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADE-FNFVRAYECFQHRNHTCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG--IKVIDFGSSCYEHQRV 379
Cdd:cd14229   81 EMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPyrVKVIDFGSASHVSKTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 -YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSS 458
Cdd:cd14229  161 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKTSRFFCR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 459 KGYPRYCT--VTTLSDGSVVlNGGRSRrgklrgppESREW-------------GNALKGC-------DDPLFLDFLKQCL 516
Cdd:cd14229  241 ETDAPYSSwrLKTLEEHEAE-TGMKSK--------EARKYifnslddiahvnmVMDLEGSdllaekaDRREFVALLKKML 311
                        330
                 ....*....|....*....
gi 153281169 517 EWDPAVRMTPGQALRHPWL 535
Cdd:cd14229  312 LIDADLRITPADTLSHPFV 330
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
216-535 2.11e-65

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 217.03  E-value: 2.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQVVKAYDHKVH-QHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFR 294
Cdd:cd14213    8 DVLRARYEIVDTLGEGAFGKVVECIDHKMGgMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQMLEWFDHH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL-------------LKQQGR 361
Cdd:cd14213   88 GHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILfvqsdyvvkynpkMKRDER 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 362 ----SGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL 437
Cdd:cd14213  168 tlknPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 438 LGMPSQKLLDASKRAKNFVSSKgypryctvttlSDGSVVLNGGR--SRRGKlrgppESREWGNALKGCDDPLFlDFLKQC 515
Cdd:cd14213  248 LGPLPKHMIQKTRKRKYFHHDQ-----------LDWDEHSSAGRyvRRRCK-----PLKEFMLSQDVDHEQLF-DLIQKM 310
                        330       340
                 ....*....|....*....|
gi 153281169 516 LEWDPAVRMTPGQALRHPWL 535
Cdd:cd14213  311 LEYDPAKRITLDEALKHPFF 330
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
221-535 3.94e-64

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: 213.54  E-value: 3.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE-------KRFHRqaaeEIRILEHLRKqdkDNTMNVIHML----- 288
Cdd:cd07834    1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVfddlidaKRILR----EIKILRHLKH---ENIIGLLDILrppsp 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 289 ENFtfrNHICMTFELLSMNLYELIKKNKfqgfslPL----VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGI 364
Cdd:cd07834   74 EEF---NDVYIVTELMETDLHKVIKSPQ------PLtddhIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSN--CDL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 365 KVIDFG----SSCYEHQRVYT-YIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELL 438
Cdd:cd07834  143 KICDFGlargVDPDEDKGFLTeYVVTRWYRAPELLLSSkKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 439 GMPSQKLLD--ASKRAKNFVSSkgypryctvttlsdgsvvlnggrsrRGKLRGPPesreWGNALKGCDdPLFLDFLKQCL 516
Cdd:cd07834  223 GTPSEEDLKfiSSEKARNYLKS-------------------------LPKKPKKP----LSEVFPGAS-PEAIDLLEKML 272
                        330
                 ....*....|....*....
gi 153281169 517 EWDPAVRMTPGQALRHPWL 535
Cdd:cd07834  273 VFNPKKRITADEALAHPYL 291
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
216-535 4.51e-63

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 211.02  E-value: 4.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQVVKAYDH-KVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFR 294
Cdd:cd14214    9 DWLQERYEIVGDLGEGTFGKVVECLDHaRGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-----------------K 357
Cdd:cd14214   89 GHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlynesksceeK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 358 QQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL 437
Cdd:cd14214  169 SVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 438 LGMPSQKLLDASKRAKNFvsSKGYPRYCTVTtlSDGSVVL-NGGRSRRGKLRGPPESREwgnalkgcddpLFlDFLKQCL 516
Cdd:cd14214  249 LGPIPSHMIHRTRKQKYF--YKGSLVWDENS--SDGRYVSeNCKPLMSYMLGDSLEHTQ-----------LF-DLLRRML 312
                        330
                 ....*....|....*....
gi 153281169 517 EWDPAVRMTPGQALRHPWL 535
Cdd:cd14214  313 EFDPALRITLKEALLHPFF 331
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
222-535 7.80e-63

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: 208.54  E-value: 7.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRneKRFH--------RqaaeEIRILEHLRKQDkdntmNVIHMLENFTF 293
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMK--KKFYsweecmnlR----EVKSLRKLNEHP-----NIVKLKEVFRE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SS 372
Cdd:cd07830   70 NDELYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV--VKIADFGlAR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYT-YIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDask 450
Cdd:cd07830  148 EIRSRPPYTdYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWP--- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 451 RAKNFVSSKGY--PrYCTVTTLSDgsvVLnggrsrrgklrgPPESREwgnalkgcddplFLDFLKQCLEWDPAVRMTPGQ 528
Cdd:cd07830  225 EGYKLASKLGFrfP-QFAPTSLHQ---LI------------PNASPE------------AIDLIKDMLRWDPKKRPTASQ 276

                 ....*..
gi 153281169 529 ALRHPWL 535
Cdd:cd07830  277 ALQHPYF 283
Pkinase pfam00069
Protein kinase domain;
222-535 2.28e-62

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 206.31  E-value: 2.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR---FHRQAAEEIRILEHLRKqdkdntMNVIHMLENFTFRNHIC 298
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLNH------PNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  299 MTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH- 376
Cdd:pfam00069  75 LVLEYVEGgSLFDLLSEKG--AFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGN--LKITDFGLARQLNs 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  377 -QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIellgmpsqklldaskraknf 455
Cdd:pfam00069 151 gSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-------------------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  456 vsskgypryctvttlsdgsvvlnggrsrRGKLRGPPESREWGNALKgcddplflDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:pfam00069 211 ----------------------------DQPYAFPELPSNLSEEAK--------DLLKKLLKKDPSKRLTATEALQHPWF 254
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
222-535 1.16e-61

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 208.02  E-value: 1.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNtMNVIHMLENFTFRNHICMTF 301
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADD-YNFVRAYECFQHKNHTCLVF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG--IKVIDFGSSCYEHQRV 379
Cdd:cd14227   96 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPyrVKVIDFGSASHVSKAV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 -YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFV-- 456
Cdd:cd14227  176 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFnr 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 -SSKGYPRYCTVTtlSDGSVVLNGGRSRrgklrgppESREW-------------GNALKGCDDPL-------FLDFLKQC 515
Cdd:cd14227  256 dTDSPYPLWRLKT--PEDHEAETGIKSK--------EARKYifnclddmaqvnmTTDLEGSDMLVekadrreFIDLLKKM 325
                        330       340
                 ....*....|....*....|
gi 153281169 516 LEWDPAVRMTPGQALRHPWL 535
Cdd:cd14227  326 LTIDADKRITPIETLNHPFV 345
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
222-534 3.33e-59

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: 199.33  E-value: 3.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKR-FHRQAAEEIRILEHLRKQdkdntmNVIHMLE------NFT 292
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRmeNEKEgFPITAIREIKLLQKLDHP------NVVRLKEivtskgSAK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-- 370
Cdd:cd07840   75 YKGSIYMVFEYMDHDLTGLLDNPEVK-FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV--LKLADFGla 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 -SSCYEHQRVYTY-IQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKL-- 445
Cdd:cd07840  152 rPYTKENNADYTNrVITLWYRPPELLLGAtRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENwp 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 -LDASKRAKNFVSSKGYPRyctvttlsdgsvvlnggrsrrgKLRgppesrewgNALKGCDDPLFLDFLKQCLEWDPAVRM 524
Cdd:cd07840  232 gVSDLPWFENLKPKKPYKR----------------------RLR---------EVFKNVIDPSALDLLDKLLTLDPKKRI 280
                        330
                 ....*....|
gi 153281169 525 TPGQALRHPW 534
Cdd:cd07840  281 SADQALQHEY 290
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
222-535 1.02e-58

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 200.32  E-value: 1.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNtMNVIHMLENFTFRNHICMTF 301
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADE-YNFVRSYECFQHKNHTCLVF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG--IKVIDFGSSCYEHQRV 379
Cdd:cd14228   96 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyrVKVIDFGSASHVSKAV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 -YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSS 458
Cdd:cd14228  176 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTSRFFNR 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 459 K---GYPRYCTVTtlSDGSVVLNGGRSRrgklrgppESREW-------------GNALKG-------CDDPLFLDFLKQC 515
Cdd:cd14228  256 DpnlGYPLWRLKT--PEEHELETGIKSK--------EARKYifnclddmaqvnmSTDLEGtdmlaekADRREYIDLLKKM 325
                        330       340
                 ....*....|....*....|
gi 153281169 516 LEWDPAVRMTPGQALRHPWL 535
Cdd:cd14228  326 LTIDADKRITPLKTLNHPFV 345
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
216-535 2.72e-58

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 198.32  E-value: 2.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQVVKAYDHKVH-QHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFR 294
Cdd:cd14215    8 DWLQERYEIVSTLGEGTFGRVVQCIDHRRGgARVALKIIKNVEKYKEAARLEINVLEKINEKDPENKNLCVQMFDWFDYH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-------------KQQGR 361
Cdd:cd14215   88 GHMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekKRDER 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 362 S----GIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL 437
Cdd:cd14215  168 SvkstAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 438 LGMPSQKLLDASKRAKNFVSSkgypRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWgnalkgcddplFLDFLKQCLE 517
Cdd:cd14215  248 LGPIPSRMIRKTRKQKYFYHG----RLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQ-----------LFDLIESMLE 312
                        330
                 ....*....|....*...
gi 153281169 518 WDPAVRMTPGQALRHPWL 535
Cdd:cd14215  313 YEPSKRLTLAAALKHPFF 330
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
221-535 2.81e-58

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: 196.77  E-value: 2.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK---MVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd07833    2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkfkESEDDEDVKKTALREVKVLRQLRHE------NIVNLKEAFRRKGRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQ 377
Cdd:cd07833   76 YLVFEYVERTLLELLEASP-GGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGV--LKLCDFGFARALTA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 378 R---VYT-YIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLG-MPSQKLLDASKR 451
Cdd:cd07833  153 RpasPLTdYVATRWYRAPELLVGDtNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGpLPPSHQELFSSN 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 452 aknfvsskgyPRYCTVTTLSdgsvvlnggrsrrgklRGPPESREwgNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd07833  233 ----------PRFAGVAFPE----------------PSQPESLE--RRYPGKVSSPALDFLKACLRMDPKERLTCDELLQ 284

                 ....
gi 153281169 532 HPWL 535
Cdd:cd07833  285 HPYF 288
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
221-535 1.13e-56

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: 192.54  E-value: 1.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFH---RQAAEEIRILEHLrkqdKDNTmNVIHMLENFTFRNHI 297
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGgipNQALREIKALQAC----QGHP-YVVKLRDVFPHGTGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS---CY 374
Cdd:cd07832   76 VLVFEYMLSSLSEVLR-DEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGV--LKIADFGLArlfSE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTY-IQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLldaskra 452
Cdd:cd07832  153 EDPRLYSHqVATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKT------- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 knfvsskgYPRYctvTTLSDgsvvlnggrsrRGKLRGPPESRE-WGNALKGCdDPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd07832  226 --------WPEL---TSLPD-----------YNKITFPESKGIrLEEIFPDC-SPEAIDLLKGLLVYNPKKRLSAEEALR 282

                 ....
gi 153281169 532 HPWL 535
Cdd:cd07832  283 HPYF 286
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
221-535 6.43e-56

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 192.55  E-value: 6.43e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKD--NTMNVIHMLENFTFR---- 294
Cdd:cd14216   11 RYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSDPNdpNREMVVQLLDDFKISgvng 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILL----------------- 356
Cdd:cd14216   91 THICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHtKCRIIHTDIKPENILLsvneqyirrlaaeatew 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 357 -----------KQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLP- 423
Cdd:cd14216  171 qrnflvnplepKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGdYLFEPh 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 424 -GED---EGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYctVTTLSDGsvvlnggrsrrGKLRGPPESREWGNA 499
Cdd:cd14216  251 sGEDysrDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKH--ITKLKPW-----------GLFEVLVEKYEWSQE 317
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 153281169 500 lkgcDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14216  318 ----EAAGFTDFLLPMLELIPEKRATAAECLRHPWL 349
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
221-542 1.88e-55

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: 189.71  E-value: 1.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR------FHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkeakdgINFTALREIKLLQELKHP------NIIGLLDVFGHK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC- 373
Cdd:cd07841   75 SNINLVFEFMETDLEKVIK-DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV--LKLADFGLARs 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 -------YEHQrVYTyiqsRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQkl 445
Cdd:cd07841  152 fgspnrkMTHQ-VVT----RWYRAPELLFGARhYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTE-- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 ldaskraKNFVSSKGYPRYCTVTTLSdgsvvlnggrsrrgklrGPPESREWGNALKGCddplfLDFLKQCLEWDPAVRMT 525
Cdd:cd07841  225 -------ENWPGVTSLPDYVEFKPFP-----------------PTPLKQIFPAASDDA-----LDLLQRLLTLNPNKRIT 275
                        330
                 ....*....|....*..
gi 153281169 526 PGQALRHPWLRRRlPKP 542
Cdd:cd07841  276 ARQALEHPYFSND-PAP 291
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
221-536 7.69e-54

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: 186.73  E-value: 7.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR-------NEKRFHRqaaeEIRILEHLRKQdkdntmNVIHMLENFT- 292
Cdd:cd07851   16 RYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSrpfqsaiHAKRTYR----ELRLLKHMKHE------NVIGLLDVFTp 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 ------FRNhICMTFELLSMNLYELIKknkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKV 366
Cdd:cd07851   86 assledFQD-VYLVTHLMGADLNNIVK---CQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNED--CELKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 367 IDFGSSCYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKL 445
Cdd:cd07851  160 LDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEEL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 LD--ASKRAKNFVssKGYPryctVTTLSDGSVVLNGGrsrrgklrgppesrewgnalkgcdDPLFLDFLKQCLEWDPAVR 523
Cdd:cd07851  240 LKkiSSESARNYI--QSLP----QMPKKDFKEVFSGA------------------------NPLAIDLLEKMLVLDPDKR 289
                        330
                 ....*....|...
gi 153281169 524 MTPGQALRHPWLR 536
Cdd:cd07851  290 ITAAEALAHPYLA 302
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
216-537 2.59e-53

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 185.07  E-value: 2.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV----RNE---KRFHRqaaeEIRILEHLRKQDkdntmNVIHML 288
Cdd:cd07852    3 KHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafRNAtdaQRTFR----EIMFLQELNDHP-----NIIKLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 289 -----ENftfRNHICMTFELLSMNLYELIKKNKFQgfslPLVRKF-AHSILQCLDALHKNRIIHCDLKPENILLKQQGRs 362
Cdd:cd07852   74 nviraEN---DKDIYLVFEYMETDLHAVIRANILE----DIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCR- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 363 gIKVIDFG--------SSCYEHQRVYTYIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLAC 433
Cdd:cd07852  146 -VKLADFGlarslsqlEEDDENPVLTDYVATRWYRAPEILLGStRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEK 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 434 MIELLGMPSQKLLDA--SKRAKNFVSSKGYPRYCTVTTLsdgsvvlnggrsrrgKLRGPPESrewgnalkgcddplfLDF 511
Cdd:cd07852  225 IIEVIGRPSAEDIESiqSPFAATMLESLPPSRPKSLDEL---------------FPKASPDA---------------LDL 274
                        330       340
                 ....*....|....*....|....*.
gi 153281169 512 LKQCLEWDPAVRMTPGQALRHPWLRR 537
Cdd:cd07852  275 LKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
222-534 3.05e-53

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: 183.24  E-value: 3.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRneKRFHRQAA----EEIRILEHLRKQDkdntmNVIHMLENFTFRNHI 297
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMK--KHFKSLEQvnnlREIQALRRLSPHP-----NILRLIEVLFDRKTG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMT--FELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsgIKVIDFGSSCYE 375
Cdd:cd07831   74 RLAlvFELMDMNLYELIKGRK-RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI---LKLADFGSCRGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRV-YT-YIQSRFYRAPEVIL-GARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLdaSKRA 452
Cdd:cd07831  150 YSKPpYTeYISTRWYRAPECLLtDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVL--KKFR 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 KNFVSSKGYPryctvttlsdgsvvlnggrSRRGKlrgppesreWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRH 532
Cdd:cd07831  228 KSRHMNYNFP-------------------SKKGT---------GLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRH 279

                 ..
gi 153281169 533 PW 534
Cdd:cd07831  280 PY 281
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
222-535 3.79e-50

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: 175.16  E-value: 3.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRnekrfhRQAAEE------IRILEHLRKQDKDNTMNVIHMLENFTFRN 295
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVR------VPLSEEgiplstIREIALLKQLESFEHPNVVRLLDVCHGPR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 -----HICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd07838   75 tdrelKLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQ--VKLADFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SScyehqRVYTYiQSRF--------YRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPS 442
Cdd:cd07838  153 LA-----RIYSF-EMALtsvvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 443 QklldaskraknfvssKGYPRYCTVTTLSDGSvvlnggRSRRGKLRGPPESrewgnalkgcdDPLFLDFLKQCLEWDPAV 522
Cdd:cd07838  227 E---------------EEWPRNSALPRSSFPS------YTPRPFKSFVPEI-----------DEEGLDLLKKMLTFNPHK 274
                        330
                 ....*....|...
gi 153281169 523 RMTPGQALRHPWL 535
Cdd:cd07838  275 RISAFEALQHPYF 287
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
221-534 1.09e-49

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: 172.66  E-value: 1.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV-------RNEKRFHRqaaeEIRILEHLRKQdkdntmNVIHMLENFTF 293
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkkklksEDEEMLRR----EIEILKRLDHP------NIVKLYEVFED 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDFGS 371
Cdd:cd05117   71 DKNLYLVMELCTGgELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSpIKIIDFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SCYE------HQRVYT--YIqsrfyrAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEgdqlacmiellgmpsQ 443
Cdd:cd05117  149 AKIFeegeklKTVCGTpyYV------APEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETE---------------Q 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 444 KLLDASKRAK-NFvsskgypryctvttlsdgsvvlnggrsrrgklrgppESREWGNAlkgcdDPLFLDFLKQCLEWDPAV 522
Cdd:cd05117  208 ELFEKILKGKySF------------------------------------DSPEWKNV-----SEEAKDLIKRLLVVDPKK 246
                        330
                 ....*....|..
gi 153281169 523 RMTPGQALRHPW 534
Cdd:cd05117  247 RLTAAEALNHPW 258
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
218-538 7.48e-49

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: 173.32  E-value: 7.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-------MVRNEKRFHRqaaeEIRILEHLRKqdkDNTMNVIHML-- 288
Cdd:cd07855    3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKkipnafdVVTTAKRTLR----ELKILRHFKH---DNIIAIRDILrp 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 289 -ENFTFRNHICMTFELLSMNLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVI 367
Cdd:cd07855   76 kVPYADFKDVYVVLDLMESDLHHIIHSD--QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCE--LKIG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFG------SSCYEHQRVYT-YIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLG 439
Cdd:cd07855  152 DFGmarglcTSPEEHKYFMTeYVATRWYRAPELMLSlPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 440 MPSQKLLDA--SKRAKNFVSSKGypryctvttlsdgsvvlnggrsrrgklRGPPesREWgNALKGCDDPLFLDFLKQCLE 517
Cdd:cd07855  232 TPSQAVINAigADRVRRYIQNLP---------------------------NKQP--VPW-ETLYPKADQQALDLLSQMLR 281
                        330       340
                 ....*....|....*....|.
gi 153281169 518 WDPAVRMTPGQALRHPWLRRR 538
Cdd:cd07855  282 FDPSERITVAEALQHPFLAKY 302
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
222-535 2.58e-48

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: 170.16  E-value: 2.58e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFH---RQAAEEIRILEHLRKQDKDNTMNVIHMlenftfRNHIC 298
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEgvpSTAIREISLLKELNHPNIVRLLDVVHS------ENKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS------ 372
Cdd:cd07835   75 LVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA--LKLADFGLArafgvp 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 --CYEHQRVytyiqSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDAS 449
Cdd:cd07835  153 vrTYTHEVV-----TLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 KRAKNFVSSkgYPRYctvttlsdgsvvlnggrsrrgklrgppESREWGNALKGCdDPLFLDFLKQCLEWDPAVRMTPGQA 529
Cdd:cd07835  228 TSLPDYKPT--FPKW---------------------------ARQDLSKVVPSL-DEDGLDLLSQMLVYDPAKRISAKAA 277

                 ....*.
gi 153281169 530 LRHPWL 535
Cdd:cd07835  278 LQHPYF 283
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
221-535 8.95e-48

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 170.97  E-value: 8.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMN--VIHMLENFTFRN--- 295
Cdd:cd14218   11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSDPKRetIVQLIDDFKISGvng 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 -HICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILL----------------- 356
Cdd:cd14218   91 vHVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHtKCKIIHTDIKPENILMcvdegyvrrlaaeatiw 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 357 KQQGR---SG------------------------IKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLG 409
Cdd:cd14218  171 QQAGApppSGssvsfgasdflvnplepqnadkirVKIADLGNACWVHKHFTEDIQTRQYRALEVLIGAEYGTPADIWSTA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 410 CILAELLTG-YPLLP--GED---EGDQLACMIELLG-MPSqklldaskrakNFVSSKGYPRYCTvttlsdgsvvlnggrS 482
Cdd:cd14218  251 CMAFELATGdYLFEPhsGEDytrDEDHIAHIVELLGdIPP-----------HFALSGRYSREYF---------------N 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 483 RRGKLRGPPESREWG---NALKGCDDPL-----FLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14218  305 RRGELRHIKNLKHWGlyeVLVEKYEWPLeqaaqFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
228-415 1.88e-47

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: 165.52  E-value: 1.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPkeKLKKLLEELLREIEILKKLNHP------NIVKLYDVFETENFLYLVMEYCE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 -MNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY-----EHQRV 379
Cdd:cd00180   75 gGSLKDLLKENK-GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT--VKLADFGLAKDldsddSLLKT 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAEL 415
Cdd:cd00180  152 TGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
217-535 3.99e-47

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: 168.25  E-value: 3.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 217 HVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLE----- 289
Cdd:cd07849    2 DVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCLRTLREIKILLRFKHE------NIIGILDiqrpp 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 290 NFTFRNHICMTFELLSMNLYELIKKnkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDF 369
Cdd:cd07849   76 TFESFKDVYIVQELMETDLYKLIKT---QHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTN--CDLKICDF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 370 G-----SSCYEHQRVYT-YIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPS 442
Cdd:cd07849  151 GlariaDPEHDHTGFLTeYVATRWYRAPEIMLNSKgYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPS 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 443 QKLLDA--SKRAKNFVssKGYPRYCTVttlsdgsvvlnggrsrrgklrgpPESREWGNAlkgcdDPLFLDFLKQCLEWDP 520
Cdd:cd07849  231 QEDLNCiiSLKARNYI--KSLPFKPKV-----------------------PWNKLFPNA-----DPKALDLLDKMLTFNP 280
                        330
                 ....*....|....*
gi 153281169 521 AVRMTPGQALRHPWL 535
Cdd:cd07849  281 HKRITVEEALAHPYL 295
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
221-534 4.72e-45

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 161.44  E-value: 4.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV---RNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd07846    2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFlesEDDKMVKKIAMREIKMLKQLRHE------NLVNLIEVFRRKKRW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG--SSCYE 375
Cdd:cd07846   76 YLVFEFVDHTVLDDLEKYP-NGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGV--VKLCDFGfaRTLAA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYT-YIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAK 453
Cdd:cd07846  153 PGEVYTdYVATRWYRAPELLVGdTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQKNP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFVsskgypryctvttlsdgsvvlnGGRSRRGKLRGPPESR--EWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd07846  233 LFA----------------------GVRLPEVKEVEPLERRypKL--------SGVVIDLAKKCLHIDPDKRPSCSELLH 282

                 ...
gi 153281169 532 HPW 534
Cdd:cd07846  283 HEF 285
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
221-535 6.01e-45

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: 159.99  E-value: 6.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEAlerEIRILSSLKHP------NIVRYLGTERTENTL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS---- 372
Cdd:cd06606   75 NIFLEYVPGgSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV--VKLADFGCAkrla 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 --CYEHQRVyTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDQLACMiellgmpsqklldask 450
Cdd:cd06606  151 eiATGEGTK-SLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKP--PWSELGNPVAAL---------------- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 451 raknfvsskgyprYCTVTTLSdgsvvlnggrsrrgklrgPPESREWGnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQAL 530
Cdd:cd06606  212 -------------FKIGSSGE------------------PPPIPEHL-------SEEAKDFLRKCLQRDPKKRPTADELL 253

                 ....*
gi 153281169 531 RHPWL 535
Cdd:cd06606  254 QHPFL 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
221-534 6.06e-45

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


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 159.99  E-value: 6.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQA---AEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEekiKREIEIMKLLNHP------NIIKLYEVIETENKI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS--CY 374
Cdd:cd14003   75 YLVMEYASGgELFDYIVNNG--RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN--LKIIDFGLSneFR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGYplLPGEDEGDqlacmiellgmpsQKLLDASKRAK 453
Cdd:cd14003  151 GGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGY--LPFDDDND-------------SKLFRKILKGK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFvsskgYPRYctvttLSdgsvvlnggrsrrgklrgpPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14003  216 YP-----IPSH-----LS-------------------PDAR---------------DLIRRMLVVDPSKRITIEEILNHP 251

                 .
gi 153281169 534 W 534
Cdd:cd14003  252 W 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
221-535 2.98e-44

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: 160.65  E-value: 2.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQ--HVALKMVRN---EKRFHRQAAEEIRILEHLRKQDkdNTMNVIHM-LENFTFR 294
Cdd:cd07857    1 RYELIKELGQGAYGIVCSARNAETSEeeTVAIKKITNvfsKKILAKRALRELKLLRHFRGHK--NITCLYDMdIVFPGNF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC- 373
Cdd:cd07857   79 NELYLYEELMEADLHQIIRSG--QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCE--LKICDFGLARg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 -----YEHQRVYT-YIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLL 446
Cdd:cd07857  155 fsenpGENAGFMTeYVATRWYRAPEIMLSfQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEETL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 D--ASKRAKNFVSSKGYPRYCTVTTLSDGSvvlnggrsrrgklrgppesrewgnalkgcdDPLFLDFLKQCLEWDPAVRM 524
Cdd:cd07857  235 SriGSPKAQNYIRSLPNIPKKPFESIFPNA------------------------------NPLALDLLEKLLAFDPTKRI 284
                        330
                 ....*....|.
gi 153281169 525 TPGQALRHPWL 535
Cdd:cd07857  285 SVEEALEHPYL 295
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
222-535 3.22e-44

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: 158.14  E-value: 3.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQA-AEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMT 300
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESiLNEIAILKKC------KHPNIVKYYGSYLKKDELWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY---EH 376
Cdd:cd05122   76 MEFCSGgSLKDLLK-NTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE--VKLIDFGLSAQlsdGK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVyTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDegdqlacmiellgMPSQKLLDaskraknFV 456
Cdd:cd05122  153 TRN-TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKP--PYSE-------------LPPMKALF-------LI 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 457 SSKGYPryctvttlsdgsvvlnggrsrrgKLRGPPESrewgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd05122  210 ATNGPP-----------------------GLRNPKKW-----------SKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
211-534 4.21e-44

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: 159.46  E-value: 4.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 211 VQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKR-FHRQAAEEIRILEHLRKQdkdntmNVIHM 287
Cdd:cd07865    3 VEFPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLmeNEKEgFPITALREIKILQLLKHE------NVVNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 288 LE---------NfTFRNHICMTFELLSMNLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKq 358
Cdd:cd07865   77 IEicrtkatpyN-RYKGSIYLVFEFCEHDLAGLLS-NKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILIT- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 359 qgRSGI-KVIDFG------------SSCYEHqRVYTYiqsrFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPG 424
Cdd:cd07865  154 --KDGVlKLADFGlarafslaknsqPNRYTN-RVVTL----WYRPPELLLGERdYGPPIDMWGAGCIMAEMWTRSPIMQG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 425 EDEGDQLACMIELLGMPSQKLLDASKRaknfvsskgYPRYctvttlsdGSVVLNGGRSRRGKLRGPPESRewgnalkgcd 504
Cdd:cd07865  227 NTEQHQLTLISQLCGSITPEVWPGVDK---------LELF--------KKMELPQGQKRKVKERLKPYVK---------- 279
                        330       340       350
                 ....*....|....*....|....*....|
gi 153281169 505 DPLFLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd07865  280 DPYALDLIDKLLVLDPAKRIDADTALNHDF 309
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
222-579 1.44e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 160.29  E-value: 1.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVhqhVALKMVR----NEKRFHRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHI 297
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAkkleSKSKEVERFLREIQILASLNHPP-----NIVKLYDFFQDEGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLS-MNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSC-- 373
Cdd:COG0515   74 YLVMEYVDgGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV-VKLIDFGLAKll 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 -------YEHQRVYTYIQSRFYRAPEVILG---ARYGMPIDMWSLGCILAELLTGYPLLPGEDEG---DQLACMIELLGM 440
Cdd:COG0515  153 pdpgstsSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSsatSQTLKIILELPT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 441 PSQKlldaskraknfvsskgypryctvttlsdgsvvlnggrsrrgklrgppesREWGNALKGCDDPLFLDFLKQCLEWDP 520
Cdd:COG0515  233 PSLA-------------------------------------------------SPLSPSNPELISKAASDLLKKLLAKDP 263
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 521 AVRMTPGQALRHPWLRRR--------LPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTN 579
Cdd:COG0515  264 KNRLSSSSDLSHDLLAHLklkesdlsDLLKPDDSAPLRLSLPPSLEALISSLNSLAISGSDLKLDDS 330
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
221-534 1.96e-43

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 156.76  E-value: 1.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEK--RFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd07847    2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVESEDdpVIKKIALREIRMLKQLKHP------NLVNLIEVFRRKRKL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSScyehq 377
Cdd:cd07847   76 HLVFEYCDHTVLNELEKNP-RGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQ--IKLCDFGFA----- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 378 RV-------YT-YIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGmpsqkllDA 448
Cdd:cd07847  148 RIltgpgddYTdYVATRWYRAPELLVGdTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLG-------DL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 SKRAKNFVSSKGYPRYCTVTTlsdgsvvlnggrsrrgklrgpPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQ 528
Cdd:cd07847  221 IPRHQQIFSTNQFFKGLSIPE---------------------PETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEE 279

                 ....*.
gi 153281169 529 ALRHPW 534
Cdd:cd07847  280 LLEHPY 285
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
221-533 2.74e-43

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 156.69  E-value: 2.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNtmnVIHMLENFTFRNHICMT 300
Cdd:cd07848    2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQEN---IVELKEAFRRRGKLYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSS---CYEHQ 377
Cdd:cd07848   79 FEYVEKNMLELLEEMP-NGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHN--DVLKLCDFGFArnlSEGSN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 378 RVYT-YIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLG-MPSQKLldaskraKNF 455
Cdd:cd07848  156 ANYTeYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGpLPAEQM-------KLF 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 456 VSSkgyPRYctvttlsdgsvvlnggrsrrGKLRGP----PESREwgNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd07848  229 YSN---PRF--------------------HGLRFPavnhPQSLE--RRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLN 283

                 ..
gi 153281169 532 HP 533
Cdd:cd07848  284 HP 285
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
221-535 7.74e-43

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: 156.76  E-value: 7.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN-------EKRFHRqaaeEIRILEHLRKQD----KDnTMNVIHMlE 289
Cdd:cd07858    6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANafdnridAKRTLR----EIKLLRHLDHENviaiKD-IMPPPHR-E 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 290 NFtfrNHICMTFELLSMNLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIKVIDF 369
Cdd:cd07858   80 AF---NDVYIVYELMDTDLHQIIRSS--QTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL--NANCDLKICDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 370 G---SSCYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKL 445
Cdd:cd07858  153 GlarTTSEKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEED 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 LD--ASKRAKNFVssKGYPRYctvttlsdgsvvlnggrsrrgklRGPPESREWGNAlkgcdDPLFLDFLKQCLEWDPAVR 523
Cdd:cd07858  233 LGfiRNEKARRYI--RSLPYT-----------------------PRQSFARLFPHA-----NPLAIDLLEKMLVFDPSKR 282
                        330
                 ....*....|..
gi 153281169 524 MTPGQALRHPWL 535
Cdd:cd07858  283 ITVEEALAHPYL 294
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
221-535 1.06e-42

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 157.11  E-value: 1.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKD--NTMNVIHMLENFTFRN--- 295
Cdd:cd14217   13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEdpNKDMVVQLIDDFKISGmng 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 -HICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILL----------------- 356
Cdd:cd14217   93 iHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILMcvddayvrrmaaeatew 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 357 --------------------------KQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGC 410
Cdd:cd14217  173 qkagapppsgsavstapdllvnpldpRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTAC 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 411 ILAELLTG-YPLLP--GED---EGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYctVTTLSDGSV--VLnggrs 482
Cdd:cd14217  253 MAFELATGdYLFEPhsGEDysrDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGELRH--ITKLKPWSLfdVL----- 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 483 rrgklrgpPESREWGNAlkgcDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14217  326 --------VEKYGWPHE----DAAQFTDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
220-534 1.26e-42

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: 154.69  E-value: 1.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR---FHRQAAEEIRILEHLRKqdkDNTMNVIHMLENFTFrNH 296
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEkegFPITSLREINILLKLQH---PNIVTVKEVVVGSNL-DK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS--CY 374
Cdd:cd07843   81 IYMVMEYVEHDLKSLMETMK-QPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI--LKICDFGLAreYG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQ-SRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQK------LL 446
Cdd:cd07843  158 SPLKPYTQLVvTLWYRAPELLLGAkEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKiwpgfsEL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 DASKrAKNFVsskgYPRYCtvttlsdgsvvlnggrsrrgKLR---GPPESREWGnalkgcddplfLDFLKQCLEWDPAVR 523
Cdd:cd07843  238 PGAK-KKTFT----KYPYN--------------------QLRkkfPALSLSDNG-----------FDLLNRLLTYDPAKR 281
                        330
                 ....*....|.
gi 153281169 524 MTPGQALRHPW 534
Cdd:cd07843  282 ISAEDALKHPY 292
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
221-432 1.75e-42

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: 153.51  E-value: 1.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR----NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNH 296
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRpelaEDEEFRERFLREARALARLSHP------NIVRVYDVGEDDGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLS-MNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYE 375
Cdd:cd14014   75 PYIVMEYVEgGSLADLLRERG--PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR--VKLTDFGIARAL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 376 HQRVYTYIQSR----FYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLA 432
Cdd:cd14014  151 GDSGLTQTGSVlgtpAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLA 211
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
221-536 2.55e-42

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 155.32  E-value: 2.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEHLRKQDKDNTMNVIHMLENFTFRNhI 297
Cdd:cd07859    1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRilrEIKLLRLLRHPDIVEIKHIMLPPSRREFKD-I 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfqgfslPLVRK----FAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSc 373
Cdd:cd07859   80 YVVFELMESDLHQVIKAND------DLTPEhhqfFLYQLLRALKYIHTANVFHRDLKPKNILANADCK--LKICDFGLA- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 yehqRVYT-----------YIQSRFYRAPEVI--LGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGM 440
Cdd:cd07859  151 ----RVAFndtptaifwtdYVATRWYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 441 PSQKLLDA--SKRAKNFVSS--KGYPRyctvttlsdgsvvlnggrsrrgklrgpPESREWGNAlkgcdDPLFLDFLKQCL 516
Cdd:cd07859  227 PSPETISRvrNEKARRYLSSmrKKQPV---------------------------PFSQKFPNA-----DPLALRLLERLL 274
                        330       340
                 ....*....|....*....|
gi 153281169 517 EWDPAVRMTPGQALRHPWLR 536
Cdd:cd07859  275 AFDPKDRPTAEEALADPYFK 294
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
221-542 5.18e-42

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 154.53  E-value: 5.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVL-KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK---------------RFHRQAAEEIRILEHLRKQdkdntmNV 284
Cdd:PTZ00024   9 RYIQKgAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrqlvgmcGIHFTTLRELKIMNEIKHE------NI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 285 IHMLENFTFRNHICMTFELLSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgI 364
Cdd:PTZ00024  83 MGLVDVYVEGDFINLVMDIMASDLKKVVDRKIR--LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI--C 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 365 KVIDFG-SSCYEHQRVY------TYIQSR----------FYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:PTZ00024 159 KIADFGlARRYGYPPYSdtlskdETMQRReemtskvvtlWYRAPELLMGAeKYHFAVDMWSVGCIFAELLTGKPLFPGEN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 427 EGDQLACMIELLGMPSQklldaskraKNFVSSKGYPRYCTVTtlsdgsvvlnggrsrrgklrgPPESREWGNALKGCDDP 506
Cdd:PTZ00024 239 EIDQLGRIFELLGTPNE---------DNWPQAKKLPLYTEFT---------------------PRKPKDLKTIFPNASDD 288
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 153281169 507 LfLDFLKQCLEWDPAVRMTPGQALRHPWLRRRlPKP 542
Cdd:PTZ00024 289 A-IDLLQSLLKLNPLERISAKEALKHEYFKSD-PLP 322
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
222-535 8.19e-42

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: 152.57  E-value: 8.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRlesEEEGVPSTAIREISLLKELQHP------NIVCLEDVLMQENRLY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNL---YELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG--SSC 373
Cdd:cd07861   76 LVFEFLSMDLkkyLDSLPKGKY--MDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV--IKLADFGlaRAF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 YEHQRVYTY-IQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKR 451
Cdd:cd07861  152 GIPVRVYTHeVVTLWYRAPEVLLGSpRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTS 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 452 AKNFVSSkgYPRYctvttlsdgsvvlnggrsRRGKLRgppesrewgNALKGCDDPlFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd07861  232 LPDYKNT--FPKW------------------KKGSLR---------TAVKNLDED-GLDLLEKMLIYDPAKRISAKKALV 281

                 ....
gi 153281169 532 HPWL 535
Cdd:cd07861  282 HPYF 285
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
221-535 1.74e-41

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: 152.73  E-value: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN-------EKRFHRqaaeEIRILEHLRKQdkdntmNVIHMLENF-T 292
Cdd:cd07856   11 RYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKpfstpvlAKRTYR----ELKLLKHLRHE------NIISLSDIFiS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSMNLYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSS 372
Cdd:cd07856   81 PLEDIYFVTELLGTDLHRLLTSRPLEK---QFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNEN--CDLKICDFGLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLD--AS 449
Cdd:cd07856  156 RIQDPQMTGYVSTRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINtiCS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 KRAKNFVSSkgYPRyctvttlsdgsvvlnggRSRRgklrgpPESREWGNAlkgcdDPLFLDFLKQCLEWDPAVRMTPGQA 529
Cdd:cd07856  236 ENTLRFVQS--LPK-----------------RERV------PFSEKFKNA-----DPDAIDLLEKMLVFDPKKRISAAEA 285

                 ....*.
gi 153281169 530 LRHPWL 535
Cdd:cd07856  286 LAHPYL 291
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
218-535 2.94e-41

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 152.51  E-value: 2.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN--EKRFH-RQAAEEIRILEHLRKQdkdntmNVIHMLENFT-- 292
Cdd:cd07878   13 VPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSLIHaRRTYRELRLLKHMKHE------NVIGLLDVFTpa 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 -----FrNHICMTFELLSMNLYELIKknkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVI 367
Cdd:cd07878   87 tsienF-NEVYLVTNLMGADLNNIVK---CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE--LRIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFGSSCYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLL 446
Cdd:cd07878  161 DFGLARQADDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 D--ASKRAKNFVSSKGY-PRyctvttlSDGSVVLNGGrsrrgklrgppesrewgnalkgcdDPLFLDFLKQCLEWDPAVR 523
Cdd:cd07878  241 KkiSSEHARKYIQSLPHmPQ-------QDLKKIFRGA------------------------NPLAIDLLEKMLVLDSDKR 289
                        330
                 ....*....|..
gi 153281169 524 MTPGQALRHPWL 535
Cdd:cd07878  290 ISASEALAHPYF 301
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
222-534 3.16e-41

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 150.73  E-value: 3.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFH---RQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHIC 298
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvpSTAIREISLLKEL------NHPNIVKLLDVIHTENKLY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS------ 372
Cdd:cd07860   76 LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA--IKLADFGLArafgvp 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 --CYEHQRVytyiqSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDAS 449
Cdd:cd07860  154 vrTYTHEVV-----TLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 KRAKNFVSSkgYPRYctvtTLSDGSVVLnggrsrrgklrgPPESREWgnalkgcddplfLDFLKQCLEWDPAVRMTPGQA 529
Cdd:cd07860  229 TSMPDYKPS--FPKW----ARQDFSKVV------------PPLDEDG------------RDLLSQMLHYDPNKRISAKAA 278

                 ....*
gi 153281169 530 LRHPW 534
Cdd:cd07860  279 LAHPF 283
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
218-535 4.49e-41

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 152.12  E-value: 4.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR-------NEKRFHRqaaeEIRILEHLRKQdkdntmNVIHMLEN 290
Cdd:cd07877   15 VPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSrpfqsiiHAKRTYR----ELRLLKHMKHE------NVIGLLDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 FT-------FrNHICMTFELLSMNLYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsg 363
Cdd:cd07877   85 FTparsleeF-NDVYLVTHLMGADLNNIVKCQKLTD---DHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 364 IKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPS 442
Cdd:cd07877  159 LKILDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 443 QKLLD--ASKRAKNFVSSKGY-PRyctvttlsdgsvvlnggrsrrgklrgppesREWGNALKGCdDPLFLDFLKQCLEWD 519
Cdd:cd07877  239 AELLKkiSSESARNYIQSLTQmPK------------------------------MNFANVFIGA-NPLAVDLLEKMLVLD 287
                        330
                 ....*....|....*.
gi 153281169 520 PAVRMTPGQALRHPWL 535
Cdd:cd07877  288 SDKRITAAQALAHAYF 303
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
222-534 8.05e-41

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: 149.55  E-value: 8.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMlenftfRNHICM 299
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHldAEEGTPSTAIREISLMKELKHENIVRLHDVIHT------ENKLML 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQR 378
Cdd:cd07836   76 VFEYMDKDLKKYMDTHGVRGaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE--LKLADFGLARAFGIP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTY---IQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLdasKRAKN 454
Cdd:cd07836  154 VNTFsneVVTLWYRAPDVLLGSRtYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTW---PGISQ 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 FvsskgyPRYctvttlsdgsvvlnggrsrrgKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd07836  231 L------PEY---------------------KPTFPRYPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
222-543 1.35e-40

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: 149.82  E-value: 1.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR---FHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFR--NH 296
Cdd:cd07845    9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNErdgIPISSLREITLLLNLRHP------NIVELKEVVVGKhlDS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSCYE 375
Cdd:cd07845   83 IFLVMEYCEQDLASLLDNMP-TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC--LKIADFGlARTYG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 H-QRVYT-YIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKL---LDAS 449
Cdd:cd07845  160 LpAKPMTpKVVTLWYRAPELLLGCTtYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIwpgFSDL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 KRAKNFVSSKG-YpryctvttlsdgsvvlNGGRSRRGKLrgppesREWGNALkgcddplfLDFLkqcLEWDPAVRMTPGQ 528
Cdd:cd07845  240 PLVGKFTLPKQpY----------------NNLKHKFPWL------SEAGLRL--------LNFL---LMYDPKKRATAEE 286
                        330
                 ....*....|....*.
gi 153281169 529 ALRHPWLRRR-LPKPP 543
Cdd:cd07845  287 ALESSYFKEKpLPCEP 302
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
221-535 3.47e-40

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: 148.19  E-value: 3.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLEnfTFRN-- 295
Cdd:cd07863    1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtNEDGLPLSTVREVALLKRLEAFDHPNIVRLMDVCA--TSRTdr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 --HICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSc 373
Cdd:cd07863   79 etKVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQ--VKLADFGLA- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 yehqRVYTY-------IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKll 446
Cdd:cd07863  156 ----RIYSCqmaltpvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPED-- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 daskraknfvsskgypRYCTVTTLSDGSVvlnGGRSRRGKLRGPPESREWGnalkgcddplfLDFLKQCLEWDPAVRMTP 526
Cdd:cd07863  230 ----------------DWPRDVTLPRGAF---SPRGPRPVQSVVPEIEESG-----------AQLLLEMLTFNPHKRISA 279

                 ....*....
gi 153281169 527 GQALRHPWL 535
Cdd:cd07863  280 FRALQHPFF 288
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
221-420 5.99e-40

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: 146.24  E-value: 5.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV----RNEKRFH--RQaaeEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkrgKSEKELRnlRQ---EIEILRKLNHP------NIIEMLDSFETK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKfqgfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-- 370
Cdd:cd14002   73 KEFVVVTEYAQGELFQILEDDG----TLPeeEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGV--VKLCDFGfa 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 371 --SSCYEHqrVYTYIQ-SRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14002  147 raMSCNTL--VLTSIKgTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQP 197
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
218-535 1.19e-39

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 148.18  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFT-- 292
Cdd:cd07880   13 VPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYrpfQSELFAKRAYRELRLLKHMKHE------NVIGLLDVFTpd 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 -----FRN-HICMTFelLSMNLYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKV 366
Cdd:cd07880   87 lsldrFHDfYLVMPF--MGTDLGKLMKHEKL---SEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE--LKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 367 IDFGSSCYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKL 445
Cdd:cd07880  160 LDFGLARQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 LD--ASKRAKNFVssKGYPRYctvttlsdgsvvlnggrsrrgklrgppESREWGNALKGCdDPLFLDFLKQCLEWDPAVR 523
Cdd:cd07880  240 VQklQSEDAKNYV--KKLPRF---------------------------RKKDFRSLLPNA-NPLAVNVLEKMLVLDAESR 289
                        330
                 ....*....|..
gi 153281169 524 MTPGQALRHPWL 535
Cdd:cd07880  290 ITAAEALAHPYF 301
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
221-534 2.69e-39

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: 146.31  E-value: 2.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK--MVRNEKR-FHRQAAEEIRILEHLRKQdkdNTMNVIHML----ENFTF 293
Cdd:cd07866    9 DYEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEKDgFPITALREIKILKKLKHP---NVVPLIDMAverpDKSKR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 -RNHICMTFELLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-- 370
Cdd:cd07866   86 kRGSVYMVTPYMDHDLSGLLENPSVK-LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGI--LKIADFGla 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 -----------SSCYEHQRVYT-YIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL 437
Cdd:cd07866  163 rpydgpppnpkGGGGGGTRKYTnLVVTRWYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 438 LGMPSQklldaskraknfvsskgypryctvTTLSdGSVVLNGGRSRRGKLRGPPESRE-WGNALKGCddplfLDFLKQCL 516
Cdd:cd07866  243 CGTPTE------------------------ETWP-GWRSLPGCEGVHSFTNYPRTLEErFGKLGPEG-----LDLLSKLL 292
                        330
                 ....*....|....*...
gi 153281169 517 EWDPAVRMTPGQALRHPW 534
Cdd:cd07866  293 SLDPYKRLTASDALEHPY 310
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
199-541 9.71e-39

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 147.87  E-value: 9.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 199 NNGGYDDDQGSYVQVPHDHVAYR-YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQaaeEIRILEHLrkqd 277
Cdd:PTZ00036  44 NNAGEDEDEEKMIDNDINRSPNKsYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNR---ELLIMKNL---- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 278 kdNTMNVIHMLENF---TFRNH-----ICMTFELLSMNLYELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHC 347
Cdd:PTZ00036 117 --NHINIIFLKDYYyteCFKKNeknifLNVVMEFIPQTVHKYMKHYARNNHALPlfLVKLYSYQLCRALAYIHSKFICHR 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 348 DLKPENILLKQQGRSgIKVIDFGSS--CYEHQRVYTYIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPG 424
Cdd:PTZ00036 195 DLKPQNLLIDPNTHT-LKLCDFGSAknLLAGQRSVSYICSRFYRAPELMLGAtNYTTHIDLWSLGCIIAEMILGYPIFSG 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 425 EDEGDQLACMIELLGMPSQKLLDASKraknfvsskgyPRYCTVTTLSDGSVVLnggrsRRGKLRGPPESRewgnalkgcd 504
Cdd:PTZ00036 274 QSSVDQLVRIIQVLGTPTEDQLKEMN-----------PNYADIKFPDVKPKDL-----KKVFPKGTPDDA---------- 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 153281169 505 dplfLDFLKQCLEWDPAVRMTPGQALRHPW---LRR---RLPK 541
Cdd:PTZ00036 328 ----INFISQFLKYEPLKRLNPIEALADPFfddLRDpciKLPK 366
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
221-536 2.53e-38

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: 144.48  E-value: 2.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-------MVRNEKRFHRqaaeEIRILEHLrkqdkdNTMNVIHMLENFT- 292
Cdd:cd07850    1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKklsrpfqNVTHAKRAYR----ELVLMKLV------NHKNIIGLLNVFTp 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 ------FRnHICMTFELLSMNLYELIKknkfqgfsLPLVRK----FAHSILQCLDALHKNRIIHCDLKPENILLKQqgRS 362
Cdd:cd07850   71 qksleeFQ-DVYLVMELMDANLCQVIQ--------MDLDHErmsyLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS--DC 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 363 GIKVIDFG--SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGM 440
Cdd:cd07850  140 TLKILDFGlaRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGT 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 441 PSQKLLDA-SKRAKNFVSSKgyPRYC--TVTTLSDGSVVLNGGRSrRGKLRgPPESRewgnalkgcddplflDFLKQCLE 517
Cdd:cd07850  220 PSDEFMSRlQPTVRNYVENR--PKYAgySFEELFPDVLFPPDSEE-HNKLK-ASQAR---------------DLLSKMLV 280
                        330
                 ....*....|....*....
gi 153281169 518 WDPAVRMTPGQALRHPWLR 536
Cdd:cd07850  281 IDPEKRISVDDALQHPYIN 299
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
221-534 5.55e-38

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: 142.81  E-value: 5.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAY--DHKVHQHVALKMVRNEKR----FHRQAAEEIRILEHLRKQdkdntmNVIHMLEnfTFR 294
Cdd:cd07842    1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKEqytgISQSACREIALLRELKHE------NVVSLVE--VFL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NH----ICMTFELLSMNLYELIK---KNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL----KQQGRsg 363
Cdd:cd07842   73 EHadksVYLLFDYAEHDLWQIIKfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGV-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 364 IKVIDFG---------SSCYEHQRVYTYIqsrFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEG----- 428
Cdd:cd07842  151 VKIGDLGlarlfnaplKPLADLDPVVVTI---WYRAPELLLGARhYTKAIDIWAIGCIFAELLTLEPIFKGREAKikksn 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 429 ----DQLACMIELLGMPSQklldaskraKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREwgnalkgcd 504
Cdd:cd07842  228 pfqrDQLERIFEVLGTPTE---------KDWPDIKKMPEYDTLKSDTKASTYPNSLLAKWMHKHKKPDSQG--------- 289
                        330       340       350
                 ....*....|....*....|....*....|
gi 153281169 505 dplfLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd07842  290 ----FDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
221-533 2.04e-37

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 140.75  E-value: 2.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN--EKRFHRqaaeEIRILEHLRkqdkdNTMNVIHMLEnfTFRNH-- 296
Cdd:cd14132   19 DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPvkKKKIKR----EIKILQNLR-----GGPNIVKLLD--VVKDPqs 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 --ICMTFELL-SMNLYELIKKnkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSC 373
Cdd:cd14132   88 ktPSLIFEYVnNTDFKTLYPT-----LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRK-LRLIDWGLAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 YEH--QRVYTYIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTG-YPLLPGEDEGDQLACMIELLGMpsQKLLDas 449
Cdd:cd14132  162 FYHpgQEYNVRVASRYYKGPELLVDYQyYDYSLDMWSLGCMLASMIFRkEPFFHGHDNYDQLVKIAKVLGT--DDLYA-- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 kraknFVSSKGypryctvTTLSDGSVVLNGGRSRRGKLR-GPPESREWgnalkgcDDPLFLDFLKQCLEWDPAVRMTPGQ 528
Cdd:cd14132  238 -----YLDKYG-------IELPPRLNDILGRHSKKPWERfVNSENQHL-------VTPEALDLLDKLLRYDHQERITAKE 298

                 ....*
gi 153281169 529 ALRHP 533
Cdd:cd14132  299 AMQHP 303
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
222-535 1.96e-36

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 138.01  E-value: 1.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKR-FHRQAAEEIRILEHLrkqdkdNTMNVIHMLENFT------ 292
Cdd:cd07864    9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldNEKEgFPITAIREIKILRQL------NHRSVVNLKEIVTdkqdal 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 -FRNH---ICMTFELLSMNLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd07864   83 dFKKDkgaFYLVFEYMDHDLMGLLE-SGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ--IKLAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FG-SSCY--EHQRVYT-YIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQ 443
Cdd:cd07864  160 FGlARLYnsEESRPYTnKVITLWYRPPELLLGeERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 444 KLLDASKRAKNFVSSKgyPRyctvttlsdgsvvlnggRSRRGKLRgppESREWGNALKgcddplfLDFLKQCLEWDPAVR 523
Cdd:cd07864  240 AVWPDVIKLPYFNTMK--PK-----------------KQYRRRLR---EEFSFIPTPA-------LDLLDHMLTLDPSKR 290
                        330
                 ....*....|..
gi 153281169 524 MTPGQALRHPWL 535
Cdd:cd07864  291 CTAEQALNSPWL 302
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
221-534 1.97e-36

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 137.56  E-value: 1.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTfrnhi 297
Cdd:cd07839    1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRlddDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLT----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 cMTFELLSMNLyeliKK--NKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS-- 372
Cdd:cd07839   76 -LVFEYCDQDL----KKyfDSCNGdIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE--LKLADFGLAra 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 ------CYEHQRVytyiqSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLT-GYPLLPGEDEGDQLACMIELLGMPSQK 444
Cdd:cd07839  149 fgipvrCYSAEVV-----TLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPTEE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 445 LLDASKRAKNFvssKGYPRYCTVTTLSDGSVVLNGgrsrrgklrgppesrewgnalKGCddplflDFLKQCLEWDPAVRM 524
Cdd:cd07839  224 SWPGVSKLPDY---KPYPMYPATTSLVNVVPKLNS---------------------TGR------DLLQNLLVCNPVQRI 273
                        330
                 ....*....|
gi 153281169 525 TPGQALRHPW 534
Cdd:cd07839  274 SAEEALQHPY 283
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
221-535 2.92e-35

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 135.80  E-value: 2.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFT----F 293
Cdd:cd07879   16 RYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpfQSEIFAKRAYRELTLLKHMQHE------NVIGLLDVFTsavsG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHicMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:cd07879   90 DEF--QDFYLVMPYMQTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCE--LKILDFGLAR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPS----QKLLDa 448
Cdd:cd07879  166 HADAEMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGpefvQKLED- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 sKRAKNFVSS-KGYPRyctvttlSDGSVVLnggrsrrgklrgPPESrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPG 527
Cdd:cd07879  245 -KAAKSYIKSlPKYPR-------KDFSTLF------------PKAS------------PQAVDLLEKMLELDVDKRLTAT 292

                 ....*...
gi 153281169 528 QALRHPWL 535
Cdd:cd07879  293 EALEHPYF 300
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
222-536 3.42e-35

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: 132.98  E-value: 3.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRF----HRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQksglEHQLRREIEIQSHLRHP------NILRLYGYFEDKKRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY-E 375
Cdd:cd14007   76 YLILEYAPNgELYKELKKQK--RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE--LKLADFGWSVHaP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDQlacmiellgmpsqkllDASKRAKNf 455
Cdd:cd14007  152 SNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKP--PFESKSHQ----------------ETYKRIQN- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 456 vsskgypryctvttlsdgsvvlnggrsrrGKLRGPPESRewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14007  213 -----------------------------VDIKFPSSVS-----------PEAKDLISKLLQKDPSKRLSLEQVLNHPWI 252

                 .
gi 153281169 536 R 536
Cdd:cd14007  253 K 253
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
221-536 6.19e-35

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 133.79  E-value: 6.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR---FHRQAAEEIRILEHLRKQDKDNTMNVIHMlenftfRNHI 297
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEdegVPSTAIREISLLKEMQHGNIVRLQDVVHS------EKRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFGSS----- 372
Cdd:PLN00009  77 YLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRR-TNALKLADFGLArafgi 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 ---CYEHQRVytyiqSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDA 448
Cdd:PLN00009 156 pvrTFTHEVV-----TLWYRAPEILLGSRhYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 SKRAKNFVSSkgYPRYctvttlsdgsvvlnggrsrrgklrgppESREWGNALKGCdDPLFLDFLKQCLEWDPAVRMTPGQ 528
Cdd:PLN00009 231 VTSLPDYKSA--FPKW---------------------------PPKDLATVVPTL-EPAGVDLLSKMLRLDPSKRITARA 280

                 ....*...
gi 153281169 529 ALRHPWLR 536
Cdd:PLN00009 281 ALEHEYFK 288
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
228-428 9.37e-35

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: 131.87  E-value: 9.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEhtlnERNILERV------NHPFIVKLHYAFQTEEKLYLVLDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY---EHQRV 379
Cdd:cd05123   75 VPGgELFSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH--IKLTDFGLAKElssDGDRT 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEG 428
Cdd:cd05123  151 YTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRK 199
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
222-535 1.29e-34

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: 131.56  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECKHP------NIVDYYDSYLVGDELWVVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMN-LYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-----SScyE 375
Cdd:cd06614   76 EYMDGGsLTDIITQNPVR-MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS--VKLADFGfaaqlTK--E 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPgedegdqlacmieLLGMPSQklldaskRAKNF 455
Cdd:cd06614  151 KSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEP--P-------------YLEEPPL-------RALFL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 456 VSSKGYPRyctvttlsdgsvvlnggrsrrgklrgPPESREWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd06614  209 ITTKGIPP--------------------------LKNPEKW--------SPEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
221-444 4.14e-34

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: 131.31  E-value: 4.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVH-QHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTF-----R 294
Cdd:cd07862    2 QYECVAEIGEGAYGKVFKARDLKNGgRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVsrtdrE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSC 373
Cdd:cd07862   82 TKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ--IKLADFGlARI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 374 YEHQRVYT-YIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQK 444
Cdd:cd07862  160 YSFQMALTsVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEE 231
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
221-537 3.48e-33

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: 129.90  E-value: 3.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILehlRKQDKDNTMNVIHML----------- 288
Cdd:cd07854    6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKkIVLTDPQSVKHALREIKII---RRLDHDNIVKVYEVLgpsgsdltedv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 289 ENFTFRNHICMTFELLSMNLYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVID 368
Cdd:cd07854   83 GSLTELNSVYIVQEYMETDLANVLEQGPL---SEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLV-LKIGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FG-----SSCYEHQRVYTY-IQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMP 441
Cdd:cd07854  159 FGlarivDPHYSHKGYLSEgLVTKWYRSPRLLLSPNnYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 442 SQKLLDA--SKRAKNFVSSKGYPRyctvttlsdgsvvlnggRSRRGKLrgpPESrewgnalkgcdDPLFLDFLKQCLEWD 519
Cdd:cd07854  239 REEDRNEllNVIPSFVRNDGGEPR-----------------RPLRDLL---PGV-----------NPEALDFLEQILTFN 287
                        330
                 ....*....|....*...
gi 153281169 520 PAVRMTPGQALRHPWLRR 537
Cdd:cd07854  288 PMDRLTAEEALMHPYMSC 305
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
222-534 3.55e-33

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: 128.80  E-value: 3.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQDKD-NTMNVIHMLENFtfRNHI 297
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRlemEEEGVPSTALREVSLLQMLSQSIYIvRLLDVEHVEENG--KPLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfQGFSLPL----VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFGSS- 372
Cdd:cd07837   81 YLVFEYLDTDLKKFIDSYG-RGPHNPLpaktIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQ-KGLLKIADLGLGr 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 -------CYEHQrvytyIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQK 444
Cdd:cd07837  159 aftipikSYTHE-----IVTLWYRAPEVLLGStHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 445 LLDASKRAKNFvssKGYPRYctvttlsdgsvvlnggrsrrgklrgppESREWGNALKGCdDPLFLDFLKQCLEWDPAVRM 524
Cdd:cd07837  234 VWPGVSKLRDW---HEYPQW---------------------------KPQDLSRAVPDL-EPEGVDLLTKMLAYDPAKRI 282
                        330
                 ....*....|
gi 153281169 525 TPGQALRHPW 534
Cdd:cd07837  283 SAKAALQHPY 292
PTZ00284 PTZ00284
protein kinase; Provisional
221-541 3.87e-33

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 132.40  E-value: 3.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNT---MNVIHMLENFTfrNHI 297
Cdd:PTZ00284 130 RFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRfplMKIQRYFQNET--GHM 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfqgfslPLV-RKFAHSILQ---CLDALHKN-RIIHCDLKPENILLKQQGRS---------- 362
Cdd:PTZ00284 208 CIVMPKYGPCLLDWIMKHG------PFShRHLAQIIFQtgvALDYFHTElHLMHTDLKPENILMETSDTVvdpvtnralp 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 363 ----GIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELL 438
Cdd:PTZ00284 282 pdpcRVRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEKTL 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 439 G-MPSQ-KLLDASKRAKNFVSSKGYPRYCTvttlsDGSVVLNGGRSR--RGKLRgppesrewgnalkgcdDPLFLDFLKQ 514
Cdd:PTZ00284 362 GrLPSEwAGRCGTEEARLLYNSAGQLRPCT-----DPKHLARIARARpvREVIR----------------DDLLCDLIYG 420
                        330       340
                 ....*....|....*....|....*..
gi 153281169 515 CLEWDPAVRMTPGQALRHPWLRRRLPK 541
Cdd:PTZ00284 421 LLHYDRQKRLNARQMTTHPYVLKYYPE 447
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
223-536 6.74e-33

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: 126.94  E-value: 6.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAYDHKVHQHVALKM--VRNEKRFHRQAAEEIRILehlRKQDKDNTMNVIHMLenftFRN-HICM 299
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLRELKTL---RSCESPYVVKCYGAF----YKEgEISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSCYEH 376
Cdd:cd06623   77 VLEYMDGgSLADLLKKVG--KIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGE--VKIADFGiSKVLEN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRV--YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEdEGDQLACMIELLGMPsqklldaskrak 453
Cdd:cd06623  153 TLDqcNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGkFPFLPPG-QPSFFELMQAICDGP------------ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgypryctvttlsdgsvvlnggrsrrgklrgPPESREwgnalkGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd06623  220 ------------------------------------PPSLPA------EEFSPEFRDFISACLQKDPKKRPSAAELLQHP 257

                 ...
gi 153281169 534 WLR 536
Cdd:cd06623  258 FIK 260
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
228-418 5.57e-32

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: 123.80  E-value: 5.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKvhQHVALKMVRNEKRFHRQAAE---EIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELL 304
Cdd:cd13999    1 IGSGSFGEVYKGKWRG--TDVAIKKLKVEDDNDELLKEfrrEVSILSKLRHP------NIVQFIGACLSPPPLCIVTEYM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SM-NLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQ------ 377
Cdd:cd13999   73 PGgSLYDLLHKKKIP-LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT--VKIADFGLSRIKNSttekmt 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153281169 378 -RVYTYIqsrfYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd13999  150 gVVGTPR----WMAPEVLRGEPYTEKADVYSFGIVLWELLTG 187
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
221-417 1.56e-31

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: 122.96  E-value: 1.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK------MVRNEKRfhrQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFR 294
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeidlsnMSEKERE---EALNEVKLLSKL------KHPNIVKYYESFEEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMtfellSM------NLYELIKKNKFQGFSLP---LVRKFAHsILQCLDALHKNRIIHCDLKPENILLKQQGRsgIK 365
Cdd:cd08215   72 GKLCI-----VMeyadggDLAQKIKKQKKKGQPFPeeqILDWFVQ-ICLALKYLHSRKILHRDLKTQNIFLTKDGV--VK 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 366 VIDFGSScyehqRVY--------TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08215  144 LGDFGIS-----KVLesttdlakTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCT 198
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
228-536 2.68e-31

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 125.24  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEkrFH-----RQAAEEIRILEHLRKqdkDNTMNVIHMLE--NFTFRNHICMT 300
Cdd:cd07853    8 IGYGAFGVVWSVTDPRDGKRVALKKMPNV--FQnlvscKRVFRELKMLCFFKH---DNVLSALDILQppHIDPFEEIYVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG--------SS 372
Cdd:cd07853   83 TELMQSDLHKIIVSP--QPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCV--LKICDFGlarveepdES 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYTyiqsRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQK-LLDASK 450
Cdd:cd07853  159 KHMTQEVVT----QYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEaMRSACE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 451 RAKNFVsskgypryctvttlsdgsvvlnggrsrrgkLRGP--PESRewgNALKGCDDPL---FLDFLKQCLEWDPAVRMT 525
Cdd:cd07853  235 GARAHI------------------------------LRGPhkPPSL---PVLYTLSSQAtheAVHLLCRMLVFDPDKRIS 281
                        330
                 ....*....|.
gi 153281169 526 PGQALRHPWLR 536
Cdd:cd07853  282 AADALAHPYLD 292
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
222-535 1.14e-30

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: 121.33  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfHRQAA-----EEIRILEHLRKQDKDNTMNVIHMLENFTFrnh 296
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLE---HEEGApftaiREASLLKDLKHANIVTLHDIIHTKKTLTL--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 icmTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG------ 370
Cdd:cd07844   76 ---VFEYLDTDLKQYMDDCG-GGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGE--LKLADFGlaraks 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 --SSCYEHQRVytyiqSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPG-EDEGDQLACMIELLGMPSQKLL 446
Cdd:cd07844  150 vpSKTYSNEVV-----TLWYRPPDVLLGSTeYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRVLGTPTEETW 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 DASKRAKNFVSSKGypRYCTVTTLsdgsvvlnggRSRRGKLRGPPESrewgnalkgcddplfLDFLKQCLEWDPAVRMTP 526
Cdd:cd07844  225 PGVSSNPEFKPYSF--PFYPPRPL----------INHAPRLDRIPHG---------------EELALKFLQYEPKKRISA 277

                 ....*....
gi 153281169 527 GQALRHPWL 535
Cdd:cd07844  278 AEAMKHPYF 286
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
218-535 1.59e-30

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: 122.83  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHM------LENF 291
Cdd:cd07876   19 VLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVftpqksLEEF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 tfrNHICMTFELLSMNLYELIKKNkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG- 370
Cdd:cd07876   99 ---QDVYLVMELMDANLCQVIHME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD--CTLKILDFGl 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 --SSCYEHQrVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDA 448
Cdd:cd07876  170 arTACTNFM-MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFMNR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 -SKRAKNFVSSKgyPRYCTVTTLSDGSVVLNGGRSRRGKLRgPPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPG 527
Cdd:cd07876  249 lQPTVRNYVENR--PQYPGISFEELFPDWIFPSESERDKLK-TSQAR---------------DLLSKMLVIDPDKRISVD 310

                 ....*...
gi 153281169 528 QALRHPWL 535
Cdd:cd07876  311 EALRHPYI 318
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
221-535 1.64e-30

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: 120.02  E-value: 1.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSvmgEIDLLKKLNHP------NIVKYIGSVKTKDSL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY-- 374
Cdd:cd06627   75 YIILEYVENgSLASIIKK--FGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG--LVKLADFGVATKln 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 -EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDegdqlacmieLLGMPSQklldaskrak 453
Cdd:cd06627  151 eVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNP--PYYD----------LQPMAAL---------- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgyprYCTVTTlsdgsvvlnggrsrrgklRGPPesrewgnaLKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd06627  209 ----------FRIVQD------------------DHPP--------LPENISPELRDFLLQCFQKDPTLRPSAKELLKHP 252

                 ..
gi 153281169 534 WL 535
Cdd:cd06627  253 WL 254
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
222-535 2.30e-30

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: 120.50  E-value: 2.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfHRQAA-----EEIRILEHLRKQDKDNTMNVIHMLENFTfrnh 296
Cdd:cd07871    7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEGApctaiREVSLLKNLKHANIVTLHDIIHTERCLT---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 icMTFELLSMNLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 376
Cdd:cd07871   80 --LVFEYLDSDLKQYLD-NCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE--LKLADFGLARAKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTY---IQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRA 452
Cdd:cd07871  155 VPTKTYsneVVTLWYRPPDVLLGStEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 KNFvSSKGYPRYCTVTTLSDGSVVLNGGrsrrgklrgppesrewgnalkgcddplfLDFLKQCLEWDPAVRMTPGQALRH 532
Cdd:cd07871  235 EEF-RSYLFPQYRAQPLINHAPRLDTDG----------------------------IDLLSSLLLYETKSRISAEAALRH 285

                 ...
gi 153281169 533 PWL 535
Cdd:cd07871  286 SYF 288
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
218-535 4.05e-30

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: 121.73  E-value: 4.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEiRILEHLRKQDKDNTMNVIHMLENFT----- 292
Cdd:cd07874   15 VLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKL--SRPFQNQTHAK-RAYRELVLMKCVNHKNIISLLNVFTpqksl 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 --FRNhICMTFELLSMNLYELIKKNkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG 370
Cdd:cd07874   92 eeFQD-VYLVMELMDANLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD--CTLKILDFG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 --SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDA 448
Cdd:cd07874  165 laRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 -SKRAKNFVSSKgyPRYCTVTTLSDGSVVLNGGRSRRGKLRGpPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPG 527
Cdd:cd07874  245 lQPTVRNYVENR--PKYAGLTFPKLFPDSLFPADSEHNKLKA-SQAR---------------DLLSKMLVIDPAKRISVD 306

                 ....*...
gi 153281169 528 QALRHPWL 535
Cdd:cd07874  307 EALQHPYI 314
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
221-535 8.00e-30

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 118.47  E-value: 8.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKvHQHVALKMVRNEKRfHRQAAE----EIRILEHLRKQDkdntmNVIHML--ENFTFR 294
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGA-DEQTLQsyknEIELLKKLKGSD-----RIIQLYdyEVTDED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkQQGRsgIKVIDFGSScy 374
Cdd:cd14131   75 DYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGR--LKLIDFGIA-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 ehqrvyTYIQS------RF-------YRAPEVILGARY----------GMPIDMWSLGCILAELLTGYPllpgedegdql 431
Cdd:cd14131  150 ------KAIQNdttsivRDsqvgtlnYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKT----------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 432 acmiellgmPSQKLldaskraknfvsSKGYPRYCTVTtlsdgsvvlnggrsrrgklrGPPESREWGNalkgCDDPLFLDF 511
Cdd:cd14131  213 ---------PFQHI------------TNPIAKLQAII--------------------DPNHEIEFPD----IPNPDLIDV 247
                        330       340
                 ....*....|....*....|....
gi 153281169 512 LKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14131  248 MKRCLQRDPKKRPSIPELLNHPFL 271
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
221-418 1.15e-29

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: 117.49  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK--------RFHRqaaeEIRILEHLrkqdkdNTMNVIHMLENFT 292
Cdd:cd14073    2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiedeqdmvRIRR----EIEIMSSL------NHPHIIRIYEVFE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSM-NLYELIKKNKfqgfSLPL--VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd14073   72 NKDKIVIVMEYASGgELYDYISERR----RLPEreARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN--AKIADF 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 370 G-SSCYEHQRV-YTYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTG 418
Cdd:cd14073  146 GlSNLYSKDKLlQTFCGSPLYASPEIVNGTPYQGPeVDCWSLGVLLYTLVYG 197
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
222-427 1.42e-29

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: 118.09  E-value: 1.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRfhrqaaeeirileHLRKQDKDNTMN----VIHMLEN------- 290
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVL--DKR-------------HIIKEKKVKYVTiekeVLSRLAHpgivkly 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 FTFRNHICMTF--ELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVI 367
Cdd:cd05581   68 YTFQDESKLYFvlEYAPNgDLLEYIRKYGS--LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH--IKIT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFGSS--------------CYEHQRVYTYIQSR-F-----YRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDE 427
Cdd:cd05581  144 DFGTAkvlgpdsspestkgDADSQIAYNQARAAsFvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNE 223
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
228-420 3.52e-29

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: 116.55  E-value: 3.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVR-----NEKRFHRQAAEEiRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFE 302
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKkrdmiRKNQVDSVLAER-NILSQAQNP------FVVKLYYSFQGKKNLYLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-NLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRVYT 381
Cdd:cd05579   74 YLPGgDLYSLLEN--VGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGH--LKLTDFGLSKVGLVRRQI 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 382 YIQSRF------------------YRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05579  150 KLSIQKksngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIP 206
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
221-420 9.36e-29

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 114.96  E-value: 9.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE----KRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNH 296
Cdd:cd14099    2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltkPKQREKLKSEIKIHRSLKHP------NIVKFHDCFEDEEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLS-MNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC-- 373
Cdd:cd14099   76 VYILLELCSnGSLMELLKRRK--ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN--VKIGDFGLAArl 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 374 -YEHQRVYT------YIqsrfyrAPEVILGAR-YGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14099  152 eYDGERKKTlcgtpnYI------APEVLEKKKgHSFEVDIWSLGVILYTLLVGKP 200
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
228-457 1.37e-28

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: 114.63  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRnekrfhRQAAEEIRILEHLrKQDKDNTMNVIH-MLENF--TFRN--HICMTFE 302
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVK------KRHIVQTRQQEHI-FSEKEILEECNSpFIVKLyrTFKDkkYLYMLME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 L-LSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS--CYEHQRV 379
Cdd:cd05572   74 YcLGGELWTILRDRGL--FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGY--VKLVDFGFAkkLGSGRKT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllP-GEDEGDQLACM------IELLGMPSQklldASKRA 452
Cdd:cd05572  150 WTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRP--PfGGDDEDPMKIYniilkgIDKIEFPKY----IDKNA 223

                 ....*
gi 153281169 453 KNFVS 457
Cdd:cd05572  224 KNLIK 228
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
218-535 1.67e-28

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 117.07  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEiRILEHLRKQDKDNTMNVIHMLENFTFRNH- 296
Cdd:cd07875   22 VLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKL--SRPFQNQTHAK-RAYRELVLMKCVNHKNIIGLLNVFTPQKSl 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 -----ICMTFELLSMNLYELIKKNkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG- 370
Cdd:cd07875   99 eefqdVYIVMELMDANLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD--CTLKILDFGl 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 -SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDA- 448
Cdd:cd07875  173 aRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMKKl 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 SKRAKNFVSSKgyPRYCTVTTLSDGSVVLNGGRSRRGKLRGpPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPGQ 528
Cdd:cd07875  253 QPTVRTYVENR--PKYAGYSFEKLFPDVLFPADSEHNKLKA-SQAR---------------DLLSKMLVIDASKRISVDE 314

                 ....*..
gi 153281169 529 ALRHPWL 535
Cdd:cd07875  315 ALQHPYI 321
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
222-543 2.96e-28

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: 114.71  E-value: 2.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfHRQAA-----EEIRILEHLRKQDKDNTMNVIHMLENFTfrnh 296
Cdd:cd07873    4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLE---HEEGApctaiREVSLLKDLKHANIVTLHDIIHTEKSLT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 icMTFELLSMNLYELIKkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 376
Cdd:cd07873   77 --LVFEYLDKDLKQYLD-DCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLARAKS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTY---IQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRA 452
Cdd:cd07873  152 IPTKTYsneVVTLWYRPPDILLGStDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 KNFVSSKgYPRYCTVTTLSDGSVVLNGGrsrrgklrgppesrewgnalkgcddplfLDFLKQCLEWDPAVRMTPGQALRH 532
Cdd:cd07873  232 EEFKSYN-YPKYRADALHNHAPRLDSDG----------------------------ADLLSKLLQFEGRKRISAEEAMKH 282
                        330
                 ....*....|....
gi 153281169 533 PW---LRRRLPKPP 543
Cdd:cd07873  283 PYfhsLGERIHKLP 296
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
221-427 3.85e-28

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: 113.27  E-value: 3.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK----RFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNH 296
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQvareGMVEQIKREIAIMKLLRHP------NIVELHEVMATKTK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYE 375
Cdd:cd14663   75 IFFVMELVTGgELFSKIAKNG--RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN--LKISDFGLSALS 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 376 HQR-----VYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGYplLPGEDE 427
Cdd:cd14663  151 EQFrqdglLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGY--LPFDDE 206
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
221-538 9.33e-28

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: 113.29  E-value: 9.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK---RFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd14086    2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKlsaRDHQKLEREARICRLLKHP------NIVRLHDSISEEGFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-SGIKVIDFGSSCY- 374
Cdd:cd14086   76 YLVFDLVTGgELFEDIVAREF--YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgAAVKLADFGLAIEv 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 --EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEgDQlacmiellgmpsQKLLDASKRA 452
Cdd:cd14086  154 qgDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYP--PFWDE-DQ------------HRLYAQIKAG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 K-NFVSskgyPRYCTVTtlsdgsvvlnggrsrrgklrgpPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd14086  219 AyDYPS----PEWDTVT----------------------PEAK---------------DLINQMLTVNPAKRITAAEALK 257

                 ....*..
gi 153281169 532 HPWLRRR 538
Cdd:cd14086  258 HPWICQR 264
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
222-418 2.74e-27

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: 111.12  E-value: 2.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAY--DHKVHQHVALKMVRN--------EKRFHRqaaeEIRILEHLRKQdkdntmNVIHMLENF 291
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEytKSGLKEKVACKIIDKkkapkdflEKFLPR----ELEILRKLRHP------NIIQVYSIF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd14080   72 ERGSKVFIFMEYAEHgDLLEYIQKRGA--LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN--VKLSDFG 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 371 SS--CYEHQRVY---TYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG 418
Cdd:cd14080  148 FArlCPDDDGDVlskTFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCG 201
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
221-426 2.75e-27

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: 110.94  E-value: 2.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQ-AAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVnlGSLSQKEREdSVNEIRLLASVNHP------NIIRYKEAFLDGNRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSC 373
Cdd:cd08530   75 CIVMEYAPFgDLSKLISKRKKKRRLFPedDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL--VKIGDLGiSKV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:cd08530  153 LKKNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEART 205
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
221-423 2.77e-27

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: 111.01  E-value: 2.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfHRQAAEEIRILEHLRkqdkdNTMNVIHMLENFTFRNHICMT 300
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSK-HPQLEYEAKVYKLLQ-----GGPGIPRLYWFGQEGDYNVMV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDFG-SSCYEHQR 378
Cdd:cd14016   75 MDLLGPSLEDLFNKCGRK-FSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkVYLIDFGlAKKYRDPR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 379 VYTYIQsrfYRAPEVILG-ARYgMPI------------DMWSLGCILAELLTGYplLP 423
Cdd:cd14016  154 TGKHIP---YREGKSLTGtARY-ASInahlgieqsrrdDLESLGYVLIYFLKGS--LP 205
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
228-534 3.17e-27

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: 110.44  E-value: 3.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS-M 306
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHP------RIIQLHEAYESPTELVLILELCSgG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNkfqgFSL--PLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSScyehQRVYT--Y 382
Cdd:cd14006   75 ELLDRLAER----GSLseEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLA----RKLNPgeE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 383 IQSRF----YRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLpgeDEGDQlacmiELLGMPSQKLLDASKRAKNFVS 457
Cdd:cd14006  147 LKEIFgtpeFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGlSPFL---GEDDQ-----ETLANISACRVDFSEEYFSSVS 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 458 skgypryctvttlsdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd14006  219 ------------------------------------------------QEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
221-535 1.31e-26

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: 109.40  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFH----------RQAAEEIRILEHLRKQdkdntmNVIHMLEN 290
Cdd:cd14084    7 KYIMSRTLGSGACGEVKLAYDKSTCKKVAIKII-NKRKFTigsrreinkpRNIETEIEILKKLSHP------CIIKIEDF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 FTFRNHICMTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLK-QQGRSGIKVID 368
Cdd:cd14084   80 FDAEDDYYIVLELMEGgELFDRVVSNK--RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSsQEEECLIKITD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSCY--EHQRVYTYIQSRFYRAPEVIL---GARYGMPIDMWSLGCILAELLTGYPLLPGEdegdqlacmiellgmpsq 443
Cdd:cd14084  158 FGLSKIlgETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEE------------------ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 444 klldaskraknfvsskgypryCTVTTLSDGSVvlnggrsrRGKLR-GPPESREWGNALKgcddplflDFLKQCLEWDPAV 522
Cdd:cd14084  220 ---------------------YTQMSLKEQIL--------SGKYTfIPKAWKNVSEEAK--------DLVKKMLVVDPSR 262
                        330
                 ....*....|...
gi 153281169 523 RMTPGQALRHPWL 535
Cdd:cd14084  263 RPSIEEALEHPWL 275
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
221-534 1.41e-26

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: 109.10  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV---------RNEKRFHRqaaeEIRILEHLrkqdkdNTMNVIHMLENF 291
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIvkrkvagndKNLQLFQR----EINILKSL------EHPGIVRLIDWY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLSM-NLYELIKKNKfqgfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVID 368
Cdd:cd14098   71 EDDQHIYLVMEYVEGgDLMDFIMAWG----AIPeqHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSCYEHQRVY--TYIQSRFYRAPEVILGAR------YGMPIDMWSLGCILAELLTGYplLPGeDEGDQLACmIELLGm 440
Cdd:cd14098  147 FGLAKVIHTGTFlvTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGA--LPF-DGSSQLPV-EKRIR- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 441 psqklldaskraknfvssKGypRYCTVTTLSdgsvvlnggrsrrgkLRGPPESRewgnalkgcddplflDFLKQCLEWDP 520
Cdd:cd14098  222 ------------------KG--RYTQPPLVD---------------FNISEEAI---------------DFILRLLDVDP 251
                        330
                 ....*....|....
gi 153281169 521 AVRMTPGQALRHPW 534
Cdd:cd14098  252 EKRMTAAQALDHPW 265
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
221-535 1.66e-26

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: 108.93  E-value: 1.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFHRQAAEEIRILEHLRKQdkdntmNVI--HMLEnfTFRN 295
Cdd:cd06626    1 RWQRGNKIGEGTFGKVYTAVNLDTGELMAMKEIRfqdNDPKTIKEIADEMKVLEGLDHP------NLVryYGVE--VHRE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIKknkfQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:cd06626   73 EVYIFMEYCQEgTLEELLR----HGRILDeaVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL--IKLGDFGSA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CY--------EHQRVYTYIQSRFYRAPEVILGAR---YGMPIDMWSLGCILAELLTGYPllPGEDEGDQLACMIElLGMP 441
Cdd:cd06626  147 VKlknntttmAPGEVNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKR--PWSELDNEWAIMYH-VGMG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 442 SQKLLDASkrakNFVSSKGYpryctvttlsdgsvvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPA 521
Cdd:cd06626  224 HKPPIPDS----LQLSPEGK------------------------------------------------DFLSRCLESDPK 251
                        330
                 ....*....|....
gi 153281169 522 VRMTPGQALRHPWL 535
Cdd:cd06626  252 KRPTASELLDHPFI 265
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
226-420 3.16e-26

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: 107.83  E-value: 3.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkRFHRQAAEEIRILEhlrkqdkdntmNVIHMLENF------------TF 293
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEID-PINTEASKEVKALE-----------CEIQLLKNLqherivqyygclQD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSM-NLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSS 372
Cdd:cd06625   74 EKSLSIFMEYMPGgSVKDEIKA--YGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNG--NVKLGDFGAS 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 373 ------CyEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd06625  150 krlqtiC-SSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKP 202
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
222-464 3.34e-26

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 109.31  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfHRQAA-----EEIRILEHLRKQDKDNTMNVIHMLENFTfrnh 296
Cdd:cd07872    8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEGApctaiREVSLLKDLKHANIVTLHDIVHTDKSLT---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 icMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 376
Cdd:cd07872   81 --LVFEYLDKDLKQYMDDCG-NIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLARAKS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTY---IQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRA 452
Cdd:cd07872  156 VPTKTYsneVVTLWYRPPDVLLGSsEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISSN 235
                        250
                 ....*....|..
gi 153281169 453 KNFvSSKGYPRY 464
Cdd:cd07872  236 DEF-KNYNFPKY 246
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
221-412 4.79e-26

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: 107.81  E-value: 4.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNH--- 296
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKrMYFNDEEQLRVAIKEIEIMKRLCGHP-----NIVQYYDSAILSSEgrk 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 -ICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKN--RIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:cd13985   76 eVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNTGR--FKLCDFGSAT 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 374 YEH------QRVYTY---IQSR---FYRAPEVI---LGARYGMPIDMWSLGCIL 412
Cdd:cd13985  154 TEHypleraEEVNIIeeeIQKNttpMYRAPEMIdlySKKPIGEKADIWALGCLL 207
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
220-426 5.35e-26

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 107.35  E-value: 5.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVIGKGSFGQVVKAYDHKvHQHVALKMVRNEKRFHRQ----AAEEIRILEHLrkqdkdNTMNVIHMLENFTFRN 295
Cdd:cd14161    3 HRYEFLETLGKGTYGRVKKARDSS-GRLVAIKSIRKDRIKDEQdllhIRREIEIMSSL------NHPHIISVYEVFENSS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY 374
Cdd:cd14161   76 KIVIVMEYASRgDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANG--NIKIADFGLSNL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 375 EHQRVY--TYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTGYPLLPGED 426
Cdd:cd14161  152 YNQDKFlqTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHD 206
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
228-535 5.81e-26

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: 107.25  E-value: 5.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMV-----RNEKRFHRQAAE----------EIRILEHLRKQdkdntmNVIHMLE--N 290
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlRKRREGKNDRGKiknalddvrrEIAIMKKLDHP------NIVRLYEviD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 FTFRNHICMTFELLSMN-LYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd14008   75 DPESDKLYLVLEYCEGGpVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT--VKISDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 370 GSScyehqRVYT----YIQSR-----FYrAPEVILG--ARY-GMPIDMWSLGCILAELLTGypLLPgedegdqlacmiel 437
Cdd:cd14008  153 GVS-----EMFEdgndTLQKTagtpaFL-APELCDGdsKTYsGKAADIWALGVTLYCLVFG--RLP-------------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 438 lgmpsqklldaskraknFVSSKGYPRYCTVTTLSDgsvvlnggrsrrgklrGPPESREWGNALKgcddplflDFLKQCLE 517
Cdd:cd14008  211 -----------------FNGDNILELYEAIQNQND----------------EFPIPPELSPELK--------DLLRRMLE 249
                        330
                 ....*....|....*...
gi 153281169 518 WDPAVRMTPGQALRHPWL 535
Cdd:cd14008  250 KDPEKRITLKEIKEHPWV 267
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
222-427 6.03e-26

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 107.53  E-value: 6.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV----------RNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENF 291
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkEREKRLEKEISRDIRTIREAALSSLLNHPHICRLRDFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLS-MNLYELIkknkFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd14077   83 RTPNHYYMLFEYVDgGQLLDYI----ISHGKLKekQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN--IKIID 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 369 FG-SSCYEHQR-VYTYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTGYplLPGEDE 427
Cdd:cd14077  157 FGlSNLYDPRRlLRTFCGSLYFAAPELLQAQPYTGPeVDVWSFGVVLYVLVCGK--VPFDDE 216
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
221-537 6.76e-26

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: 107.33  E-value: 6.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKrfhrqaAE--------EIRILEHLRKQdkdntmNVIHMLENFT 292
Cdd:cd06609    2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE------AEdeiediqqEIQFLSQCDSP------YITKYYGSFL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSM-NLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG- 370
Cdd:cd06609   70 KGSKLWIIMEYCGGgSVLDLLKPGPLDETYIAFI---LREVLLGLEYLHSEGKIHRDIKAANILLSEEGD--VKLADFGv 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEHQ--RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPgedegdqlacmieLLGMPSQKLLda 448
Cdd:cd06609  145 SGQLTSTmsKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEP--P-------------LSDLHPMRVL-- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 449 skraknFVSSKGYPRyctvttlsdgsvvlnggrsrrgKLRGPPESREwgnalkgcddplFLDFLKQCLEWDPAVRMTPGQ 528
Cdd:cd06609  208 ------FLIPKNNPP----------------------SLEGNKFSKP------------FKDFVELCLNKDPKERPSAKE 247

                 ....*....
gi 153281169 529 ALRHPWLRR 537
Cdd:cd06609  248 LLKHKFIKK 256
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
221-418 7.81e-26

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 107.05  E-value: 7.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR-----------NEKRFHRQaaeEIRIleHLRKQDKDNtmnVIHMLE 289
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYksgpnskdgndFQKLPQLR---EIDL--HRRVSRHPN---IITLHD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 290 NFTFRNHICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFahsILQCLDAL---HKNRIIHCDLKPENILLKQQGRSgIK 365
Cdd:cd13993   73 VFETEVAIYIVLEYCPNgDLFEAITENRIYVGKTELIKNV---FLQLIDAVkhcHSLGIYHRDIKPENILLSQDEGT-VK 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 366 VIDFGSSCYEHQRVYTYIQSRFYRAPEVI-----LGARYG-MPIDMWSLGCILAELLTG 418
Cdd:cd13993  149 LCDFGLATTEKISMDFGVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFG 207
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
222-416 1.17e-25

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: 106.32  E-value: 1.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRF------HRQAAE---EIRILEHLRKQDKDNTMNVIHMLENFT 292
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILvdtwvrDRKLGTvplEIHILDTLNKRSHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRnHICMTFELLSMNLYELIKKNKfqgfslPLVRKFAHSIL-QCLDA---LHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd14004   82 FY-YLVMEKHGSGMDLFDFIERKP------NMDEKEAKYIFrQVADAvkhLHDQGIVHRDIKDENVILDGNGT--IKLID 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSCY-EHQRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELL 416
Cdd:cd14004  153 FGSAAYiKSGPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLV 202
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
225-547 1.45e-25

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: 106.74  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALK--MVRNEKRFHRQAaeeIRILEHLRKQDKDNTMNVIHM-LENFTFRNHICMTF 301
Cdd:cd06621    6 LSSLGEGAGGSVTKCRLRNTKTIFALKtiTTDPNPDVQKQI---LRELEINKSCASPYIVKYYGAfLDEQDSSIGIAMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 -ELLSMN-LYELIKKNKFQGFSLPLVrKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRV 379
Cdd:cd06621   83 cEGGSLDsIYKKVKKKGGRIGEKVLG-KIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ--VKLCDFGVSGELVNSL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 Y-TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPgedEGDQLACMIELLG----MPSQKLLDAskrak 453
Cdd:cd06621  160 AgTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNrFPFPP---EGEPPLGPIELLSyivnMPNPELKDE----- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgypryctvttlsdgsvvlnggrsrrgklrgPPESREWGNALKgcddplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd06621  232 ------------------------------------PENGIKWSESFK--------DFIEKCLEKDGTRRPGPWQMLAHP 267
                        330
                 ....*....|....
gi 153281169 534 WLRRRLPKPPTGEK 547
Cdd:cd06621  268 WIKAQEKKKVNMAK 281
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
228-420 2.90e-25

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: 105.00  E-value: 2.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMV---RNEKRFHRQAAEEIRILehlRKQDKDNTMNVIHMLENftfRNHICMTFELL 304
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkKLNKKLQENLESEIAIL---KSIKHPNIVRLYDVQKT---EDFIYLVLEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDFGSSCYEHQRVY-- 380
Cdd:cd14009   75 AGgDLSQYIRKRG--RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPvLKIADFGFARSLQPASMae 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14009  153 TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKP 192
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
222-535 4.01e-25

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: 105.43  E-value: 4.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFrnhicm 299
Cdd:cd07870    2 YLNLEKLGEGSYATVYKGISRINGQLVALKVIsmKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTF------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---SSCYEH 376
Cdd:cd07870   76 VFEYMHTDLAQYMIQHP-GGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE--LKLADFGlarAKSIPS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPG-EDEGDQLACMIELLGMPSQKLLDASKRAKN 454
Cdd:cd07870  153 QTYSSEVVTLWYRPPDVLLGAtDYSSALDIWGAGCIFIEMLQGQPAFPGvSDVFEQLEKIWTVLGVPTEDTWPGVSKLPN 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 FvsskgYPRYCTVTTLSDGSVVLNggrsrrgKLRGPPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd07870  233 Y-----KPEWFLPCKPQQLRVVWK-------RLSRPPKAE---------------DLASQMLMMFPKDRISAQDALLHPY 285

                 .
gi 153281169 535 L 535
Cdd:cd07870  286 F 286
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
222-533 5.31e-25

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: 104.75  E-value: 5.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfhrQAAeeiriLEHLRKQDKdnTM------NVIHMLENFTFRN 295
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKC---QTS-----MDELRKEIQ--AMsqcnhpNVVSYYTSFVVGD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIK-KNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSS- 372
Cdd:cd06610   73 ELWLVMPLLSGgSLLDIMKsSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDG--SVKIADFGVSa 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 ------CYEHQRVYTYIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPllPGEDegdqlacmiellgMPSQKl 445
Cdd:cd06610  151 slatggDRTRKVRKTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAA--PYSK-------------YPPMK- 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 ldaskraknfvsskgypryctvttlsdgsVVLNggrsrrgKLRGPPESREWGNALKGCDDpLFLDFLKQCLEWDPAVRMT 525
Cdd:cd06610  215 -----------------------------VLML-------TLQNDPPSLETGADYKKYSK-SFRKMISLCLQKDPSKRPT 257

                 ....*...
gi 153281169 526 PGQALRHP 533
Cdd:cd06610  258 AEELLKHK 265
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
222-535 1.28e-24

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: 103.10  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK----RFHRQAAEEI---RILEHlrkqdkDNTMNVIHMLENftfR 294
Cdd:cd14081    3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKlskeSVLMKVEREIaimKLIEH------PNVLKLYDVYEN---K 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSM-NLYE-LIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-- 370
Cdd:cd14081   74 KYLYLVLEYVSGgELFDyLVKKGRL---TEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN--IKIADFGma 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEHQRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGYplLPGEDEGDqlacmiellgmpsQKLLDAS 449
Cdd:cd14081  149 SLQPEGSLLETSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGA--LPFDDDNL-------------RQLLEKV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 KRAKnFVsskgYPRYCtvttlsdgsvvlnggrsrrgklrgPPESRewgnalkgcddplflDFLKQCLEWDPAVRMTPGQA 529
Cdd:cd14081  214 KRGV-FH----IPHFI------------------------SPDAQ---------------DLLRRMLEVNPEKRITIEEI 249

                 ....*.
gi 153281169 530 LRHPWL 535
Cdd:cd14081  250 KKHPWF 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
222-427 1.55e-24

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 103.15  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNekrfhRQAAE---------EIRILEHLRKQdkdntmNVIHMLENF- 291
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSK-----KKAPEdylqkflprEIEVIKGLKHP------NLICFYEAIe 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 -TFRNHICMTfelLSMN--LYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd14162   71 tTSRVYIIME---LAENgdLLDYIRKNGA--LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN--LKITD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 369 FGSSCYEHQRV-------YTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGYplLPGEDE 427
Cdd:cd14162  144 FGFARGVMKTKdgkpklsETYCGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGR--LPFDDS 208
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
222-535 1.63e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 102.69  E-value: 1.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVH-------QHVALKMVRNEKRFHRQAAEeIRILEHLRKQDkdntmNVIHMLENFTFR 294
Cdd:cd14019    3 YRIIEKIGEGTFSSVYKAEDKLHDlydrnkgRLVALKHIYPTSSPSRILNE-LECLERLGGSN-----NVSGLITAFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELlsmnlyelIKKNKFQGF----SLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIkVIDFG 370
Cdd:cd14019   77 DQVVAVLPY--------IEHDDFRDFyrkmSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGV-LVDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEHQ-------RVYTyiqsRFYRAPEVILgaRY---GMPIDMWSLGCILAELLTG-YPLLPGEDEGDQLAcmiELlg 439
Cdd:cd14019  148 LAQREEDrpeqrapRAGT----RGFRAPEVLF--KCphqTTAIDIWSAGVILLSILSGrFPFFFSSDDIDALA---EI-- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 440 mpsqklldaskraknfvsskgypryctvttlsdgsvvlnggrsrrGKLRGppesrewgnalkgcdDPLFLDFLKQCLEWD 519
Cdd:cd14019  217 ---------------------------------------------ATIFG---------------SDEAYDLLDKLLELD 236
                        330
                 ....*....|....*.
gi 153281169 520 PAVRMTPGQALRHPWL 535
Cdd:cd14019  237 PSKRITAEEALKHPFF 252
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
221-535 3.93e-24

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 101.84  E-value: 3.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd14087    2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMI-ETKCRGREVCEsELNVLRRVRHT------NIIQLIEVFETKERVYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNlyELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQG-RSGIKVIDFGSSCY--- 374
Cdd:cd14087   75 VMELATGG--ELFDRIIAKGsFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGpDSKIMITDFGLASTrkk 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 -EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGypLLPGEDEGdqlacmiellgmpSQKLLDASKRAK 453
Cdd:cd14087  153 gPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSG--TMPFDDDN-------------RTRLYRQILRAK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFVSSKGYPryctvttlsdgsvvlngGRSRRGKlrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14087  218 YSYSGEPWP-----------------SVSNLAK-----------------------DFIDRLLTVNPGERLSATQALKHP 257

                 ..
gi 153281169 534 WL 535
Cdd:cd14087  258 WI 259
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
222-420 4.06e-24

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: 102.66  E-value: 4.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAyDHKVHQH-VALKMVRNEKRFHRQAAE----EIRILEHLRK----------QDKDNtmnvIH 286
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLV-KHKDSGKyYALKILKKAKIIKLKQVEhvlnEKRILSEVRHpfivnllgsfQDDRN----LY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 287 MLENFtfrnhiCMTFELLSMnlyeLIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKV 366
Cdd:cd05580   78 MVMEY------VPGGELFSL----LRRSGRF---PNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH--IKI 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 367 IDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05580  143 TDFGFAKRVKDRTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYP 196
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
222-538 4.17e-24

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: 102.71  E-value: 4.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFgQVVKAYDHKV-HQHVALKMVRNEKRfhrQAAEEIRILehLRKQdkdNTMNVIHMLENFTFRNHICMT 300
Cdd:cd14091    2 YEIKEEIGKGSY-SVCKRCIHKAtGKEYAVKIIDKSKR---DPSEEIEIL--LRYG---QHPNIITLRDVYDDGNSVYLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLS-MNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR--SGIKVIDFG------- 370
Cdd:cd14091   73 TELLRgGELLDRILRQKF--FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpESLRICDFGfakqlra 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ------SSCYEHQRVytyiqsrfyrAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLPGEDEGdqlacmiellgmPSQ 443
Cdd:cd14091  151 engllmTPCYTANFV----------APEVLKKQGYDAACDIWSLGVLLYTMLAGYtPFASGPNDT------------PEV 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 444 KLldasKRaknfvsskgypryctvttLSDGSVVLNGGRsrrgklrgppesreWGNAlkgcdDPLFLDFLKQCLEWDPAVR 523
Cdd:cd14091  209 IL----AR------------------IGSGKIDLSGGN--------------WDHV-----SDSAKDLVRKMLHVDPSQR 247
                        330
                 ....*....|....*
gi 153281169 524 MTPGQALRHPWLRRR 538
Cdd:cd14091  248 PTAAQVLQHPWIRNR 262
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
221-534 4.23e-24

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: 101.68  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA--EEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd14083    4 KYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSleNEIAVLRKIKHP------NIVQLLDIYESKSHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNlyELIKKNKFQGFSLPlvRKFAHSILQCLDA---LHKNRIIHCDLKPENIL-LKQQGRSGIKVIDFGSSCY 374
Cdd:cd14083   78 LVMELVTGG--ELFDRIVEKGSYTE--KDASHLIRQVLEAvdyLHSLGIVHRDLKPENLLyYSPDEDSKIMISDFGLSKM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVY-TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDqlacmiellgmpsQKLLDASKRAK 453
Cdd:cd14083  154 EDSGVMsTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYP--PFYDEND-------------SKLFAQILKAE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 -NFVSskgyPRYctvTTLSDGSVvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRH 532
Cdd:cd14083  219 yEFDS----PYW---DDISDSAK----------------------------------DFIRHLMEKDPNKRYTCEQALEH 257

                 ..
gi 153281169 533 PW 534
Cdd:cd14083  258 PW 259
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
223-537 9.90e-24

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: 100.88  E-value: 9.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAYdHKVHQHV-ALKMVRNEKrfhrQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd06605    4 EYLGELGEGNGGVVSKVR-HRPSGQImAVKVIRLEI----DEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKnKFQGFSLPLVRKFAHSILQCLDALHKNR-IIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRV- 379
Cdd:cd06605   79 EYMDGGSLDKILK-EVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQ--VKLCDFGVSGQLVDSLa 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEDEG-----DQLACMIEllgMPSQKLldaskrak 453
Cdd:cd06605  156 KTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrFPYPPPNAKPsmmifELLSYIVD---EPPPLL-------- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgypryctvttlsdgsvvlnggrsrrgklrgppESREWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd06605  225 --------------------------------------PSGKF--------SPDFQDFVSQCLQKDPTERPSYKELMEHP 258

                 ....
gi 153281169 534 WLRR 537
Cdd:cd06605  259 FIKR 262
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
222-427 1.45e-23

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: 100.04  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd14079    4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEkirrEIQILKLFRHP------HIIRLYEVIETPTDI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMN-LYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgRSGIKVIDFGSSCYEH 376
Cdd:cd14079   78 FMVMEYVSGGeLFDYIVQKG--RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDS--NMNVKIADFGLSNIMR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 377 QRVY--TYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTGYplLPGEDE 427
Cdd:cd14079  154 DGEFlkTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGS--LPFDDE 205
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
222-420 2.35e-23

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: 101.59  E-value: 2.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALK-------MVRNEKRFHRqaaEEIRILEHLrkqdkdNTMNVIHMLENFTFR 294
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKilrksdmLKREQIAHVR---AERDILADA------DSPWIVRLHYAFQDE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLS----MNLyeLIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd05573   74 DHLYLVMEYMPggdlMNL--LIKYDVFPE---ETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGH--IKLADFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSC---YEHQRVYTYIQSRF-----------------------------YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05573  147 LCTkmnKSGDRESYLNDSVNtlfqdnvlarrrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEMLYG 226

                 ..
gi 153281169 419 YP 420
Cdd:cd05573  227 FP 228
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
222-535 2.39e-23

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: 100.45  E-value: 2.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEnEIAVLKRIKHE------NIVTLEDIYESTTHYYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNlyELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL-LKQQGRSGIKVIDFG-SSCYEHQ 377
Cdd:cd14166   79 MQLVSGG--ELFDRILERGvYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKIMITDFGlSKMEQNG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 378 RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEgdqlacmiellgmpsQKLLDASKraknfvs 457
Cdd:cd14166  157 IMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETE---------------SRLFEKIK------- 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 458 sKGYPRYctvttlsdgsvvlnggrsrrgklrgppESREWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14166  215 -EGYYEF---------------------------ESPFWDDISESAK-----DFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
226-534 3.02e-23

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 99.28  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfhRQAAEEIRIleHLRKQDKDNTMNVIHMLENfTFRNHICMtfeLLS 305
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALKVLRDN----PKARREVEL--HWRASGCPHIVRIIDVYEN-TYQGRKCL---LVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 M------NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGI-KVIDFGSSCYEHQR 378
Cdd:cd14089   77 MecmeggELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAIlKLTDFGFAKETTTK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 V------YTyiqsRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPgedegdqlacmiellgmpsqklldaskra 452
Cdd:cd14089  157 KslqtpcYT----PYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYP--P----------------------------- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 knFVSSKGYPryctvttLSDGSvvlnGGRSRRGKLRGPPEsrEWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRH 532
Cdd:cd14089  202 --FYSNHGLA-------ISPGM----KKRIRNGQYEFPNP--EWSNVSEEAK-----DLIRGLLKTDPSERLTIEEVMNH 261

                 ..
gi 153281169 533 PW 534
Cdd:cd14089  262 PW 263
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
220-535 3.17e-23

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 100.53  E-value: 3.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKViGKGSFGQVVKAY--DHKVHQHVALKMVRNEKrFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRN-- 295
Cdd:cd07867    3 FEYEGCKV-GRGTYGHVYKAKrkDGKDEKEYALKQIEGTG-ISMSACREIALLRELKHP------NVIALQKVFLSHSdr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSMNLYELIK-----KNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQG--RSGIKV 366
Cdd:cd07867   75 KVWLLFDYAEHDLWHIIKfhrasKANKKPMQLPrsMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpeRGRVKI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 367 ID------FGSSCYEHQRVYTYIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEG---------DQ 430
Cdd:cd07867  155 ADmgfarlFNSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEDiktsnpfhhDQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 431 LACMIELLGMPSQKLLDASKRAKNFVS-SKGYPRyctvTTLSDGSVVlnggrSRRGKLRGPPESRewgnalkgcddpLFL 509
Cdd:cd07867  235 LDRIFSVMGFPADKDWEDIRKMPEYPTlQKDFRR----TTYANSSLI-----KYMEKHKVKPDSK------------VFL 293
                        330       340
                 ....*....|....*....|....*.
gi 153281169 510 dFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd07867  294 -LLQKLLTMDPTKRITSEQALQDPYF 318
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
222-535 3.41e-23

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 99.26  E-value: 3.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHrQAAEEIRILehlrKQDKdnTMNVIHMLENFTFRNH--ICM 299
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQ-EIIKEISIL----KQCD--SPYIVKYYGSYFKNTDlwIVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TF-ELLSMN-LYELIKKNkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC---Y 374
Cdd:cd06612   78 EYcGAGSVSdIMKITNKT----LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ--AKLADFGVSGqltD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDQLAcMIELLGMPSQKLLDASKrakn 454
Cdd:cd06612  152 TMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKP--PYSDIHPMRA-IFMIPNKPPPTLSDPEK---- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 fvsskgypryctvttlsdgsvvlnggrsrrgklrgppesreWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd06612  225 -----------------------------------------W--------SPEFNDFVKKCLVKDPEERPSAIQLLQHPF 255

                 .
gi 153281169 535 L 535
Cdd:cd06612  256 I 256
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
222-418 3.93e-23

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: 98.87  E-value: 3.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLRK----------QDKDNTMNVIHM 287
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRnvlnELEILQELEHpflvnlwysfQDEEDMYMVVDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 288 LENFTFRNHIcmtfellsmnlyelIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVI 367
Cdd:cd05578   82 LLGGDLRYHL--------------QQKVKF---SEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH--VHIT 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 368 DFGSSCYEHQRVYT--YIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05578  143 DFNIATKLTDGTLAtsTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRG 195
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
228-420 5.08e-23

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: 98.51  E-value: 5.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYdHKVHQH--VALKMVrNEKRFHRQAAE----EIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd14121    3 LGSGTYATVYKAY-RKSGARevVAVKCV-SKSSLNKASTEnlltEIELLKKLKHP------HIVELKDFQWDEEHIYLIM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSM-NLYELIKKNKfqgfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCY--EH 376
Cdd:cd14121   75 EYCSGgDLSRFIRSRR----TLPesTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHlkPN 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14121  151 DEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRA 194
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
221-535 6.23e-23

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: 98.91  E-value: 6.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd06608    7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHP-----NIATFYGAFIKKDPPGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FEL-LSMNL------YELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS 371
Cdd:cd06608   82 DQLwLVMEYcgggsvTDLVKGLRKKGKRLKeeWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE--VKLVDFGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SC---YEHQRVYTYIQSRFYRAPEVI-----LGARYGMPIDMWSLGCILAELLTGYPLLpgedeGDQ--LACMIELLGMP 441
Cdd:cd06608  160 SAqldSTLGRRNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIELADGKPPL-----CDMhpMRALFKIPRNP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 442 SQKLLDASKRAKNFVsskgypryctvttlsdgsvvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPA 521
Cdd:cd06608  235 PPTLKSPEKWSKEFN-----------------------------------------------------DFISECLIKNYE 261
                        330
                 ....*....|....
gi 153281169 522 VRMTPGQALRHPWL 535
Cdd:cd06608  262 QRPFTEELLEHPFI 275
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
225-420 9.24e-23

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: 97.94  E-value: 9.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRiLEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELL 304
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVK-AERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SM-NLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS--CYEHQRVYT 381
Cdd:cd05611   80 NGgDCASLIKT--LGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH--LKLTDFGLSrnGLEKRHNKK 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153281169 382 YIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05611  156 FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYP 194
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
222-535 1.41e-22

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: 97.62  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKrfhrQAAEEIRILEH----LRKQDKDNtmnVIHMLENFTFRNHI 297
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREK----AGSSAVKLLERevdiLKHVNHAH---IIHLEEVFETPKRM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELL-SMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQ-----QGRSGIKVIDFGS 371
Cdd:cd14097   76 YLVMELCeDGELKELLLRKGF--FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidnNDKLNIKVTDFGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SCYEHQRVYTYIQSR----FYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEgdqlacmiellgmpsQKLLD 447
Cdd:cd14097  154 SVQKYGLGEDMLQETcgtpIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSE---------------EKLFE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 448 ASKRAKnfvsskgypryCTVTTLSDGSVvlnggrSRRGKlrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPG 527
Cdd:cd14097  219 EIRKGD-----------LTFTQSVWQSV------SDAAK-----------------------NVLQQLLKVDPAHRMTAS 258

                 ....*...
gi 153281169 528 QALRHPWL 535
Cdd:cd14097  259 ELLDNPWI 266
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
226-535 1.44e-22

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: 97.47  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAE----EIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvDDDKKSRESVKqleqEIALLSKLRHP------NIVQYYGTEREEDNLYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSScyEHQR 378
Cdd:cd06632   80 FLEYVPGgSIHKLLQR--YGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV--VKLADFGMA--KHVE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTYIQS----RFYRAPEVIL--GARYGMPIDMWSLGCILAELLTGYPllP-GEDEGDQlacmiellgmpsqklldaskr 451
Cdd:cd06632  154 AFSFAKSfkgsPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKP--PwSQYEGVA--------------------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 452 aknfvsskgypryctvttlsdgsVVLNGGRSrrGKLRGPPESREwgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd06632  211 -----------------------AIFKIGNS--GELPPIPDHLS----------PDAKDFIRLCLQRDPEDRPTASQLLE 255

                 ....
gi 153281169 532 HPWL 535
Cdd:cd06632  256 HPFV 259
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
219-443 1.53e-22

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 98.23  E-value: 1.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 219 AYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTfrnh 296
Cdd:cd07869    4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRlqEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLT---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 icMTFELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 376
Cdd:cd07869   80 --LVFEYVHTDLCQYMDKHP-GGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE--LKLADFGLARAKS 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 377 QRVYTY---IQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTGYPLLPG-EDEGDQLACMIELLGMPSQ 443
Cdd:cd07869  155 VPSHTYsneVVTLWYRPPDVLLGStEYSTCLDMWGVGCIFVEMIQGVAAFPGmKDIQDQLERIFLVLGTPNE 226
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
228-419 2.24e-22

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: 96.99  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHV--ALKMVR------NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLE-NFTFRNHIC 298
Cdd:cd13994    1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRrrddesKRKDYVKRLTSEYIISSKLHHP------NIVKVLDlCQDLHGKWC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS----- 372
Cdd:cd13994   75 LVMEYCPGgDLFTLIEKAD--SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV--LKLTDFGTAevfgm 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYTY--IQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGY 419
Cdd:cd13994  151 PAEKESPMSAglCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGR 200
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
221-415 2.33e-22

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: 96.96  E-value: 2.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLrkqdkdNTMNVIHMLENFTFRNH 296
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQdclkEIDLLQQL------NHPNIIKYLASFIENNE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSM-NLYELIKKNKFQG--FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:cd08224   75 LNIVLELADAgDLSRLIKHFKKQKrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGV--VKLGDLGLGR 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 374 Y-------EHQRVYTyiqsRFYRAPEVILGARYGMPIDMWSLGCILAEL 415
Cdd:cd08224  153 FfsskttaAHSLVGT----PYYMSPERIREQGYDFKSDIWSLGCLLYEM 197
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
221-430 2.61e-22

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: 96.63  E-value: 2.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQ--AAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmIENEVAILRRVKHP------NIVQLIEEYDTDTELY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKK-NKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL--KQQGRSGIKVIDFGSSCY 374
Cdd:cd14095   75 LVMELVKGgDLFDAITSsTKF---TERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveHEDGSKSLKLADFGLATE 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDeGDQ 430
Cdd:cd14095  152 VKEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPD-RDQ 206
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
222-420 2.75e-22

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: 96.33  E-value: 2.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYdHKVHQHV-ALKMV---RNEKRFHRQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHI 297
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVV-RKVDGRVyALKQIdisRMSRKMREEAIDEARVLSKL------NSPYVIKYYDSFVDKGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG------ 370
Cdd:cd08529   75 NIVMEYAENgDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN--VKIGDLGvakils 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 371 -SSCYEHqrvyTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YP 420
Cdd:cd08529  153 dTTNFAQ----TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGkHP 200
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
220-457 2.86e-22

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 96.52  E-value: 2.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRneKRFHRQAAE---EIRILEHLrkqdkdNTMNVIHMLENFTFRNH 296
Cdd:cd14193    4 YNVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIK--ARSQKEKEEvknEIEVMNQL------NHANLIQLYDAFESRND 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSM-NLYELIKKNKFQGFSLPLVrKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFG-SSCY 374
Cdd:cd14193   76 IVLVMEYVDGgELFDRIIDENYNLTELDTI-LFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGlARRY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 E-HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQ----LACMIELLGmpsQKLLDAS 449
Cdd:cd14193  155 KpREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETlnniLACQWDFED---EEFADIS 231

                 ....*...
gi 153281169 450 KRAKNFVS 457
Cdd:cd14193  232 EEAKDFIS 239
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
228-535 3.19e-22

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: 96.14  E-value: 3.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS- 305
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRnEIEIMNQLRHP------RLLQLYDAFETPREMVLVMEYVAg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSScyehqRVY---TY 382
Cdd:cd14103   75 GELFERVVDDDFE-LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLA-----RKYdpdKK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 383 IQSRF----YRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLpGEDEGDQLAcmiellgmpsqklldaskraknfvs 457
Cdd:cd14103  149 LKVLFgtpeFVAPEVVNYEPISYATDMWSVGVICYVLLSGLsPFM-GDNDAETLA------------------------- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 458 skgypryctvttlsdgsvvlnggrsrrgklrgppesrewgNALKGC---DDPLF-------LDFLKQCLEWDPAVRMTPG 527
Cdd:cd14103  203 ----------------------------------------NVTRAKwdfDDEAFddisdeaKDFISKLLVKDPRKRMSAA 242

                 ....*...
gi 153281169 528 QALRHPWL 535
Cdd:cd14103  243 QCLQHPWL 250
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
214-543 4.26e-22

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: 96.35  E-value: 4.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 214 PHDHvayrYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfhrQAAE------EIRILEHLRKQdkdntmNVIHM 287
Cdd:cd06611    3 PNDI----WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE-----SEEEledfmvEIDILSECKHP------NIVGL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 288 LENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVI 367
Cdd:cd06611   68 YEAYFYENKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDG--DVKLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFGSSC---YEHQRVYTYIQSRFYRAPEVIL-----GARYGMPIDMWSLGCILAELLTGYPllPGEDegdqLACMIELLG 439
Cdd:cd06611  146 DFGVSAknkSTLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEP--PHHE----LNPMRVLLK 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 440 MPsqklldaskraknfvssKGYPryctvTTLSdgsvvlnggrsrrgklrgppESREWGNALKgcddplflDFLKQCLEWD 519
Cdd:cd06611  220 IL-----------------KSEP-----PTLD--------------------QPSKWSSSFN--------DFLKSCLVKD 249
                        330       340
                 ....*....|....*....|....
gi 153281169 520 PAVRMTPGQALRHPWLRRRLPKPP 543
Cdd:cd06611  250 PDDRPTAAELLKHPFVSDQSDNKA 273
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
221-542 6.36e-22

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: 96.33  E-value: 6.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRnekrFHRQAAEEIRILEHLRKQDKDNTmNVIHMLENFTFRNHICMT 300
Cdd:cd06655   20 KYTRYEKIGQGASGTVFTAIDVATGQEVAIKQIN----LQKQPKKELIINEILVMKELKNP-NIVNFLDSFLVGDELFVV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY---EH 376
Cdd:cd06655   95 MEYLAGgSLTDVVTETCMDEAQIAAV---CRECLQALEFLHANQVIHRDIKSDNVLLGMDG--SVKLTDFGFCAQitpEQ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDegdqlacmiellgmpsqklldaSKRAKNFV 456
Cdd:cd06655  170 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN----------------------PLRALYLI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 SSKGYPRYCTVTTLSdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPWLr 536
Cdd:cd06655  228 ATNGTPELQNPEKLS----------------------------------PIFRDFLNRCLEMDVEKRGSAKELLQHPFL- 272

                 ....*.
gi 153281169 537 rRLPKP 542
Cdd:cd06655  273 -KLAKP 277
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
222-420 8.56e-22

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: 95.30  E-value: 8.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALK------MVRNEKrfhRQAAEEIRILEHL----------RKQDKDNTmnvi 285
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKeidygkMSEKEK---QQLVSEVNILRELkhpnivryydRIVDRANT---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 286 hmlenftfRNHICMTF---ELLSMnlyeLIKKNKFQGFSLP--LVRKFAHSILQCLDALH-----KNRIIHCDLKPENIL 355
Cdd:cd08217   75 --------TLYIVMEYcegGDLAQ----LIKKCKKENQYIPeeFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIF 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 356 LKQQGrsGIKVIDFG-SSCYEHQRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd08217  143 LDSDN--NVKLGDFGlARVLSHDSSFakTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHP 208
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
222-420 1.49e-21

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: 95.76  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIR----ILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd05599    3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRaerdILAEADNP------WVVKLYYSFQDEENL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLS----MNLyeLIKKNKFQgfslPLVRKF--AHSILqCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS 371
Cdd:cd05599   77 YLIMEFLPggdmMTL--LMKKDTLT----EEETRFyiAETVL-AIESIHKLGYIHRDIKPDNLLLDARGH--IKLSDFGL 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 372 SCYEH--QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05599  148 CTGLKksHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYP 198
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
222-419 2.43e-21

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 93.77  E-value: 2.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRfhRQAAEEI-----RILEHLRKQDKDNtmnVIHMLENFTFRN- 295
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIV--DRR--RASPDFVqkflpRELSILRRVNHPN---IVQMFECIEVANg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSCYE 375
Cdd:cd14164   75 RLYIVMEAAATDLLQKIQEVHH--IPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK-IKIADFGFARFV 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 376 H---QRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGY 419
Cdd:cd14164  152 EdypELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGT 199
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
222-420 2.55e-21

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


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 94.39  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRF-HRQAAE---EIRILEHLrkqdkdNTMNVIHMLENFTFRNHI 297
Cdd:cd14209    3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVkLKQVEHtlnEKRILQAI------NFPFLVKLEYSFKDNSNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 376
Cdd:cd14209   77 YMVMEYVPGgEMFSHLRRIG--RFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGY--IKVTDFGFAKRVK 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14209  153 GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYP 196
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
220-535 3.45e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 95.12  E-value: 3.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKViGKGSFGQVVKAY--DHKVHQHVALKMVRNEKrFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFR--N 295
Cdd:cd07868   18 FEYEGCKV-GRGTYGHVYKAKrkDGKDDKDYALKQIEGTG-ISMSACREIALLRELKHP------NVISLQKVFLSHadR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSMNLYELIK-----KNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQG--RSGIKV 366
Cdd:cd07868   90 KVWLLFDYAEHDLWHIIKfhrasKANKKPVQLPrgMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpeRGRVKI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 367 ID------FGSSCYEHQRVYTYIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGEDEG---------DQ 430
Cdd:cd07868  170 ADmgfarlFNSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEDiktsnpyhhDQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 431 LACMIELLGMPSQK-LLDASKRAKNFVSSKGYPRyctvTTLSDGSVVlnggrSRRGKLRGPPESREWgnalkgcddplfl 509
Cdd:cd07868  250 LDRIFNVMGFPADKdWEDIKKMPEHSTLMKDFRR----NTYTNCSLI-----KYMEKHKVKPDSKAF------------- 307
                        330       340
                 ....*....|....*....|....*.
gi 153281169 510 DFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd07868  308 HLLQKLLTMDPIKRITSEQAMQDPYF 333
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
226-535 4.68e-21

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: 93.18  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEhlrkQDKDNTmNVIHMLENFTFRNHICMTFE 302
Cdd:cd14106   14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEilhEIAVLE----LCKDCP-RVVNLHEVYETRSELILILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-KQQGRSGIKVIDFGSSCY--EHQR 378
Cdd:cd14106   89 LAAGgELQTLLDEE--ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFPLGDIKLCDFGISRVigEGEE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQlacmiellgmpsqklldaskraknfvss 458
Cdd:cd14106  167 IREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQET---------------------------- 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 459 kgyprYCTVTtlsdgsvvlnggrsrRGKLRGPPEsrEWGNAlkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14106  219 -----FLNIS---------------QCNLDFPEE--LFKDV-----SPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
222-535 4.96e-21

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: 93.17  E-value: 4.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA--EEIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSieNEIAVLHKIKHP------NIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNlyELIKKNKFQGFSLPlvRKFAHSILQCLDA---LHKNRIIHCDLKPENILL-KQQGRSGIKVIDFGSSCYE 375
Cdd:cd14167   79 IMQLVSGG--ELFDRIVEKGFYTE--RDASKLIFQILDAvkyLHDMGIVHRDLKPENLLYySLDEDSKIMISDFGLSKIE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 H--QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDqlacmiellgmpsQKLLDASKRAK 453
Cdd:cd14167  155 GsgSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP--PFYDEND-------------AKLFEQILKAE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFVSSkgyPRYctvTTLSDGSVvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14167  220 YEFDS---PYW---DDISDSAK----------------------------------DFIQHLMEKDPEKRFTCEQALQHP 259

                 ..
gi 153281169 534 WL 535
Cdd:cd14167  260 WI 261
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
221-417 7.23e-21

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: 92.34  E-value: 7.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFH--RQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSavEDSRKEAVLLAKMKHP------NIVAFKESFEADGHLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLS-MNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS-CYEH 376
Cdd:cd08219   75 IVMEYCDgGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK--VKLGDFGSArLLTS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 377 QRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08219  153 PGAYacTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCT 195
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
221-554 8.88e-21

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: 92.62  E-value: 8.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd14104    1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHR------NILRLHESFESHEELVMI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLS-MNLYELIKKNKFQGFSLPLVrKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYE---H 376
Cdd:cd14104   75 FEFISgVDIFERITTARFELNEREIV-SYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLkpgD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYrAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELlgmpsqklldaskraknfv 456
Cdd:cd14104  154 KFRLQYTSAEFY-APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNA------------------- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 sskgypryctvttlsdgsvvlnggrsrrgklrgppesrEWG---NALKGCDDPLfLDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14104  214 --------------------------------------EYAfddEAFKNISIEA-LDFVDRLLVKERKSRMTAQEALNHP 254
                        330       340
                 ....*....|....*....|.
gi 153281169 534 WLRRRLpkpptgEKTSVKRIT 554
Cdd:cd14104  255 WLKQGM------ETVSSKDIK 269
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
221-542 1.04e-20

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: 92.86  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKmvrnEKRFHRQAAEEIRILEHLRKQDKDNTmNVIHMLENFTFRNHICMT 300
Cdd:cd06656   20 KYTRFEKIGQGASGTVYTAIDIATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY---EH 376
Cdd:cd06656   95 MEYLAGgSLTDVVTETCMDEGQIAAV---CRECLQALDFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDegdqlacmiellgmpsqklldaSKRAKNFV 456
Cdd:cd06656  170 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN----------------------PLRALYLI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 SSKGYPRYCTVTTLSdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPWLr 536
Cdd:cd06656  228 ATNGTPELQNPERLS----------------------------------AVFRDFLNRCLEMDVDRRGSAKELLQHPFL- 272

                 ....*.
gi 153281169 537 rRLPKP 542
Cdd:cd06656  273 -KLAKP 277
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
222-458 1.22e-20

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 91.95  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEV--LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE-EIRILEHLrkqdkdNTMNVIHMLENFTFRNHIC 298
Cdd:cd14192    4 YAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKnEINIMNQL------NHVNLIQLYDAFESKTNLT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKFQGFSLPLVRkFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFG-SSCYE- 375
Cdd:cd14192   78 LIMEYVDGgELFDRITDESYQLTELDAIL-FTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGlARRYKp 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL-LGMPSQKLLDASKRAKN 454
Cdd:cd14192  157 REKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCkWDFDAEAFENLSEEAKD 236

                 ....
gi 153281169 455 FVSS 458
Cdd:cd14192  237 FISR 240
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
221-536 1.81e-20

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: 91.14  E-value: 1.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRnekrFHRQAAEEIRILEHLRKQDKDNTmNVIHMLENFTFRNHICMT 300
Cdd:cd06647    8 KYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY---EH 376
Cdd:cd06647   83 MEYLAGgSLTDVVTETCMDEGQIAAV---CRECLQALEFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDegdqlacmiellgmpsqklldaSKRAKNFV 456
Cdd:cd06647  158 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN----------------------PLRALYLI 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 SSKGYPRYCTVTTLSdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPWLR 536
Cdd:cd06647  216 ATNGTPELQNPEKLS----------------------------------AIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
226-429 2.10e-20

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 92.28  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEhlrKQDKDNTMnvIHMLENFTFRNHICMTF 301
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVEctmtEKRVLA---LANRHPFL--TGLHACFQTEDRLYFVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLS----MnlYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---SSCY 374
Cdd:cd05570   76 EYVNggdlM--FHIQRARRF---TEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGH--IKIADFGmckEGIW 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGD 429
Cdd:cd05570  149 GGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDE 203
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
221-418 2.14e-20

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: 91.61  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR------NEKR--FHRQAAEEIRILEHLRKQdkdntmNVIHMLENFT 292
Cdd:cd13990    1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQlnkdwsEEKKqnYIKHALREYEIHKSLDHP------RIVKLYDVFE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNH-ICMTFELLSMN-LYELIKKNKfqgfSLPlvRKFAHSIL-QCLDAL-----HKNRIIHCDLKPENILLKQQGRSG- 363
Cdd:cd13990   75 IDTDsFCTVLEYCDGNdLDFYLKQHK----SIP--EREARSIImQVVSALkylneIKPPIIHYDLKPGNILLHSGNVSGe 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 364 IKVIDFGSSCYEHQRVY-------------TYiqsrFYRAPEVILGARyGMPI-----DMWSLGCILAELLTG 418
Cdd:cd13990  149 IKITDFGLSKIMDDESYnsdgmeltsqgagTY----WYLPPECFVVGK-TPPKisskvDVWSVGVIFYQMLYG 216
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
225-426 2.50e-20

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: 90.69  E-value: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   225 LKVIGKGSFGQVVKAY----DHKVHQHVALKMVRNE------KRFHRqaaeEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:smart00221   4 GKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDaseqqiEEFLR----EARIMRKLDHP------NIVKLLGVCTEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   295 NHICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:smart00221  74 EPLMIVMEYMPGgDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV--VKISDFGLSR 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169   374 YEHQRVYTYIQSR----FYRAPEVILGARYGMPIDMWSLGCILAELLTG----YPLLPGED 426
Cdd:smart00221 152 DLYDDDYYKVKGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgeepYPGMSNAE 212
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
222-420 2.54e-20

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: 90.69  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMI--DKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELL---SMNLYeliKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSC---YE 375
Cdd:cd14186   81 EMChngEMSRY---LKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRN--MNIKIADFGLATqlkMP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14186  156 HEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRP 200
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
222-420 2.58e-20

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: 91.73  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKM--------VRNEKRFHrqaaEEIRILEHLRKQdkdntmNVIHMLENFTF 293
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVmaipevirLKQEQHVH----NEKRVLKEVSHP------FIIRLFWTEHD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSMNlyELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:cd05612   73 QRFLYMLMEYVPGG--ELFSYLRNSGrFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH--IKLTDFGFA 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 373 CYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05612  149 KKLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYP 196
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
222-437 4.23e-20

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: 90.01  E-value: 4.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGqVVKAYDH-KVHQHVALKMVRNEKRFHRQ--AAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd14185    2 YEIGRTIGDGNFA-VVKECRHwNENQEYAMKIIDKSKLKGKEdmIESEILIIKSLSHP------NIVKLFEVYETEKEIY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELL-SMNLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQ--GRSGIKVIDFGSSCYE 375
Cdd:cd14185   75 LILEYVrGGDLFDAIIES--VKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNpdKSTTLKLADFGLAKYV 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGED-EGDQLACMIEL 437
Cdd:cd14185  153 TGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPErDQEELFQIIQL 215
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
227-418 4.66e-20

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 90.29  E-value: 4.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKVHQHVALKMV-------RNEKRfHRQAAE----EIRILEHLRKQdkdntmNVIHMLENFTFRN 295
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKQVelpsvsaENKDR-KKSMLDalqrEIALLRELQHE------NIVQYLGSSSDAN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFE---------LLSMnlyelikknkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKV 366
Cdd:cd06628   80 HLNIFLEyvpggsvatLLNN----------YGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG--GIKI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 367 IDFG-SSCYEHQRVYTYIQ--------SRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd06628  148 SDFGiSKKLEANSLSTKNNgarpslqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTG 208
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
226-418 4.76e-20

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: 90.47  E-value: 4.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRnEKRFHRQAAEEIRILEhlrKQ--DKDNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd05630    6 RVLGKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRKGEAMALNE---KQilEKVNSRFVVSLAYAYETKDALCLVLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 -----LSMNLYELIKKnkfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY--EH 376
Cdd:cd05630   82 mnggdLKFHIYHMGQA----GFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH--IRISDLGLAVHvpEG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05630  156 QTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAG 197
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
225-426 6.42e-20

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 89.51  E-value: 6.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   225 LKVIGKGSFGQVVKAY----DHKVHQHVALKMVRNE------KRFHRqaaeEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:smart00219   4 GKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDaseqqiEEFLR----EARIMRKLDHP------NVVKLLGVCTEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   295 NHICMTFELLSM-NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:smart00219  74 EPLYIVMEYMEGgDLLSYLRKNR-PKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV--VKISDFGLSR 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169   374 YEHQRVYTYIQSR----FYRAPEVILGARYGMPIDMWSLGCILAELLTG----YPLLPGED 426
Cdd:smart00219 151 DLYDDDYYRKRGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgeqpYPGMSNEE 211
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
221-418 6.63e-20

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: 89.60  E-value: 6.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK-------RFHRQAAEEIRILEHLRKQDKDNtmnVIHMLENFTF 293
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewamiNGPVPVPLEIALLLKASKPGVPG---VIRLLDWYER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFE--LLSMNLYELIKKnkfQGfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDF 369
Cdd:cd14005   78 PDGFLLIMErpEPCQDLFDFITE---RG-ALSenLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLR-TGEVKLIDF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 370 GSSCYEHQRVYT-YIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG 418
Cdd:cd14005  153 GCGALLKDSVYTdFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCG 203
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
222-536 6.64e-20

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: 90.27  E-value: 6.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN--EKRFHRQaaeEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICM 299
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKtvDKKIVRT---EIGVLLRL------SHPNIIKLKEIFETPTEISL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNlyELIKKNKFQGFSLPlvRKFAHSILQCLDA---LHKNRIIHCDLKPENILLKQQG-RSGIKVIDFGSSCYE 375
Cdd:cd14085   76 VLELVTGG--ELFDRIVEKGYYSE--RDAADAVKQILEAvayLHENGIVHRDLKPENLLYATPApDAPLKIADFGLSKIV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLpgEDEGDQLAcmiellgmpSQKLLDASkra 452
Cdd:cd14085  152 DQQVTmkTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFePFY--DERGDQYM---------FKRILNCD--- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 453 KNFVSskgyPRYCTVttlSDGSVvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRH 532
Cdd:cd14085  218 YDFVS----PWWDDV---SLNAK----------------------------------DLVKKLIVLDPKKRLTTQQALQH 256

                 ....
gi 153281169 533 PWLR 536
Cdd:cd14085  257 PWVT 260
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
226-549 6.94e-20

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: 90.48  E-value: 6.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRqaaeEIRIleHLRKQDKDNTMNVIHMLENFtFRNHICMTFELLS 305
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARR----EVEL--HWRASQCPHIVRIVDVYENL-YAGRKCLLIVMEC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MN---LYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-KQQGRSGIKVIDFG--SSCYEHQRV 379
Cdd:cd14170   81 LDggeLFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYtSKRPNAILKLTDFGfaKETTSHNSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllpgedegdqlacmiellgmpsqklldaskrakNFVSSK 459
Cdd:cd14170  161 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYP---------------------------------PFYSNH 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 460 GYpryctvtTLSDGSvvlnGGRSRRGKLRGP-PESREWGNALKgcddplflDFLKQCLEWDPAVRMTPGQALRHPWLRRR 538
Cdd:cd14170  208 GL-------AISPGM----KTRIRMGQYEFPnPEWSEVSEEVK--------MLIRNLLKTEPTQRMTITEFMNHPWIMQS 268
                        330
                 ....*....|.
gi 153281169 539 LPKPPTGEKTS 549
Cdd:cd14170  269 TKVPQTPLHTS 279
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
228-420 9.52e-20

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: 89.28  E-value: 9.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfhrqaaeeIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFEL-LSM 306
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSKR--------PEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYcTGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFqgfsLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYE--------- 375
Cdd:cd14010   80 DLETLLRQDGN----LPesSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGT--LKLSDFGLARREgeilkelfg 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 376 ----------HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14010  154 qfsdegnvnkVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKP 208
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
226-535 1.14e-19

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: 88.98  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMV--------RNEKRFH------RQAAEEIRILEHLrkqdkdntmNVIHMLENF 291
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVelpktssdRADSRQKtvvdalKSEIDTLKDLDHP---------NIVQYLGFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLS----MNLYElikknKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVI 367
Cdd:cd06629   78 ETEDYFSIFLEYVPggsiGSCLR-----KYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGIC--KIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFGSS-----CYEHQRVYTYIQSRFYRAPEVI--LGARYGMPIDMWSLGCILAELLTGYPllPGEDEgDQLACMIELlgm 440
Cdd:cd06629  151 DFGISkksddIYGNNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRR--PWSDD-EAIAAMFKL--- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 441 psqklldaskraknfvsskgypryctvttlsdgsvvlnggrsrrGKLRGPPESREWGNAlkgcdDPLFLDFLKQCLEWDP 520
Cdd:cd06629  225 --------------------------------------------GNKRSAPPVPEDVNL-----SPEALDFLNACFAIDP 255
                        330
                 ....*....|....*
gi 153281169 521 AVRMTPGQALRHPWL 535
Cdd:cd06629  256 RDRPTAAELLSHPFL 270
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
222-420 1.19e-19

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 90.26  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRnekrfhRQAAEEIRILEHLrKQDKDNTMNVIH-----MLENFTFRNH 296
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK------KREILKMKQVQHV-AQEKSILMELSHpfivnMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFE-LLSMNLY-ELIKKNKFQGFslplVRKFAHS-ILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:PTZ00263  93 VYFLLEfVVGGELFtHLRKAGRFPND----VAKFYHAeLVLAFEYLHSKDIIYRDLKPENLLLDNKGH--VKVTDFGFAK 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:PTZ00263 167 KVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYP 213
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
223-533 1.39e-19

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: 89.42  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAydhkvhQHVALKMVRNEKRFHRQAAEEIR--ILEHLRKQDKDNTMNVIHMLENFTFR-NHICM 299
Cdd:cd06620    8 ETLKDLGAGNGGSVSKV------LHIPTGTIMAKKVIHIDAKSSVRkqILRELQILHECHSPYIVSFYGAFLNEnNNIII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKnKFQGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQR 378
Cdd:cd06620   82 CMEYMDCGSLDKILK-KKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQ--IKLCDFGVSGELINS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VY-TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEDEGDQLACMIELLGMPSQKLLDASKRaknFV 456
Cdd:cd06620  159 IAdTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGeFPFAGSNDDDDGYNGPMGILDLLQRIVNEPPPR---LP 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 457 SSKGYPRYCTvttlsdgsvvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd06620  236 KDRIFPKDLR-------------------------------------------DFVDRCLLKDPRERPSPQLLLDHD 269
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
222-535 1.62e-19

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: 88.79  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA--EEIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMveNEIAVLRRINHE------NIVSLEDIYESPTHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNlyELIKKNKFQGFSLPlvRKFAHSILQCLDA---LHKNRIIHCDLKPENILLKQQGR-SGIKVIDFGSSCYE 375
Cdd:cd14169   79 AMELVTGG--ELFDRIIERGSYTE--KDASQLIGQVLQAvkyLHQLGIVHRDLKPENLLYATPFEdSKIMISDFGLSKIE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVY-TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDQlacmiELLgmpsQKLLDASKRAkn 454
Cdd:cd14169  155 AQGMLsTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYP--PFYDENDS-----ELF----NQILKAEYEF-- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 fvsskgypryctvttlsdgsvvlnggrsrrgklrgppESREWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd14169  222 -------------------------------------DSPYWDDISESAK-----DFIRHLLERDPEKRFTCEQALQHPW 259

                 .
gi 153281169 535 L 535
Cdd:cd14169  260 I 260
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
222-538 1.80e-19

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: 89.14  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAA-------EEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIV-DVAKFTSSPGlstedlkREASICHMLKHP------HIVELLETYSSD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMN--LYELIKK--NKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDF 369
Cdd:cd14094   78 GMLYMVFEFMDGAdlCFEIVKRadAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 370 GSS-------CYEHQRVYTyiqsRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllpgedegdqlacmiellgmps 442
Cdd:cd14094  157 GVAiqlgesgLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCL---------------------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 443 qklldaskraknfvsskgyPRYCTVTTLSDGSVvlnggrsrRGKLrgPPESREWGNALKGCDdplflDFLKQCLEWDPAV 522
Cdd:cd14094  211 -------------------PFYGTKERLFEGII--------KGKY--KMNPRQWSHISESAK-----DLVRRMLMLDPAE 256
                        330
                 ....*....|....*.
gi 153281169 523 RMTPGQALRHPWLRRR 538
Cdd:cd14094  257 RITVYEALNHPWIKER 272
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
226-431 2.61e-19

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: 89.23  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMnVIHMLENFTFRNHICMTFELLS 305
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPF-LTHLYCTFQTKEHLFFVMEFLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MN--LYELIKKNKFQGFSLPLvrkFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---SSCYEHQRVY 380
Cdd:cd05620   80 GGdlMFHIQDKGRFDLYRATF---YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH--IKIADFGmckENVFGDNRAS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEgDQL 431
Cdd:cd05620  155 TFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDE-DEL 204
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
221-457 2.92e-19

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: 88.65  E-value: 2.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKA-YDHKVHQHVALKMVRNEK--RFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHI 297
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVRKADlsSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNlyELIKK-NKFQGFSLPLVRkfaHSILQCLDA---LHKNRIIHCDLKPENILL----------KQQGRSG 363
Cdd:cd14096   82 YIVLELADGG--EIFHQiVRLTYFSEDLSR---HVITQVASAvkyLHEIGVVHRDIKPENLLFepipfipsivKLRKADD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 364 ---------------------IKVIDFG-SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPl 421
Cdd:cd14096  157 detkvdegefipgvggggigiVKLADFGlSKQVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 422 lPGEDEGdqlacmIELLGMpsqKLL------------DASKRAKNFVS 457
Cdd:cd14096  236 -PFYDES------IETLTE---KISrgdytflspwwdEISKSAKDLIS 273
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
221-418 3.11e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 91.39  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE--------KRFHR--QAAEEiriLEH-----LRKQDKDNTMNVI 285
Cdd:NF033483   8 RYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDlardpefvARFRReaQSAAS---LSHpnivsVYDVGEDGGIPYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 286 HMlenftfrnhicmtfELLS-MNLYELIKKNKfqgfslPL-VRK---FAHSILQCLDALHKNRIIHCDLKPENILLKQQG 360
Cdd:NF033483  85 VM--------------EYVDgRTLKDYIREHG------PLsPEEaveIMIQILSALEHAHRNGIVHRDIKPQNILITKDG 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 361 RsgIKVIDFG-------SSCYEHQRVytyIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:NF033483 145 R--VKVTDFGiaralssTTMTQTNSV---LGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTG 204
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
228-423 4.50e-19

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 87.89  E-value: 4.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLRKQDKDNTMNVIHMLENFTfRNHIcmtfEL 303
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRErwclEVQIMKKLNHPNVVSARDVPPELEKLS-PNDL----PL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSM------NLYELIkkNKFQ---GFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGI-KVIDFG--- 370
Cdd:cd13989   76 LAMeycsggDLRKVL--NQPEnccGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGyak 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 371 -----SSCYEhqrvytYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLP 423
Cdd:cd13989  154 eldqgSLCTS------FVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYrPFLP 206
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
222-431 4.54e-19

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: 87.08  E-value: 4.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVL--KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEHLRKQdkdntmNVIHMLENFTFRNH 296
Cdd:cd14082    3 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQlrnEVAILQQLSHP------GVVNLECMFETPER 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-SGIKVIDFGSSCYE 375
Cdd:cd14082   77 VFVVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfPQVKLCDFGFARII 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 376 HQRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEDEGDQL 431
Cdd:cd14082  157 GEKSFrrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDINDQI 215
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
222-418 4.62e-19

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: 87.00  E-value: 4.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV---RNEKRFHRQAAEEIRIlehlrkQDKDNTMNVIHMLeNFTFRNHIC 298
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkRAPGDCPENIKKEVCI------QKMLSHKNVVRFY-GHRREGEFQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTF-ELLSMNlyELIKKNKFQ-GFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIKVIDFG-SSCYE 375
Cdd:cd14069   76 YLFlEYASGG--ELFDKIEPDvGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLL--DENDNLKISDFGlATVFR 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 376 H---QRVYT-YIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG 418
Cdd:cd14069  152 YkgkERLLNkMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAG 199
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
222-421 6.30e-19

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 87.30  E-value: 6.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAY--DHKVHQHVAlkmvrnEKRFHRQAAeeirILEHLRKQDkdntmNVIHMLENFTfrNHI-- 297
Cdd:cd14020   17 YRVSSGRGADQPTSALKEFqlDHQGSQESG------DYGFAKERA----ALEQLQGHR-----NIVTLYGVFT--NHYsa 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 -----CMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSS 372
Cdd:cd14020   80 nvpsrCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDEC-FKLIDFGLS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYTYIQSRFYRAPEVILG---ARYGM--------PIDMWSLGCILAELLTGYPL 421
Cdd:cd14020  159 FKEGNQDVKYIQTDGYRAPEAELQnclAQAGLqsetectsAVDLWSLGIVLLEMFSGMKL 218
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
222-537 9.07e-19

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 87.11  E-value: 9.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAydhkVHQHVALKMVRneKRFHRQAAEEIR--ILEHLRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd06615    3 FEKLGELGAGNGGVVTKV----LHRPSGLIMAR--KLIHLEIKPAIRnqIIRELKVLHECNSPYIVGFYGAFYSDGEISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKnKFQGFSLPLVRKFAHSILQCLDALH-KNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQR 378
Cdd:cd06615   77 CMEHMDGGSLDQVLK-KAGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNILVNSRGE--IKLCDFGVSGQLIDS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VY-TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPlLPGEDEGdQLACMielLGMPSQKLLDASKRAKNFV 456
Cdd:cd06615  154 MAnSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrYP-IPPPDAK-ELEAM---FGRPVSEGEAKESHRPVSG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 SSKGYPRYCTVTTLSDGSVvlnggrsrrgklRGPPESREwgnalKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLR 536
Cdd:cd06615  229 HPPDSPRPMAIFELLDYIV------------NEPPPKLP-----SGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291

                 .
gi 153281169 537 R 537
Cdd:cd06615  292 R 292
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
226-420 1.01e-18

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: 86.64  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRnEKRFHRQAAE-----EIRILEhlrkqdKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd05605    6 RVLGKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRKGEamalnEKQILE------KVNSRFVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELlsMNLYELikknKFQ-------GFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:cd05605   79 LTI--MNGGDL----KFHiynmgnpGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGH--VRISDLGLAV 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 374 Y--EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05605  151 EipEGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQA 199
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
222-422 1.21e-18

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: 86.60  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLrkQDKDNTMNVIHMLENFTFRN--HICM 299
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVKFYGMYYKKDVKNgdQLWL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKNKFQG--FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY-- 374
Cdd:cd06638   98 VLELCNGgSVTDLVKGFLKRGerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG--GVKLVDFGVSAQlt 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 375 -EHQRVYTYIQSRFYRAPEVI-----LGARYGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd06638  176 sTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPL 229
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
226-431 1.21e-18

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: 87.06  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKrfhrqaaeeirILEhlrKQDKDNTM-------------NVIHMLENFT 292
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDV-----------VLE---DDDVECTMierrvlalasqhpFLTHLFCTFQ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLsmNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS 371
Cdd:cd05592   67 TESHLFFVMEYL--NGGDLMFHIQQSGrFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH--IKIADFGM 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 372 sCYEhqRVYTYIQ-SRF-----YRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEgDQL 431
Cdd:cd05592  143 -CKE--NIYGENKaSTFcgtpdYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDE-DEL 204
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
222-417 1.24e-18

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 85.94  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVV---KAYDHK--VHQHVALKmvRNEKRFHRQAAEEIRILEHLrkqdkdNTMNVIhmlenfTFRNH 296
Cdd:cd08221    2 YIPVRVLGRGAFGEAVlyrKTEDNSlvVWKEVNLS--RLSEKERRDALNEIDILSLL------NHDNII------TYYNH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 -ICMTFELLSM------NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd08221   68 fLDGESLFIEMeycnggNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADL--VKLGDF 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 370 GSSCY---EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08221  146 GISKVldsESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLT 196
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
218-458 1.28e-18

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: 86.20  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQ--AAEEIRILEHLRKQdkdntmNVIHMLENFTFRN 295
Cdd:cd14183    4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmIQNEVSILRRVKHP------NIVLLIEEMDMPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIKK-NKFQGFSlplVRKFAHSILQCLDALHKNRIIHCDLKPENILL--KQQGRSGIKVIDFGS 371
Cdd:cd14183   78 ELYLVMELVKGgDLFDAITStNKYTERD---ASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSKSLKLGDFGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEgDQLACMIELL----GMPSQKLLD 447
Cdd:cd14183  155 ATVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGD-DQEVLFDQILmgqvDFPSPYWDN 233
                        250
                 ....*....|.
gi 153281169 448 ASKRAKNFVSS 458
Cdd:cd14183  234 VSDSAKELITM 244
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
222-533 1.41e-18

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: 85.82  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR----NEKRFHRQaaeEIRILEHLRKQdkdntmNVIHMLENFtFRNH- 296
Cdd:cd06613    2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKlepgDDFEIIQQ---EISMLKECRHP------NIVAYFGSY-LRRDk 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 --ICMTF-ELLSM-NLYELIKKnkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSS 372
Cdd:cd06613   72 lwIVMEYcGGGSLqDIYQVTGP-----LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDG--DVKLADFGVS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 C---YEHQRVYTYIQSRFYRAPEVILGAR---YGMPIDMWSLGCILAELLTGYPllPgedegdqlacMIELLGMpsqkll 446
Cdd:cd06613  145 AqltATIAKRKSFIGTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAELQP--P----------MFDLHPM------ 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 daskRAKNFVSSKGYPryctvttlsdgsvvlnggrsrrgklrgPP---ESREWgnalkgcdDPLFLDFLKQCLEWDPAVR 523
Cdd:cd06613  207 ----RALFLIPKSNFD---------------------------PPklkDKEKW--------SPDFHDFIKKCLTKNPKKR 247
                        330
                 ....*....|
gi 153281169 524 MTPGQALRHP 533
Cdd:cd06613  248 PTATKLLQHP 257
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
222-546 1.96e-18

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 85.85  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAEeIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd06643    7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIdtKSEEELEDYMVE-IDILASCDHP------NIVKLLDAFYYENNLWI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCYEH--- 376
Cdd:cd06643   80 LIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG--DIKLADFGVSAKNTrtl 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGAR-----YGMPIDMWSLGCILAELLTGYPllpgedegdqlacmiellgmPSQKlldaskr 451
Cdd:cd06643  158 QRRDSFIGTPYWMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQIEP--------------------PHHE------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 452 aknfvsskgypryctvttLSDGSVVLNGGRSRRGKLRGPpeSReWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd06643  211 ------------------LNPMRVLLKIAKSEPPTLAQP--SR-W--------SPEFKDFLRKCLEKNVDARWTTSQLLQ 261
                        330
                 ....*....|....*
gi 153281169 532 HPWLRRRLPKPPTGE 546
Cdd:cd06643  262 HPFVSVLVSNKPLRE 276
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
226-418 1.98e-18

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: 86.20  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFhrQAAEEIRILEHLRkqdkdNTMNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd14092   12 EALGDGSFSVCRKCVHKKTGQEFAVKIV--SRRL--DTSREVQLLRLCQ-----GHPNIVKLHEVFQDELHTYLVMELLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MN-LYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDFGSSCY--EHQRVYT 381
Cdd:cd14092   83 GGeLLERIRKKK--RFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAeIKIVDFGFARLkpENQPLKT 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 382 YIQSRFYRAPEVILGAR----YGMPIDMWSLGCILAELLTG 418
Cdd:cd14092  161 PCFTLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSG 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
222-418 2.00e-18

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: 86.90  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVV---KAYDHKVHQHVALKMVRNEKRFHR-QAAEEIR----ILEHLRKQDkdnTMNVIHMLENFTF 293
Cdd:cd05614    2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMKVLRKAALVQKaKTVEHTRternVLEHVRQSP---FLVTLHYAFQTDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTF----ELLSmNLYELikknkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd05614   79 KLHLILDYvsggELFT-HLYQR------DHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH--VVLTDF 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 370 GSS----CYEHQRVYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05614  150 GLSkeflTEEKERTYSFCGTIEYMAPEIIRGkSGHGKAVDWWSLGILMFELLTG 203
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
226-427 2.00e-18

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: 86.52  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRIL----EHlrkqdkdntMNVIHMLENFTFRNHI 297
Cdd:cd05619   11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVEctmvEKRVLslawEH---------PFLTHLFCTFQTKENL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMN--LYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYE 375
Cdd:cd05619   82 FFVMEYLNGGdlMFHIQSCHKF---DLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH--IKIADFGM-CKE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 376 H----QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDE 427
Cdd:cd05619  156 NmlgdAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDE 211
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
222-425 2.11e-18

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: 85.54  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHR----QAAEEIRILEHlrkqdKDNTMnVIHMLENFTFRNHI 297
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRnqiqQVFVERDILTF-----AENPF-VVSMYCSFETKRHL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNkfqGFSLP--LVRK-FAHSILqCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS-- 372
Cdd:cd05609   76 CMVMEYVEGGDCATLLKN---IGPLPvdMARMyFAETVL-ALEYLHSYGIVHRDLKPDNLLITSMGH--IKLTDFGLSki 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 373 --------CYEH------------QRVYT--YIqsrfyrAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGE 425
Cdd:cd05609  150 glmslttnLYEGhiekdtrefldkQVCGTpeYI------APEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD 218
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
221-557 2.44e-18

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: 85.93  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKmvrnEKRFHRQAAEEIRILEHLRKQDKDNTmNVIHMLENFTFRNHICMT 300
Cdd:cd06654   21 KYTRFEKIGQGASGTVYTAMDVATGQEVAIR----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY---EH 376
Cdd:cd06654   96 MEYLAGgSLTDVVTETCMDEGQIAAV---CRECLQALEFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDegdqlacmiellgmpsqklldaSKRAKNFV 456
Cdd:cd06654  171 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN----------------------PLRALYLI 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 457 SSKGYPRYCTVTTLSdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTPGQALRHPWLr 536
Cdd:cd06654  229 ATNGTPELQNPEKLS----------------------------------AIFRDFLNRCLEMDVEKRGSAKELLQHQFL- 273
                        330       340
                 ....*....|....*....|.
gi 153281169 537 rRLPKPPTGEKTSVKRITEST 557
Cdd:cd06654  274 -KIAKPLSSLTPLIAAAKEAT 293
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
222-535 2.44e-18

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: 85.23  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK-RFHR------QAAEEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRsKASRrgvsreDIEREVSILRQVLHP------NIITLHDVFENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL--KQQGRSGIKVIDFG- 370
Cdd:cd14105   81 TDVVLILELVAGgELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldKNVPIPRIKLIDFGl 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEHQRVYTYI-QSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACmiellgmpsqklldas 449
Cdd:cd14105  159 AHKIEDGNEFKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAN---------------- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 450 kraknfVSSKGYP---RYCTVTTlsdgsvvlnggrsrrgklrgppesrewgnalkgcddPLFLDFLKQCLEWDPAVRMTP 526
Cdd:cd14105  223 ------ITAVNYDfddEYFSNTS------------------------------------ELAKDFIRQLLVKDPRKRMTI 260

                 ....*....
gi 153281169 527 GQALRHPWL 535
Cdd:cd14105  261 QESLRHPWI 269
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
221-535 2.50e-18

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 84.94  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd14114    3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRkEIQIMNQLHHP------KLINLHDAFEDDNEMVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCY--EH 376
Cdd:cd14114   77 ILEFLSGgELFERIAAEHYK-MSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHldPK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLAcmiellgmpSQKLLDASKRAKNFv 456
Cdd:cd14114  156 ESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLR---------NVKSCDWNFDDSAF- 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 457 sskgypryctvttlsdgsvvlnGGRSRRGKlrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14114  226 ----------------------SGISEEAK-----------------------DFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
222-535 3.47e-18

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: 84.66  E-value: 3.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLK-VIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQaaeeirILEHLRKQDKDNTMNVIHMLENFtFRNHICMT 300
Cdd:cd14172    5 YKLSKqVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARRE------VEHHWRASGGPHIVHILDVYENM-HHGKRCLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM---NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGI-KVIDFGSS--CY 374
Cdd:cd14172   78 IIMECMeggELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVlKLTDFGFAkeTT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllpgedegdqlacmiellgmpsqklldaskrakN 454
Cdd:cd14172  158 VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFP---------------------------------P 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 FVSSKGypryctvTTLSDGSvvlnGGRSRRGKLRGP-PESREWGNALKgcddplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14172  205 FYSNTG-------QAISPGM----KRRIRMGQYGFPnPEWAEVSEEAK--------QLIRHLLKTDPTERMTITQFMNHP 265

                 ..
gi 153281169 534 WL 535
Cdd:cd14172  266 WI 267
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
222-416 3.48e-18

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: 85.04  E-value: 3.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRnekrFHRQAAEEIRILEHLRKQDKDNTMNVIHMleNFTFRNHICMtf 301
Cdd:cd13996    8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR----LTEKSSASEKVLREVKALAKLNHPNIVRY--YTAWVEEPPL-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 eLLSMNLYE-------LIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkQQGRSGIKVIDFGSSCY 374
Cdd:cd13996   80 -YIQMELCEggtlrdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL-DNDDLQVKIGDFGLATS 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 375 EHQ-------------RVYTYIQSR----FYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd13996  158 IGNqkrelnnlnnnnnGNTSNNSVGigtpLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
226-420 3.88e-18

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: 85.83  E-value: 3.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAyDHKVHQHV-ALK-------MVRNEKRfHRQAAEEIrilehLRKqdkdntmNVIHMLE---NFTFR 294
Cdd:cd05575    1 KVIGKGSFGKVLLA-RHKAEGKLyAVKvlqkkaiLKRNEVK-HIMAERNV-----LLK-------NVKHPFLvglHYSFQ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNLYEL---IKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGs 371
Cdd:cd05575   67 TKDKLYFVLDYVNGGELffhLQRERH--FPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGH--VVLTDFG- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 372 SCYEHQR----VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05575  142 LCKEGIEpsdtTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLP 194
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
228-418 3.91e-18

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: 84.89  E-value: 3.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAEEIRILEhlrKQ--DKDNTMNVIHMLENFTFRNHICMTFELls 305
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKL-DKKRIKKKKGETMALNE---KIilEKVSSPFIVSLAYAFETKDKLCLVLTL-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLYEL---IKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY--EHQRVY 380
Cdd:cd05577   75 MNGGDLkyhIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH--VRISDLGLAVEfkGGKKIK 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153281169 381 TYIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTG 418
Cdd:cd05577  153 GRVGTHGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIAG 191
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
218-456 3.95e-18

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: 84.77  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLK-----VIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAA---EEIRILEHLRKQdkdntmNVIHMLE 289
Cdd:cd06624    1 LEYEYEYDEsgervVLGKGTFGVVYAARDLSTQVRIAIKEI--PERDSREVQplhEEIALHSRLSHK------NIVQYLG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 290 NFTFRNHICMTFELL-SMNLYELIKkNKFQgfslPLVRK------FAHSILQCLDALHKNRIIHCDLKPENILLKQQgrS 362
Cdd:cd06624   73 SVSEDGFFKIFMEQVpGGSLSALLR-SKWG----PLKDNentigyYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--S 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 363 G-IKVIDFGSS--------CYEhqrvyTYIQSRFYRAPEVI-LGAR-YGMPIDMWSLGCILAELLTGYPllPGEDEGDQL 431
Cdd:cd06624  146 GvVKISDFGTSkrlaginpCTE-----TFTGTLQYMAPEVIdKGQRgYGPPADIWSLGCTIIEMATGKP--PFIELGEPQ 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 153281169 432 ACMIElLGM-------PSQklldASKRAKNFV 456
Cdd:cd06624  219 AAMFK-VGMfkihpeiPES----LSEEAKSFI 245
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
225-420 4.54e-18

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 85.40  E-value: 4.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEH-LRKQDKDNTMNVIHmlenFTFRNHICMTFEL 303
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNvLLKNVKHPFLVGLH----YSFQTTDKLYFVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSMNLYELI-KKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGsSCYE----HQR 378
Cdd:cd05604   77 DFVNGGELFfHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH--IVLTDFG-LCKEgisnSDT 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153281169 379 VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05604  154 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLP 195
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
228-418 4.86e-18

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: 83.96  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKA-YDHKVHQHVALKMVRNEKRFHRQA--AEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELL 304
Cdd:cd14120    1 IGHGAFAVVFKGrHRKKPDLPVAIKCITKKNLSKSQNllGKEIKILKELSHE------NVVALLDCQETSSSVYLVMEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 S---MNLYELIKKNkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-------IKVIDFGSSCY 374
Cdd:cd14120   75 NggdLADYLQAKGT----LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKpspndirLKIADFGFARF 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153281169 375 EHQRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14120  151 LQDGMMaaTLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTG 196
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
222-441 5.60e-18

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 84.31  E-value: 5.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR----NEKRFHRQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHI 297
Cdd:cd08228    4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemMDAKARQDCVKEIDLLKQL------NHPNVIKYLDSFIEDNEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 374
Cdd:cd08228   78 NIVLELADAgDLSQMIKYFKKQKRLIPerTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV--VKLGDLGLGRF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 ---EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT----------------------GYPLLPGEDEGD 429
Cdd:cd08228  156 fssKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAAlqspfygdkmnlfslcqkieqcDYPPLPTEHYSE 235
                        250
                 ....*....|..
gi 153281169 430 QLACMIELLGMP 441
Cdd:cd08228  236 KLRELVSMCIYP 247
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
220-420 7.62e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 83.90  E-value: 7.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVIGKGSFGQVVKA-YDHKVHQHVALKMVrNEKRFHRQA---AEEIRILEHLRKQdkdntmNVIHMLENFTFRN 295
Cdd:cd14201    6 FEYSRKDLVGHGAFAVVFKGrHRKKTDWEVAIKSI-NKKNLSKSQillGKEIKILKELQHE------NIVALYDVQEMPN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLsmNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-----SG--IKVI 367
Cdd:cd14201   79 SVFLVMEYC--NGGDLADYLQAKGtLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvSGirIKIA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 368 DFGSSCYEHQRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14201  157 DFGFARYLQSNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKP 211
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
222-546 8.65e-18

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: 83.93  E-value: 8.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAEeIRILEHLrkqdkdNTMNVIHMLENFTFRNHICM 299
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIetKSEEELEDYMVE-IEILATC------NHPYIVKLLGAFYWDGKLWI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH--- 376
Cdd:cd06644   87 MIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD--IKLADFGVSAKNVktl 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVIL-----GARYGMPIDMWSLGCILAELltgypllpgedegdqlaCMIEllgmPSQKLLDASKr 451
Cdd:cd06644  165 QRRDSFIGTPYWMAPEVVMcetmkDTPYDYKADIWSLGITLIEM-----------------AQIE----PPHHELNPMR- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 452 aknfvsskgypryctvttlsdgsVVLNGGRSRRGKLRGPpesREWgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALR 531
Cdd:cd06644  223 -----------------------VLLKIAKSEPPTLSQP---SKW--------SMEFRDFLKTALDKHPETRPSAAQLLE 268
                        330
                 ....*....|....*
gi 153281169 532 HPWLRRRLPKPPTGE 546
Cdd:cd06644  269 HPFVSSVTSNRPLRE 283
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
222-456 9.85e-18

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 83.49  E-value: 9.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFgQVVKAYDHKVHQH-VALKMVrNEKRFHR-QAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICM 299
Cdd:cd14113    9 YSEVAELGRGRF-SVVKKCDQRGTKRaVATKFV-NKKLMKRdQVTHELGVLQSLQHP------QLVGLLDTFETPTSYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMN-LYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQ-GRSGIKVIDFG------S 371
Cdd:cd14113   81 VLEMADQGrLLDYVVR--WGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSlSKPTIKLADFGdavqlnT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SCYEHQrvytYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLpgeDEGDQLACM-IELL--GMPSQKLLD 447
Cdd:cd14113  159 TYYIHQ----LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVsPFL---DESVEETCLnICRLdfSFPDDYFKG 231

                 ....*....
gi 153281169 448 ASKRAKNFV 456
Cdd:cd14113  232 VSQKAKDFV 240
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
221-457 1.03e-17

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: 83.16  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQ--AAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd14184    2 KYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhlIENEVSILRRVKHP------NIIMLIEEMDTPAELY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQ--QGRSGIKVIDFGSSCYE 375
Cdd:cd14184   76 LVMELVKGgDLFDAITSST--KYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypDGTKSLKLGDFGLATVV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPG-----EDEGDQLacMIELLGMPSQKLLDASK 450
Cdd:cd14184  154 EGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSennlqEDLFDQI--LLGKLEFPSPYWDNITD 231

                 ....*..
gi 153281169 451 RAKNFVS 457
Cdd:cd14184  232 SAKELIS 238
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
222-420 1.04e-17

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 85.47  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQaaeEIRileHLRkQDKD---NTMNV--IHMLENFTFRNH 296
Cdd:cd05600   13 FQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLN---EVN---HVL-TERDiltTTNSPwlVKLLYAFQDPEN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 IcmtfeLLSMnlyELIKKNKFQGFSLPL-------VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd05600   86 V-----YLAM---EYVPGGDFRTLLNNSgilseehARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGH--IKLTDF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 370 GSSC----YEH--------QRVYTYIQSRF----------------------------YRAPEVILGARYGMPIDMWSLG 409
Cdd:cd05600  156 GLASgtlsPKKiesmkirlEEVKNTAFLELtakerrniyramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLG 235
                        250
                 ....*....|.
gi 153281169 410 CILAELLTGYP 420
Cdd:cd05600  236 CILFECLVGFP 246
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
221-427 1.06e-17

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: 83.20  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK------RFHRqaaeEIRILEHLRKQdkdNTMNVIHMLENftfR 294
Cdd:cd14078    4 YYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgddlpRVKT----EIEALKNLSHQ---HICRLYHVIET---D 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLS-MNLYELI-KKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG-- 370
Cdd:cd14078   74 NKIFMVLEYCPgGELFDYIvAKDRL---SEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDED--QNLKLIDFGlc 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 371 ---SSCYEHQrVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGYplLPGEDE 427
Cdd:cd14078  149 akpKGGMDHH-LETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGF--LPFDDD 206
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
222-418 1.32e-17

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 82.83  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGqVVKAYDHKVHQ-HVALKMV-------RNEKRFHRqaaeEIRILEHLRKQ------DKDNTMNVIHM 287
Cdd:cd14071    2 YDIERTIGKGNFA-VVKLARHRITKtEVAIKIIdksqldeENLKKIYR----EVQIMKMLNHPhiiklyQVMETKDMLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 288 LENFTFRNHIcmtFELLSMN--LYELIKKNKFQgfslplvrkfahSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIK 365
Cdd:cd14071   77 VTEYASNGEI---FDYLAQHgrMSEKEARKKFW------------QILSAVEYCHKRHIVHRDLKAENLLL--DANMNIK 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 366 VIDFGSSCY--EHQRVYTYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTG 418
Cdd:cd14071  140 IADFGFSNFfkPGELLKTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCG 195
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
222-429 1.38e-17

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 82.85  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGqVVKAYDHKVH-QHVALKMVRNEKR---FHRQAAEEIR---ILEHlrkqdkdntMNVIHMLENFTFR 294
Cdd:cd14074    5 YDLEETLGRGHFA-VVKLARHVFTgEKVAVKVIDKTKLddvSKAHLFQEVRcmkLVQH---------PNVVRLYEVIDTQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSM-NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-KQQGRsgIKVIDFG-S 371
Cdd:cd14074   75 TKLYLILELGDGgDMYDYIMKHE-NGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGL--VKLTDFGfS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SCYEH-QRVYTYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTGYPllPGEDEGD 429
Cdd:cd14074  152 NKFQPgEKLETSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILYMLVCGQP--PFQEAND 209
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
222-420 1.55e-17

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 84.30  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEIRILEH---LRKQDKDNTMNVIHmlenFTFRNHIC 298
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVL--QKKAILKKKEEKHIMSErnvLLKNVKHPFLVGLH----FSFQTTDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKK-NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGsSCYE-- 375
Cdd:cd05602   83 LYFVLDYINGGELFYHlQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH--IVLTDFG-LCKEni 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 376 --HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05602  160 epNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLP 206
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
226-433 1.55e-17

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 83.55  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEIRILEHLrkqdkDNTMNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIV--SKRMEANTQREIAALKLC-----EGHPNIVKLHEVYHDQLHTFLVMELLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 M-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQG-RSGIKVIDFGSSCY---EHQRVY 380
Cdd:cd14179   86 GgELLERIKKKQH--FSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdNSEIKIIDFGFARLkppDNQPLK 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYplLPGEDEGDQLAC 433
Cdd:cd14179  164 TPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQ--VPFQCHDKSLTC 214
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
225-426 1.90e-17

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: 83.61  E-value: 1.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFG---QVVKAYDHKVHQHVALK------MVRNEK-RFHRQAaeEIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd05584    1 LKVLGKGGYGkvfQVRKTTGSDKGKIFAMKvlkkasIVRNQKdTAHTKA--ERNILEAVKHP------FIVDLHYAFQTG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSMNlyELIKKNKFQGFSLPLVRKFAHS-ILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG--- 370
Cdd:cd05584   73 GKLYLILEYLSGG--ELFMHLEREGIFMEDTACFYLAeITLALGHLHSLGIIYRDLKPENILLDAQGH--VKLTDFGlck 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 371 SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:cd05584  149 ESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAEN 204
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
222-436 2.01e-17

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: 83.89  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEhlrKQDKDNTMNVIHMLENFTFRNHI 297
Cdd:cd05615   12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVEctmvEKRVLA---LQDKPPFLTQLHSCFQTVDRLYF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYEHQ 377
Cdd:cd05615   89 VMEYVNGGDLMYHIQQVGKFKE---PQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH--IKIADFGM-CKEHM 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 378 ----RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIE 436
Cdd:cd05615  163 vegvTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIME 225
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
228-458 2.02e-17

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: 81.93  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS-- 305
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP------QYITLHDTYESPTSYILVLELMDdg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 ------MNLYELIKKNkfqgfslplVRKFAHSILQCLDALHKNRIIHCDLKPENILLK-QQGRSGIKVIDFGSSCY--EH 376
Cdd:cd14115   75 rlldylMNHDELMEEK---------VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIPVPRVKLIDLEDAVQisGH 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGypLLPGEDEGDQLACMIEL---LGMPSQKLLDASKRAK 453
Cdd:cd14115  146 RHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSG--VSPFLDESKEETCINVCrvdFSFPDEYFGDVSQAAR 223

                 ....*
gi 153281169 454 NFVSS 458
Cdd:cd14115  224 DFINV 228
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
222-420 2.28e-17

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: 83.52  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHR-QAAE---EIRILehlrkQDKDNTMnVIHMLenFTFRNHI 297
Cdd:cd05598    3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRnQVAHvkaERDIL-----AEADNEW-VVKLY--YSFQDKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTF--------ELLSMnlyeLIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd05598   75 NLYFvmdyipggDLMSL----LIKKGIFEE---DLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGH--IKLTDF 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 370 GSsC----YEHQRVYTYIQSRF----YRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05598  146 GL-CtgfrWTHDSKYYLAHSLVgtpnYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQP 203
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
226-465 2.39e-17

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: 82.38  E-value: 2.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE------EIRILEHLRKqdkDNTMNVIHMLENFTFRNHICM 299
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEvnalecEIQLLKNLRH---DRIVQYYGCLRDPEEKKLSIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKnkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS------C 373
Cdd:cd06653   85 VEYMPGGSVKDQLKA--YGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGN--VKLGDFGASkriqtiC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPgedEGDQLACMIELLGMPSQKLL--DASKR 451
Cdd:cd06653  161 MSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATQPTKPQLpdGVSDA 237
                        250
                 ....*....|....*....
gi 153281169 452 AKN-----FVSSKGYPRYC 465
Cdd:cd06653  238 CRDflrqiFVEEKRRPTAE 256
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
227-427 2.50e-17

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: 83.00  E-value: 2.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRqaAEEIRILEHLRKQDKDNTMNVIHMleNFTFRNHICMTFELLSM 306
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSR--SEVTHTLAERTVLAQVDCPFIVPL--KFSFQSPEKLYLVLAFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS---SCYEHQRVYTY 382
Cdd:cd05585   77 NGGELFHHLQREGrFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH--IALCDFGLcklNMKDDDKTNTF 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 383 IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDE 427
Cdd:cd05585  155 CGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLP--PFYDE 197
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
216-559 2.62e-17

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: 82.79  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA--EEIRILEHLRKQdkdntmNVIHMLENFTF 293
Cdd:cd14168    6 EDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSieNEIAVLRKIKHE------NIVALEDIYES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSMNlyELIKKNKFQGFslpLVRKFAHSIL-QCLDA---LHKNRIIHCDLKPENIL-LKQQGRSGIKVID 368
Cdd:cd14168   80 PNHLYLVMQLVSGG--ELFDRIVEKGF---YTEKDASTLIrQVLDAvyyLHRMGIVHRDLKPENLLyFSQDEESKIMISD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSCYEHQR--VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDqlacmiellgmpsQKLL 446
Cdd:cd14168  155 FGLSKMEGKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP--PFYDEND-------------SKLF 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 DASKRAKNFVSSKGYpryctvTTLSDGSVvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTP 526
Cdd:cd14168  220 EQILKADYEFDSPYW------DDISDSAK----------------------------------DFIRNLMEKDPNKRYTC 259
                        330       340       350
                 ....*....|....*....|....*....|...
gi 153281169 527 GQALRHPWLrrrlpkppTGEKTSVKRITESTGA 559
Cdd:cd14168  260 EQALRHPWI--------AGDTALCKNIHESVSA 284
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
228-423 2.84e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 82.70  E-value: 2.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNE--KRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNhicmtFELLS 305
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQElsPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLAPND-----LPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLYE--LIKK--NKFQ---GFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkQQGRSGI--KVIDFGSSCYEH 376
Cdd:cd14038   77 MEYCQggDLRKylNQFEnccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGEQRLihKIIDLGYAKELD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QR--VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLP 423
Cdd:cd14038  156 QGslCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFrPFLP 205
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
225-458 3.39e-17

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 81.83  E-value: 3.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIgKGSFGQVvKAYDHKVHQHVALKMVRNEKRFHrqaAEEIRIlEHLRKQDKdntmNVIHMLENFTFRNHIcmtfeLL 304
Cdd:PHA03390  22 LKLI-DGKFGKV-SVLKHKPTQKLFVQKIIKAKNFN---AIEPMV-HQLMKDNP----NFIKLYYSVTTLKGH-----VL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SM------NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL---LKQQgrsgIKVIDFG----- 370
Cdd:PHA03390  87 IMdyikdgDLFDLLKKEGK--LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLydrAKDR----IYLCDYGlckii 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 --SSCYEHQRVYtyiqsrFyrAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEDEGDQLACMIELLGMPSQKLLD 447
Cdd:PHA03390 161 gtPSCYDGTLDY------F--SPEKIKGHNYDVSFDWWAVGVLTYELLTGkHPFKEDEDEELDLESLLKRQQKKLPFIKN 232
                        250
                 ....*....|.
gi 153281169 448 ASKRAKNFVSS 458
Cdd:PHA03390 233 VSKNANDFVQS 243
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
226-418 3.82e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 81.96  E-value: 3.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRnEKRFHRQAAE-----EIRILEhlrkqdKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd05631    6 RVLGKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRKGEamalnEKRILE------KVNSRFVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FEL-----LSMNLYELIKKnkfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY- 374
Cdd:cd05631   79 LTImnggdLKFHIYNMGNP----GFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGH--IRISDLGLAVQi 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 375 -EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05631  153 pEGETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQG 197
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
222-427 4.49e-17

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: 82.35  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLrkqdkdNTMN---VIHMLENFTFR 294
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVEslmcEKRIFETV------NSARhpfLVNLFACFQTP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFEL-----LSMNLYELIkknkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd05589   75 EHVCFVMEYaaggdLMMHIHEDV-------FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIADF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 370 GSsCYEH----QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDE 427
Cdd:cd05589  146 GL-CKEGmgfgDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDE 206
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
221-415 4.54e-17

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


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 81.32  E-value: 4.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK--RFHRQAAE-EIRILEHLrkqdkdNTMNVIHMLENFTFRNHI 297
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQmtKEERQAALnEVKVLSML------HHPNIIEYYESFLEDKAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFGSS--CY 374
Cdd:cd08220   75 MIVMEYAPGgTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKK-RTVVKIGDFGISkiLS 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAEL 415
Cdd:cd08220  154 SKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
320-418 5.17e-17

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: 81.29  E-value: 5.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 320 FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS----CYEHQRVYTYIQSRFYRAPEVIL 395
Cdd:cd05583   96 FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGH--VVLTDFGLSkeflPGENDRAYSFCGTIEYMAPEVVR 173
                         90       100
                 ....*....|....*....|....*
gi 153281169 396 GARYG--MPIDMWSLGCILAELLTG 418
Cdd:cd05583  174 GGSDGhdKAVDWWSLGVLTYELLTG 198
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
222-418 5.26e-17

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: 81.02  E-value: 5.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNekrfhRQAAEEIRILEHLRKQDKDNTM----NVIHMLENFTFRNHI 297
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDK-----KKAKKDSYVTKNLRREGRIQQMirhpNITQLLDILETENSY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFEL-LSMNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG-SSCYE 375
Cdd:cd14070   79 YLVMELcPGGNLMHRIYDKK--RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEN--DNIKLIDFGlSNCAG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 376 ----HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14070  155 ilgySDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTG 201
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
221-420 5.40e-17

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: 81.50  E-value: 5.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGsFGQVVKAYDHK-VHQHVALKM--VRNEKRFHRQAAEEIR--------ILEHLRKQDkdntmNVIHMLE 289
Cdd:cd14182    4 KYEPKEILGRG-VSSVVRRCIHKpTRQEYAVKIidITGGGSFSPEEVQELReatlkeidILRKVSGHP-----NIIQLKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 290 NFTFRNHICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVID 368
Cdd:cd14182   78 TYETNTFFFLVFDLMKKgELFDYLTEK--VTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDD--MNIKLTD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSC--YEHQRVYTYIQSRFYRAPEVILGAR------YGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14182  154 FGFSCqlDPGEKLREVCGTPGYLAPEIIECSMddnhpgYGKEVDMWSTGVIMYTLLAGSP 213
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
226-420 5.75e-17

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: 81.32  E-value: 5.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMV---RNEKRFHRQAAE----EIRILEHLrkqdkdNTMNVIHMLENFTFRNHIC 298
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVsfcRNSSSEQEEVVEaireEIRMMARL------NHPNIVRMLGATQHKSHFN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKKnKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSCyehqR 378
Cdd:cd06630   80 IFVEWMAGGSVASLLS-KYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQR-LRIADFGAAA----R 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 379 VYTYI------QSRF-----YRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd06630  154 LASKGtgagefQGQLlgtiaFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKP 206
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
228-427 5.97e-17

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: 81.25  E-value: 5.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAA-------------------------EEIRILehlRKQDKDNTM 282
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKIL-SKKKLLKQAGffrrppprrkpgalgkpldpldrvyREIAIL---KKLDHPNVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 283 NVIHMLENfTFRNHICMTFELLSMN-LYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR 361
Cdd:cd14118   78 KLVEVLDD-PNEDNLYMVFELVDKGaVMEVPTDNPL---SEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 362 sgIKVIDFGSSCYEH---QRVYTYIQSRFYRAPEVILGARY---GMPIDMWSLGCILAELLTGYplLPGEDE 427
Cdd:cd14118  154 --VKIADFGVSNEFEgddALLSSTAGTPAFMAPEALSESRKkfsGKALDIWAMGVTLYCFVFGR--CPFEDD 221
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
222-426 6.30e-17

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: 81.37  E-value: 6.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQDKDNTMnvihmlenftfRNHICM 299
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNldTDDDDVSDIQKEVALLSQLKLGQPKNII-----------KYYGSY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 tfeLLSMNLYelIKKNKFQGFSL-------PLVRKFAHSI----LQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd06917   72 ---LKGPSLW--IIMDYCEGGSIrtlmragPIAERYIAVImrevLVALKFIHKDGIIHRDIKAANILVTNTGN--VKLCD 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 369 FGSSCYEHQ---RVYTYIQSRFYRAPEVIL-GARYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:cd06917  145 FGVAASLNQnssKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSDVD 206
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
225-426 6.61e-17

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: 81.25  E-value: 6.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfhrQAAEEIR-ILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd06640    9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIDLE-----EAEDEIEdIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSM-NLYELIKKNKFQGFSLPLVRKfahSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY---EHQRV 379
Cdd:cd06640   84 LGGgSALDLLRAGPFDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGD--VKLADFGVAGQltdTQIKR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGED 426
Cdd:cd06640  159 NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEP--PNSD 203
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
228-418 7.16e-17

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 80.78  E-value: 7.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKvHQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELL- 304
Cdd:cd14066    1 IGSGGFGTVYKGVLEN-GTVVAVKRLNemNCAASKKEFLTELEMLGRLRHP------NLVRLLGYCLESDEKLLVYEYMp 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SMNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALH---KNRIIHCDLKPENILLKQQGRSgiKVIDFGSSCYEHQRVY 380
Cdd:cd14066   74 NGSLEDRLHCHKGSPpLPWPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEP--KLTDFGLARLIPPSES 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 381 TYIQSRF-----YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14066  152 VSKTSAVkgtigYLAPEYIRTGRVSTKSDVYSFGVVLLELLTG 194
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
216-432 7.47e-17

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: 80.83  E-value: 7.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAE-----EIRILEHLRKQdkdntmNVIHML 288
Cdd:cd14194    1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIkkRRTKSSRRGVSRedierEVSILKEIQHP------NVITLH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 289 ENFTFRNHICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL--KQQGRSGIK 365
Cdd:cd14194   75 EVYENKTDVILILELVAGgELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldRNVPKPRIK 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 366 VIDFG-----SSCYEHQRVYTYIQsrfYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLA 432
Cdd:cd14194  153 IIDFGlahkiDFGNEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLA 221
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
222-422 7.51e-17

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: 81.19  E-value: 7.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLrkqdkDNTMNVIHMLENFTFRNH----- 296
Cdd:cd06639   24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSL-----PNHPNVVKFYGMFYKADQyvggq 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSM-NLYELIKKNKFQGFSL--PLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSC 373
Cdd:cd06639   99 LWLVLELCNGgSVTELVKGLLKCGQRLdeAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGVSA 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 374 Y---EHQRVYTYIQSRFYRAPEVILGAR-----YGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd06639  177 QltsARLRRNTSVGTPFWMAPEVIACEQqydysYDARCDVWSLGITAIELADGDPPL 233
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
225-436 7.83e-17

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 81.67  E-value: 7.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEhlrKQDKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVEctmvEKRVLA---LSGKPPFLTQLHSCFQTMDRLYFVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FellsMN----LYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYEH 376
Cdd:cd05587   78 Y----VNggdlMYHIQQVGKFKE---PVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH--IKIADFGM-CKEG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 377 ----QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIE 436
Cdd:cd05587  148 ifggKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIME 211
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
226-535 8.17e-17

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: 80.73  E-value: 8.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA-EEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMTFELL 304
Cdd:cd14190   10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVlLEIQVMNQL------NHRNLIQLYEAIETPNEIVLFMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SMNlyELIKKNKFQGFSLPLVRK--FAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFG-SSCYE-HQRVY 380
Cdd:cd14190   84 EGG--ELFERIVDEDYHLTEVDAmvFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGlARRYNpREKLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLacmiellgmpsqklldaskraKNFVSSKG 460
Cdd:cd14190  162 VNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETL---------------------NNVLMGNW 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 461 YPRYCTVTTLSDgsvvlnggrsrrgklrgppESRewgnalkgcddplflDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14190  221 YFDEETFEHVSD-------------------EAK---------------DFVSNLIIKERSARMSATQCLKHPWL 261
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
220-418 8.62e-17

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: 80.83  E-value: 8.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVIGKGSFGQVVKAYDHKVHQ-HVALKMV--RNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNH 296
Cdd:cd14202    2 FEFSRKDLIGHGAFAVVFKGRHKEKHDlEVAVKCInkKNLAKSQTLLGKEIKILKELKHE------NIVALYDFQEIANS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSM-NLYELIkkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLK-QQGRSG------IKVID 368
Cdd:cd14202   76 VYLVMEYCNGgDLADYL--HTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSySGGRKSnpnnirIKIAD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 369 FGSSCYEHQRVY--TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14202  154 FGFARYLQNNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTG 205
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
222-458 1.22e-16

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: 80.05  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrneKRFHRQAAEEIRilehlrkqDKDNTMNVIH------MLENFTFRN 295
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF---KAYSAKEKENIR--------QEISIMNCLHhpklvqCVDAFEEKA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSS-- 372
Cdd:cd14191   73 NIVMVLEMVSGgELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLArr 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELL-GMPSQKLLDASKR 451
Cdd:cd14191  152 LENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwDFDDEAFDEISDD 231

                 ....*..
gi 153281169 452 AKNFVSS 458
Cdd:cd14191  232 AKDFISN 238
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
222-474 1.25e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 81.96  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRnekrfhRQA-AEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMT 300
Cdd:PHA03212  94 FSILETFTPGAEGFAFACIDNKTCEHVVIKAGQ------RGGtATEAHILRAI------NHPSIIQLKGTFTYNKFTCLI 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKfqgfSLPLVRKFA--HSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY---- 374
Cdd:PHA03212 162 LPRYKTDLYCYLAAKR----NIAICDILAieRSVLRAIQYLHENRIIHRDIKAENIFINHPG--DVCLGDFGAACFpvdi 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGED--EGD-----QLACMIELLGM-PSQKLL 446
Cdd:PHA03212 236 NANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKDglDGDcdsdrQIKLIIRRSGThPNEFPI 315
                        250       260
                 ....*....|....*....|....*...
gi 153281169 447 DASKRAKnfvssKGYPRYCTVTTLSDGS 474
Cdd:PHA03212 316 DAQANLD-----EIYIGLAKKSSRKPGS 338
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
222-456 1.88e-16

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: 79.56  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHK------SIVRFHDAFEKRRVVIIVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQGFSLplVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSS--CYEHQRV 379
Cdd:cd14108   78 ELCHEELLERITKRPTVCESE--VRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAqeLTPNEPQ 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL-LGMPSQKLLDASKRAKNFV 456
Cdd:cd14108  156 YCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYnVAFEESMFKDLCREAKGFI 233
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
226-456 2.03e-16

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: 79.32  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfHRQAAEEIRILE---HLRKqdkdntmNVIH--MLENFTF-RNHICM 299
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPE-SPETSKEVNALEceiQLLK-------NLLHerIVQYYGClRDPQER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSMNLYELIKKNKFQGF---SLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSS---- 372
Cdd:cd06652   80 TLSIFMEYMPGGSIKDQLKSYgalTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVG--NVKLGDFGASkrlq 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 --CYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPgedEGDQLACMIELLGMPSQKLLDA-- 448
Cdd:cd06652  158 tiCLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQPTNPQLPAhv 234

                 ....*...
gi 153281169 449 SKRAKNFV 456
Cdd:cd06652  235 SDHCRDFL 242
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
221-441 2.10e-16

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 79.22  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMvrnekRFHRQAAEEIRILEH-LRK-QDKDNTMNVIHMLENFTFrNHIC 298
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKV-----ESKSQPKQVLKMEVAvLKKlQGKPHFCRLIGCGRTERY-NYIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTfeLLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRSG-----IKVIDFGSSc 373
Cdd:cd14017   75 MT--LLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAI---GRGPsdertVYILDFGLA- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 yehqRVYTYIQSRFYRAPEVILG----ARYgMPI------------DMWSLGCILAELLTGypLLP--GEDEGDQLACMI 435
Cdd:cd14017  149 ----RQYTNKDGEVERPPRNAAGfrgtVRY-ASVnahrnkeqgrrdDLWSWFYMLIEFVTG--QLPwrKLKDKEEVGKMK 221

                 ....*.
gi 153281169 436 ELLGMP 441
Cdd:cd14017  222 EKIDHE 227
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
228-535 2.14e-16

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: 79.22  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNeKRFHR------QAAEEIRILEHLRKQdkdntmNVIHMLEnfTFRNH----I 297
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKK-RKLRRipngeaNVKREIQILRRLNHR------NVIKLVD--VLYNEekqkL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKFQGFslPLVRkfAHSIL-QCLDAL---HKNRIIHCDLKPENILLKQQGRsgIKVIDFG--- 370
Cdd:cd14119   72 YMVMEYCVGGLQEMLDSAPDKRL--PIWQ--AHGYFvQLIDGLeylHSQGIIHKDIKPGNLLLTTDGT--LKISDFGvae 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 --SSCYEHQRVYTYIQSRFYRAPEVILGARY--GMPIDMWSLGCILAELLTG-YPLlpgedEGDQLACMIELLGmpsqkl 445
Cdd:cd14119  146 alDLFAEDDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGkYPF-----EGDNIYKLFENIG------ 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 446 ldaskraknfvsskgypryctvttlsdgsvvlnggrsrRGKLRGPPESrewgnalkgcdDPLFLDFLKQCLEWDPAVRMT 525
Cdd:cd14119  215 --------------------------------------KGEYTIPDDV-----------DPDLQDLLRGMLEKDPEKRFT 245
                        330
                 ....*....|
gi 153281169 526 PGQALRHPWL 535
Cdd:cd14119  246 IEQIRQHPWF 255
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
226-427 2.62e-16

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: 80.02  E-value: 2.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRnEKRFHRQAAEEIRILEhlrKQ--DKDNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd05632    8 RVLGKGGFGEVCACQVRATGKMYACKRLE-KKRIKKRKGESMALNE---KQilEKVNSQFVVNLAYAYETKDALCLVLTI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 -----LSMNLYELIKKnkfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY--EH 376
Cdd:cd05632   84 mnggdLKFHIYNMGNP----GFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGH--IRISDLGLAVKipEG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDE 427
Cdd:cd05632  158 ESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKE 208
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
222-418 2.80e-16

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: 79.66  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVV---KAYDHKVHQHVALKMVRNEKRFHR-QAAEEIR----ILEHLRKQDKDNTMNvihmlenFTF 293
Cdd:cd05613    2 FELLKVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLKKATIVQKaKTAEHTRterqVLEHIRQSPFLVTLH-------YAF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSMNLYELIKK-NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:cd05613   75 QTDTKLHLILDYINGGELFTHlSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGH--VVLTDFGLS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 373 ----CYEHQRVYTYIQSRFYRAPEVILGARYG--MPIDMWSLGCILAELLTG 418
Cdd:cd05613  153 keflLDENERAYSFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTG 204
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
221-420 2.98e-16

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: 79.32  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV-RNEKRFHRQAAEEIRilehlrkqdkDNTMNVIHMLENFTFRNHI-- 297
Cdd:cd14093    4 KYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIdITGEKSSENEAEELR----------EATRREIEILRQVSGHPNIie 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 ------CMTFELLsmnLYELIKK-------NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgI 364
Cdd:cd14093   74 lhdvfeSPTFIFL---VFELCRKgelfdylTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN--V 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 365 KVIDFGSSCY--EHQRVYTYIQSRFYRAPEVI-----LGAR-YGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14093  149 KISDFGFATRldEGEKLRELCGTPGYLAPEVLkcsmyDNAPgYGKEVDMWACGVIMYTLLAGCP 212
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
222-420 4.12e-16

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 78.46  E-value: 4.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV---RNEKR-FHRQAAEEIRILEHLRKQdkdntmNVIHMLENF--TFRN 295
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLfkaQLEKAgVEHQLRREVEIQSHLRHP------NILRLYGYFhdATRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSMNLYELIKKNKFQGfslplvRKFAHSILQCLDAL---HKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:cd14116   81 YLILEYAPLGTVYRELQKLSKFDE------QRTATYITELANALsycHSKRVIHRDIKPENLLLGSAGE--LKIADFGWS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 373 CYE-HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14116  153 VHApSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKP 201
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
222-418 4.72e-16

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 79.74  E-value: 4.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE----KRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd05593   17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLKNTRHP------FLTSLKYSFQTKDRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---SSC 373
Cdd:cd05593   91 CFVMEYVNGgELFFHLSRERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH--IKITDFGlckEGI 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05593  167 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 211
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
200-418 5.79e-16

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 79.69  E-value: 5.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 200 NGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE----KRFHRQAAEEIRILEhlrk 275
Cdd:cd05594    5 NSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivaKDEVAHTLTENRVLQ---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 276 qdkdNTMNVIHMLENFTFRNHICMTFELLSMNLYEL-IKKNKFQGFSLPLVRKFAHSILQCLDALHKNR-IIHCDLKPEN 353
Cdd:cd05594   81 ----NSRHPFLTALKYSFQTHDRLCFVMEYANGGELfFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLEN 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 354 ILLKQQGRsgIKVIDFGsSCYEHQR----VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05594  157 LMLDKDGH--IKITDFG-LCKEGIKdgatMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 222
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
221-414 6.34e-16

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: 78.23  E-value: 6.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHV-ALKMVrneKRFHRQAAEEIRILEH---LRKQDKDNTMNVIHMLENFTFRNH 296
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKL---KPNYAGAKDRLRRLEEvsiLRELTLDGHDNIVQLIDSWEYHGH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFEL-----LSMNLYELIKKNKFQGFSlplVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFG- 370
Cdd:cd14052   78 LYIQTELcengsLDVFLSELGLLGRLDEFR---VWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEG--TLKIGDFGm 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 371 SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAE 414
Cdd:cd14052  153 ATVWPLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
221-420 7.13e-16

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: 78.09  E-value: 7.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR-NEKRFHRQAAEEIR--------ILEHLRkqdkdNTMNVIHMLENF 291
Cdd:cd14181   11 KYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvTAERLSPEQLEEVRsstlkeihILRQVS-----GHPSIITLIDSY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd14181   86 ESSTFIFLVFDLMRRgELFDYLTEK--VTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLH--IKLSDFG 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 371 SSCY--EHQRVYTYIQSRFYRAPEVILGAR------YGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14181  162 FSCHlePGEKLRELCGTPGYLAPEILKCSMdethpgYGKEVDLWACGVILFTLLAGSP 219
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
225-540 7.52e-16

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 78.54  E-value: 7.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNV--IHMLENFTFrnhICMTF 301
Cdd:cd06633   26 LHEIGHGSFGAVYFATNSHTNEVVAIKkMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYkgCYLKDHTAW---LVMEY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSM-NLYELIKKnkfqgfslPL----VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 376
Cdd:cd06633  103 CLGSAsDLLEVHKK--------PLqeveIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ--VKLADFGSASIAS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 QrVYTYIQSRFYRAPEVILG---ARYGMPIDMWSLGCILAELLTGYPllpgedegdqlacmiELLGMPSQKLLdaskrak 453
Cdd:cd06633  173 P-ANSFVGTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIELAERKP---------------PLFNMNAMSAL------- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFVSSKGYPryctvtTLsdgsvvlnggrsrrgklrgppESREWGNALKGcddplFLDFlkqCLEWDPAVRMTPGQALRHP 533
Cdd:cd06633  230 YHIAQNDSP------TL---------------------QSNEWTDSFRG-----FVDY---CLQKIPQERPSSAELLRHD 274

                 ....*..
gi 153281169 534 WLRRRLP 540
Cdd:cd06633  275 FVRRERP 281
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
222-420 8.02e-16

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: 77.98  E-value: 8.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV---RNEKR-FHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd14117    8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfksQIEKEgVEHQLRREIEIQSHLRHP------NILRLYNYFHDRKRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLY-ELIKKNKF-QGFSLPLVRKFAHSILQCldalHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 374
Cdd:cd14117   82 YLILEYAPRgELYkELQKHGRFdEQRTATFMEELADALHYC----HEKKVIHRDIKPENLLMGYKGE--LKIADFGWSVH 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 375 EHQ-RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14117  156 APSlRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMP 202
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
222-541 9.43e-16

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: 78.15  E-value: 9.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFgQVVKAYDHKV-HQHVALKMVRNEKRfhrQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd14175    3 YVVKETIGVGSY-SVCKRCVHKAtNMEYAVKVIDKSKR---DPSEEIEILLRYGQHP-----NIITLKDVYDDGKHVYLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELL-SMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL-LKQQGR-SGIKVIDFGSSCY--- 374
Cdd:cd14175   74 TELMrGGELLDKILRQKF--FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpESLRICDFGFAKQlra 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLPGEDEgdqlacmiellgMPSQKLldaskrak 453
Cdd:cd14175  152 ENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYtPFANGPSD------------TPEEIL-------- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgypryctvTTLSDGSVVLNGGrsrrgklrgppesrEWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14175  212 --------------TRIGSGKFTLSGG--------------NWNTVSDAAK-----DLVSKMLHVDPHQRLTAKQVLQHP 258
                        330
                 ....*....|
gi 153281169 534 WLRRR--LPK 541
Cdd:cd14175  259 WITQKdkLPQ 268
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
226-418 9.64e-16

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: 78.51  E-value: 9.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNE----KRFHRQAAEEIRILEhlrkqdkdNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEviiaKDEVAHTVTESRVLQ--------NTRHPFLTALKYAFQTHDRLCF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELI-KKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYE----H 376
Cdd:cd05595   73 VMEYANGGELFfHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGH--IKITDFGL-CKEgitdG 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05595  150 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 191
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
226-456 1.03e-15

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 77.43  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE------EIRILEHLRKQdkdntmnviHMLENF-TFRNHIC 298
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEvsalecEIQLLKNLQHE---------RIVQYYgCLRDRAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKKNKFQGF---SLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSS--- 372
Cdd:cd06651   84 KTLTIFMEYMPGGSVKDQLKAYgalTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG--NVKLGDFGASkrl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 ---CYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPgedEGDQLACMIELLGMPSQKLLDA- 448
Cdd:cd06651  162 qtiCMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQLPSh 238

                 ....*....
gi 153281169 449 -SKRAKNFV 456
Cdd:cd06651  239 iSEHARDFL 247
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
226-418 1.07e-15

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: 78.17  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKrfhrqaaeeirILEhlrKQDKDNTMNVIHMLEN------------FTF 293
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEV-----------IIA---KDEVAHTLTENRVLQNtrhpfltslkysFQT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLsmNLYEL---IKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd05571   67 NDRLCFVMEYV--NGGELffhLSRERV--FSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGH--IKITDFG 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 371 SsCYEHQRvYTYIQSRF-----YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05571  141 L-CKEEIS-YGATTKTFcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 191
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
220-418 1.43e-15

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: 77.25  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEvLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAEEIRILEHlRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd05607    3 YFYE-FRVLGKGGFGEVCAVQVKNTGQMYACKKL-DKKRLKKKSGEKMALLEK-EILEKVNSPFIVSLAYAFETKTHLCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLS-----MNLYELIKKnkfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCY 374
Cdd:cd05607   80 VMSLMNggdlkYHIYNVGER----GIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05607  156 EGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAG 199
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
222-582 1.44e-15

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: 78.14  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfhrQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR---DPTEEIEILLRYGQHP-----NIITLKDVYDDGKYVYVVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL-LKQQGR-SGIKVIDFGSSCY---E 375
Cdd:cd14176   93 ELMKGgELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpESIRICDFGFAKQlraE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLPGEDEgdqlacmiellgMPSQKLldaskrakn 454
Cdd:cd14176  171 NGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYtPFANGPDD------------TPEEIL--------- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 fvsskgypryctvTTLSDGSVVLNGGRsrrgklrgppesreWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd14176  230 -------------ARIGSGKFSLSGGY--------------WNSVSDTAK-----DLVSKMLHVDPHQRLTAALVLRHPW 277
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 535 L--RRRLPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTNLAQ 582
Cdd:cd14176  278 IvhWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQ 327
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
221-414 1.46e-15

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: 76.72  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNvihmLENFTFRNHIC- 298
Cdd:cd06607    2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKkMSYSGKQSTEKWQDIIKEVKFLRQLRHPNTIE----YKGCYLREHTAw 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 --MTFELLSM-NLYELIKKnkfqgfslPL----VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS 371
Cdd:cd06607   78 lvMEYCLGSAsDIVEVHKK--------PLqeveIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGT--VKLADFGS 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 372 SCYeHQRVYTYIQSRFYRAPEVILG---ARYGMPIDMWSLG--CI-LAE 414
Cdd:cd06607  148 ASL-VCPANSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGitCIeLAE 195
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
221-417 1.47e-15

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 76.77  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK---MVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd08218    1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKeinISKMSPKEREESRKEVAVLSKMKHP------NIVQYQESFEENGNL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFG-----S 371
Cdd:cd08218   75 YIVMDYCDGgDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDG--IIKLGDFGiarvlN 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153281169 372 SCYEHQRvyTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08218  153 STVELAR--TCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCT 196
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
221-417 1.50e-15

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: 76.92  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQ---AAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEkeaSKKEVILLAKMKHP------NIVTFFASFQENGRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGiKVIDFGSSCY-- 374
Cdd:cd08225   75 FIVMEYCDGgDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVA-KLGDFGIARQln 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 375 -EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08225  154 dSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCT 197
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
227-420 2.12e-15

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 76.50  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKVHQHVA------LKMVRNE-KRFhrqaAEEIRILEHLrkqDKDNTMNVIHMLENfTFRNHICM 299
Cdd:cd13983    8 VLGRGSFKTVYRAFDTEEGIEVAwneiklRKLPKAErQRF----KQEIEILKSL---KHPNIIKFYDSWES-KSKKEVIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELL-SMNLYELIKknKFQGFSLPLVRKFAHSILQCLDALHKNR--IIHCDLKPENILLkqQGRSG-IKVIDFGSSCY- 374
Cdd:cd13983   80 ITELMtSGTLKQYLK--RFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI--NGNTGeVKIGDLGLATLl 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 375 EHQRVYTYIQSRFYRAPEvILGARYGMPIDMWSLGCILAELLTG-YP 420
Cdd:cd13983  156 RQSFAKSVIGTPEFMAPE-MYEEHYDEKVDIYAFGMCLLEMATGeYP 201
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
226-417 2.20e-15

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: 76.42  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAY---DHKVHQHVALKMVRNE--KRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDasESERKDFLKEARVMKKLGHP------NVVRLLGVCTEEEPLYLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLS-MNLYELIKKNK-------FQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:cd00192   75 MEYMEgGDLLDFLRKSRpvfpspePSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV--VKISDFGLS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 --CYEHQRVYTYIQSRFYR---APEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd00192  153 rdIYDDDYYRKKTGGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWEIFT 202
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
228-417 2.24e-15

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: 76.32  E-value: 2.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKvhQHVALKMVRNEKrfHRQAAE-EIRileHLRKQDKDNtmnVIHMLENFTFRNHICMTFELLSM 306
Cdd:cd14058    1 VGRGSFGVVCKARWRN--QIVAVKIIESES--EKKAFEvEVR---QLSRVDHPN---IIKLYGACSNQKPVCLVMEYAEG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 -NLYELIKKNKFQgfslpLVRKFAHSI---LQC---LDALHK---NRIIHCDLKPENILLKQQGRSgIKVIDFGSSCYEH 376
Cdd:cd14058   71 gSLYNVLHGKEPK-----PIYTAAHAMswaLQCakgVAYLHSmkpKALIHRDLKPPNLLLTNGGTV-LKICDFGTACDIS 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 377 QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd14058  145 THMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVIT 185
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
226-420 2.28e-15

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: 77.32  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAydhkvhqhvalkmvrneKRFHRQAAEEIRILEH---LRKQDKDNTM---NVihMLEN--------- 290
Cdd:cd05603    1 KVIGKGSFGKVLLA-----------------KRKCDGKFYAVKVLQKktiLKKKEQNHIMaerNV--LLKNlkhpflvgl 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 -FTFRNHICMTFELLSMNLYEL-IKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd05603   62 hYSFQTSEKLYFVLDYVNGGELfFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGH--VVLTD 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 369 FGsSCYE----HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd05603  140 FG-LCKEgmepEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLP 194
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
225-541 2.35e-15

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 76.63  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfhrQAAEEIR-ILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd06642    9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIDLE-----EAEDEIEdIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSM-NLYELIKKNKFQGFSLPLVRKfahSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFGSSCY---EHQRV 379
Cdd:cd06642   84 LGGgSALDLLKPGPLEETYIATILR---EILKGLDYLHSERKIHRDIKAANVLLSEQG--DVKLADFGVAGQltdTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDegdqLACMIELLGMPsqklldaskraKNfvssk 459
Cdd:cd06642  159 NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEP--PNSD----LHPMRVLFLIP-----------KN----- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 460 gypryctvttlsdgsvvlnggrsrrgklrGPPesrewgnALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRL 539
Cdd:cd06642  217 -----------------------------SPP-------TLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYT 260

                 ..
gi 153281169 540 PK 541
Cdd:cd06642  261 KK 262
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
225-416 2.92e-15

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: 76.46  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAEEIRILEHlRKQDKDNTMNVIHMLENFTFRNHICMTFEL- 303
Cdd:cd05608    6 FRVLGKGGFGEVSACQMRATGKLYACKKL-NKKRLKKRKGYEGAMVEK-RILAKVHSRFIVSLAYAFQTKTDLCLVMTIm 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 ----LSMNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQ-R 378
Cdd:cd05608   84 nggdLRYHIYNVDEENP--GFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQtK 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153281169 379 VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd05608  162 TKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMI 199
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
223-420 3.96e-15

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 75.92  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAydhkvhQHVALKMVRNEKRFHRQ--AAEEIRILEHL----RKQDKDNTMNVIHMLenftFRNH 296
Cdd:cd06617    4 EVIEELGRGAYGVVDKM------RHVPTGTIMAVKRIRATvnSQEQKRLLMDLdismRSVDCPYTVTFYGAL----FREG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ---ICMtfELLSMNLYELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKN-RIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd06617   74 dvwICM--EVMDTSLDKFYKKVYDKGLTIPedILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ--VKLCDFG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 371 SSCYEHQRVYTYIQ--SRFYRAPEVILGAR----YGMPIDMWSLGCILAELLTG-YP 420
Cdd:cd06617  150 ISGYLVDSVAKTIDagCKPYMAPERINPELnqkgYDVKSDVWSLGITMIELATGrFP 206
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
222-436 4.00e-15

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: 76.58  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEhlrKQDKDNTMNVIHMLENFTFRNHI 297
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVEctmvEKRVLA---LSGKPPFLTQLHSCFQTMDRLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYEHQ 377
Cdd:cd05616   79 VMEYVNGGDLMYHIQQVGRFKE---PHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH--IKIADFGM-CKENI 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 378 ----RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIE 436
Cdd:cd05616  153 wdgvTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIME 215
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
222-429 4.06e-15

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 77.20  E-value: 4.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQV---VKAYDHKVHqhvALKMVRNEKRFHRQAaeeiriLEHLRKQD----KDNTMNVIHMLENFTFR 294
Cdd:cd05629    3 FHTVKVIGKGAFGEVrlvQKKDTGKIY---AMKTLLKSEMFKKDQ------LAHVKAERdvlaESDSPWVVSLYYSFQDA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLS----MNLyeLIKknkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd05629   74 QYLYLIMEFLPggdlMTM--LIK---YDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH--IKLSDFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEH---------------------------------------QRVYTYIQSRF-----------YRAPEVILGARYG 400
Cdd:cd05629  147 LSTGFHkqhdsayyqkllqgksnknridnrnsvavdsinltmsskDQIATWKKNRRlmaystvgtpdYIAPEIFLQQGYG 226
                        250       260
                 ....*....|....*....|....*....
gi 153281169 401 MPIDMWSLGCILAELLTGYPLLPGEDEGD 429
Cdd:cd05629  227 QECDWWSLGAIMFECLIGWPPFCSENSHE 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
222-418 4.21e-15

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 75.59  E-value: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAEEI--RILEHLRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKII-DKKKAPDDFVEKFlpRELEILARLNHKSIIKTYEIFETSDGKVYIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSmNLYELIKKnkfqGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSS--CYE 375
Cdd:cd14165   82 ELGVQG-DLLEFIKL----RGALPedVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKD--FNIKLTDFGFSkrCLR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 376 HQRVYTYIQSRF-----YRAPEVILGARYGMPI-DMWSLGCILAELLTG 418
Cdd:cd14165  155 DENGRIVLSKTFcgsaaYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCG 203
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
315-458 4.96e-15

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: 75.55  E-value: 4.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 315 NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG--------SSCYEHQRVYTYIQ-S 385
Cdd:cd06631   95 ARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV--IKLIDFGcakrlcinLSSGSQSQLLKSMRgT 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 386 RFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEgDQLACMIEL---LGMPSQKLLDASKRAKNFVSS 458
Cdd:cd06631  173 PYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKP--PWADM-NPMAAIFAIgsgRKPVPRLPDKFSPEARDFVHA 245
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
221-417 5.11e-15

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: 75.15  E-value: 5.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---------NEKRfhrQAAEEIRILEHLrkqdkdNTMNVIHMLENF 291
Cdd:cd08222    1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKeisvgelqpDETV---DANREAKLLSKL------DHPAIVKFHDSF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFEL-----LSMNLYElIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKqqgRSGIKV 366
Cdd:cd08222   72 VEKESFCIVTEYceggdLDDKISE-YKKSG-TTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK---NNVIKV 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 367 IDFGSSCY---EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08222  147 GDFGISRIlmgTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCC 200
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
228-536 6.79e-15

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: 74.79  E-value: 6.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA-EEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLSM 306
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLfNEVVIMRDYQHP------NIVEMYSSYLVGDELWVVMEFLEG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 N-LYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---SSCYEHQRVYTY 382
Cdd:cd06648   89 GaLTDIVTHTRMNE---EQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGR--VKLSDFGfcaQVSKEVPRRKSL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 383 IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEgdqlacmiellgmpsqKLLDASKRAKNfvsskgyp 462
Cdd:cd06648  164 VGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEP--PYFNE----------------PPLQAMKRIRD-------- 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 463 ryctvttlsdgsvvlnggrsrrgklRGPPESREWGNAlkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLR 536
Cdd:cd06648  218 -------------------------NEPPKLKNLHKV-----SPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
226-435 7.00e-15

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: 76.10  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE----EIRILEHLRK-----------QDKDNTMNVIHMLEN 290
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVEctmtEKRILSLARNhpfltqlyccfQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 FTFRNHIcmtfellsmnlyelikkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFG 370
Cdd:cd05590   81 GDLMFHI-----------------QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC--KLADFG 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 371 SsCYEHQR----VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMI 435
Cdd:cd05590  142 M-CKEGIFngktTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAIL 209
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
228-420 7.18e-15

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 75.48  E-value: 7.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVR---NEKrfhrqaaEEIRILEHLRKQDKDNTMNVIHMLENFTFRNH---ICMTF 301
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKRIRstvDEK-------EQKRLLMDLDVVMRSSDCPYIVKFYGALFREGdcwICMEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKN-RIIHCDLKPENILLKQQGrsGIKVIDFGSScyeHQRV 379
Cdd:cd06616   87 MDISLdKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNG--NIKLCDFGIS---GQLV 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 380 YTYIQS-----RFYRAPEVIL--GARYGMPI--DMWSLGCILAELLTG---YP 420
Cdd:cd06616  162 DSIAKTrdagcRPYMAPERIDpsASRDGYDVrsDVWSLGITLYEVATGkfpYP 214
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
227-425 7.84e-15

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: 75.14  E-value: 7.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAE---EIRILEHLRkqdkdNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKII--EKHPGHSRSRvfrEVETLHQCQ-----GHPNILQLIEYFEDDERFYLVFEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSMN-LYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-SGIKVIDF--GSSCYEHQRV 379
Cdd:cd14090   82 MRGGpLLSHIEKRVH--FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvSPVKICDFdlGSGIKLSSTS 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YTYIQ---------SRFYRAPEVI-----LGARYGMPIDMWSLGCILAELLTGYPLLPGE 425
Cdd:cd14090  160 MTPVTtpelltpvgSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGR 219
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
225-433 8.47e-15

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 74.45  E-value: 8.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  225 LKVIGKGSFGQVVKAY----DHKVHQHVALKMVRNEKRFHRQAA--EEIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLKEGADEEEREDflEEASIMKKLDHP------NIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  299 MTFELLSM-NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQ 377
Cdd:pfam07714  78 IVTEYMPGgDLLDFLRKHK-RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV--VKISDFGLSRDIYD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169  378 RVYTYIQSR-----FYRAPEVILGARYGMPIDMWSLGCILAELLTG----YPLLPGED------EGDQLAC 433
Cdd:pfam07714 155 DDYYRKRGGgklpiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLgeqpYPGMSNEEvleyleDGYRLPQ 225
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
222-418 8.55e-15

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: 76.21  E-value: 8.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMnVIHMLENFTFRNHICMTF 301
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPF-LVGLHSCFQTTSRLFLVI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMN--LYELIKKNKfqgfsLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYEHQ 377
Cdd:cd05617   96 EYVNGGdlMFHMQRQRK-----LPeeHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH--IKLTDYGM-CKEGL 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 378 R----VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05617  168 GpgdtTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAG 212
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
223-535 8.79e-15

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: 74.89  E-value: 8.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR---NEKRFhRQAAEEIRILEhlrkqdKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd06622    4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRlelDESKF-NQIIMELDILH------KAVSPYIVDFYGAFFIEGAVYM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELL---SMN-LYEliKKNKFQGFSLPLVRKFAHSILQCLDAL-HKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSC 373
Cdd:cd06622   77 CMEYMdagSLDkLYA--GGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQ--VKLCDFGvSGN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILG------ARYGMPIDMWSLGCILAELLTG-YPllpgedegdqlacmiellgmpsqkll 446
Cdd:cd06622  153 LVASLAKTNIGCQSYMAPERIKSggpnqnPTYTVQSDVWSLGLSILEMALGrYP-------------------------- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 daskraknfvsskgYPRYCTVTTLSDGSVVLNGGRSRRgklrgPPESREWGNalkgcddplflDFLKQCLEWDPAVRMTP 526
Cdd:cd06622  207 --------------YPPETYANIFAQLSAIVDGDPPTL-----PSGYSDDAQ-----------DFVAKCLNKIPNRRPTY 256

                 ....*....
gi 153281169 527 GQALRHPWL 535
Cdd:cd06622  257 AQLLEHPWL 265
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
222-426 9.22e-15

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: 74.64  E-value: 9.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN----EKRFHRQAAEEIRILEHLrkqDKDNTMNVIHMLEnfTFRNHI 297
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKsggpEEFIQRFLPRELQIVERL---DHKNIIHVYEMLE--SADGKI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLS-MNLYELIkknkFQGFSLP------LVRKFAHSILQCldalHKNRIIHCDLKPENILLkqQGRSgIKVIDFG 370
Cdd:cd14163   77 YLVMELAEdGDVFDCV----LHGGPLPehrakaLFRQLVEAIRYC----HGCGVAHRDLKCENALL--QGFT-LKLTDFG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 371 ------SSCYEHQRvyTYIQSRFYRAPEVILG----ARYGmpiDMWSLGCILAELLTGYplLPGED 426
Cdd:cd14163  146 fakqlpKGGRELSQ--TFCGSTAYAAPEVLQGvphdSRKG---DIWSMGVVLYVMLCAQ--LPFDD 204
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
222-535 9.72e-15

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: 74.61  E-value: 9.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR------NEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd14196    7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrqsraSRRGVSREEIErEVSILRQVLHP------NIITLHDVYENR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL--KQQGRSGIKVIDFG- 370
Cdd:cd14196   81 TDVVLILELVSGgELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldKNIPIPHIKLIDFGl 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ----SSCYEHQRVYTYIQsrfYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDqlacmiellgmpsqkll 446
Cdd:cd14196  159 aheiEDGVEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQE----------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 daskraknfvsskgypryctvtTLSDGSVVlnggrsrrgklrgppeSREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTP 526
Cdd:cd14196  219 ----------------------TLANITAV----------------SYDFDEEFFSHTSELAKDFIRKLLVKETRKRLTI 260

                 ....*....
gi 153281169 527 GQALRHPWL 535
Cdd:cd14196  261 QEALRHPWI 269
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
336-448 1.52e-14

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: 74.74  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 336 LDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCIL 412
Cdd:cd05582  110 LDHLHSLGIIYRDLKPENILLDEDGH--IKLTDFGlskESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLM 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 153281169 413 AELLTGYPLLPGEDEGDQLACMIEL-LGMP------SQKLLDA 448
Cdd:cd05582  188 FEMLTGSLPFQGKDRKETMTMILKAkLGMPqflspeAQSLLRA 230
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
222-422 1.72e-14

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: 74.37  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntMNVIHMLENFTFRNHICMTF 301
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHH-----RNIATYYGAFIKKNPPGMDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 EL-LSM------NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 374
Cdd:cd06637   83 QLwLVMefcgagSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAE--VKLVDFGVSAQ 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 375 EHQ---RVYTYIQSRFYRAPEVIL-----GARYGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd06637  161 LDRtvgRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
222-540 1.92e-14

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: 74.28  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfhrQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKR---DPSEEIEILMRYGQHP-----NIITLKDVYDDGRYVYLVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRS--GIKVIDFGSSCY---E 375
Cdd:cd14177   78 ELMKGgELLDRILRQKF--FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANadSIRICDFGFAKQlrgE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLPGEDEgdqlacmiellgMPSQKLLdaskrakn 454
Cdd:cd14177  156 NGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYtPFANGPND------------TPEEILL-------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 fvsskgypryctvtTLSDGSVVLNGGrsrrgklrgppesrEWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd14177  216 --------------RIGSGKFSLSGG--------------NWDTVSDAAK-----DLLSHMLHVDPHQRYTAEQVLKHSW 262

                 ....*...
gi 153281169 535 L--RRRLP 540
Cdd:cd14177  263 IacRDQLP 270
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
222-422 2.50e-14

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: 73.50  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILE---HLRkqdkdntmNVIHMLENFTFR---- 294
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKkysHHR--------NIATYYGAFIKKsppg 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 --NHICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS 371
Cdd:cd06636   90 hdDQLWLVMEFCGAgSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE--VKLVDFGV 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 372 SCYEHQ---RVYTYIQSRFYRAPEVIL-----GARYGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd06636  168 SAQLDRtvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
221-418 2.53e-14

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 72.94  E-value: 2.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN--------EKRFhrqaaEEIRILEHLrkqdkdNTMNVIHMLENFT 292
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKtqlnpsslQKLF-----REVRIMKIL------NHPNIVKLFEVIE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLS-------MNLYELIKKNKFQGfslplvrKFaHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIK 365
Cdd:cd14072   70 TEKTLYLVMEYASggevfdyLVAHGRMKEKEARA-------KF-RQIVSAVQYCHQKRIVHRDLKAENLLLDAD--MNIK 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 366 VIDFGSS--CYEHQRVYTYIQSRFYRAPEVILGARYGMP-IDMWSLGCILAELLTG 418
Cdd:cd14072  140 IADFGFSneFTPGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSG 195
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
222-415 2.55e-14

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: 73.56  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR------NEKRFHRqaaeEIRILEHLRKQdkdntmnviHMLENFT--F 293
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKlrseskNNSRILR----EVMLLSRLNHQ---------HVVRYYQawI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNH---ICMTFeLLSMNLYELIKKNKFQ--GFSLPLVRKfahsILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd14046   75 ERAnlyIQMEY-CEKSTLRDLIDSGLFQdtDRLWRLFRQ----ILEGLAYIHSQGIIHRDLKPVNIFLDSNGN--VKIGD 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSCYEHQRVYTYIQ---------------------SRFYRAPEVILGA--RYGMPIDMWSLGCILAEL 415
Cdd:cd14046  148 FGLATSNKLNVELATQdinkstsaalgssgdltgnvgTALYVAPEVQSGTksTYNEKVDMYSLGIIFFEM 217
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
228-535 2.57e-14

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: 73.87  E-value: 2.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA-EEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS- 305
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLfNEVVIMRDYQHP------NVVEMYKSYLVGEELWVLMEYLQg 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 ---MNLYELIKKNKFQgfslplVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRV--- 379
Cdd:cd06659  103 galTDIVSQTRLNEEQ------IATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGR--VKLSDFGFCAQISKDVpkr 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllpgedegdqlacmiellgmP--SQKLLDASKRAKNfvs 457
Cdd:cd06659  175 KSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEP--------------------PyfSDSPVQAMKRLRD--- 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 458 skgypryctvttlsdgsvvlnggrsrrgklRGPPESRewgNALKGcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd06659  232 ------------------------------SPPPKLK---NSHKA--SPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
221-430 2.66e-14

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: 73.14  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQ-HVALKMVRNEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd14088    2 RYDLGQVIKTEEFCEIFRAKDKTTGKlYTCKKFLKRDGRKVRKAAKnEINILKMVKHP------NILQLVDVFETRKEYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLS-MNLYELIKKnkfQGFSLPlvRKFAHSILQCLDA---LHKNRIIHCDLKPENIL-LKQQGRSGIKVIDFGSSC 373
Cdd:cd14088   76 IFLELATgREVFDWILD---QGYYSE--RDTSNVIRQVLEAvayLHSLKIVHRNLKLENLVyYNRLKNSKIVISDFHLAK 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 374 YEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPllPGEDEGDQ 430
Cdd:cd14088  151 LENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNP--PFYDEAEE 205
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
222-420 3.13e-14

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: 73.31  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHV-ALKMVRNEK-RFHRQAAE----------EIRIL-EHLRKQdkdntmNVIHML 288
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVRKKSNGQTLlALKEINMTNpAFGRTEQErdksvgdiisEVNIIkEQLRHP------NIVRYY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 289 ENFTFRNHICMTFELLS-MNLYELIK--KNKFQGFSLPLVRKFAHSILQCLDALHKNR-IIHCDLKPENILLKQQGRsgI 364
Cdd:cd08528   76 KTFLENDRLYIVMELIEgAPLGEHFSslKEKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDK--V 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 365 KVIDFG---SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd08528  154 TITDFGlakQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQP 212
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
222-420 3.16e-14

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: 73.18  E-value: 3.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfhrQAAEEIR-ILEHLRKQDKDNTMNVIHMLENFTFRNHICMT 300
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLE-----EAEDEIEdIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELL----SMNLYELIKKNKFQgfslplVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY-- 374
Cdd:cd06641   81 MEYLgggsALDLLEPGPLDETQ------IATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE--VKLADFGVAGQlt 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 375 -EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd06641  153 dTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEP 199
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
222-536 4.11e-14

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: 72.73  E-value: 4.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR------NEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd14195    7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKkrrlssSRRGVSREEIErEVNILREIQHP------NIITLHDIFENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFELLSM-NLYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG--IKVIDFG- 370
Cdd:cd14195   81 TDVVLILELVSGgELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNprIKLIDFGi 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ----SSCYEHQRVYTYIQsrfYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMiellgmpsqkll 446
Cdd:cd14195  159 ahkiEAGNEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNI------------ 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 447 daskRAKNFVSSKGYprYCTVTTLSDgsvvlnggrsrrgklrgppesrewgnalkgcddplflDFLKQCLEWDPAVRMTP 526
Cdd:cd14195  224 ----SAVNYDFDEEY--FSNTSELAK-------------------------------------DFIRRLLVKDPKKRMTI 260
                        330
                 ....*....|
gi 153281169 527 GQALRHPWLR 536
Cdd:cd14195  261 AQSLEHSWIK 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
222-456 4.23e-14

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: 72.61  E-value: 4.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGqVVKAYDHKVHQHV-ALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd14107    4 YEVKEEIGRGTFG-FVKRVTHKGNGECcAAKFIPLRSSTRARAFQERDILARLSHR------RLTCLLDQFETRKTLILI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMN--LYELIKKNKFQGFSlplVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFG----SSCY 374
Cdd:cd14107   77 LELCSSEelLDRLFLKGVVTEAE---VKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGfaqeITPS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQrvYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGE-DEGDQLACMIELLGMPSQKLLDASKRAK 453
Cdd:cd14107  154 EHQ--FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGEnDRATLLNVAEGVVSWDTPEITHLSEDAK 231

                 ...
gi 153281169 454 NFV 456
Cdd:cd14107  232 DFI 234
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
221-427 4.35e-14

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: 72.66  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVL--KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEHLRkqdkdNTMNVIHMLENFTFRN 295
Cdd:cd14197    8 RYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEiihEIAVLELAQ-----ANPWVINLHEVYETAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDFGSS- 372
Cdd:cd14197   83 EMILVLEYAAGgEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGdIKIVDFGLSr 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 373 -CYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDE 427
Cdd:cd14197  163 iLKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDK 218
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
225-418 4.65e-14

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 72.42  E-value: 4.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKvhQHVALKMVRNEK--RFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTfrnhiCMTFE 302
Cdd:cd13979    8 QEPLGSGGFGSVYKATYKG--ETVAVKIVRRRRknRASRQSFWAELNAARLRHE------NIVRVLAAET-----GTDFA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSMNLYELIKKNKFQ------GFSLPLVR--KFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFGSS-- 372
Cdd:cd13979   75 SLGLIIMEYCGNGTLQqliyegSEPLPLAHriLISLDIARALRFCHSHGIVHLDVKPANILISEQGVC--KLCDFGCSvk 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 373 -----CYEHQRVYTYIQSRfYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd13979  153 lgegnEVGTPRSHIGGTYT-YRAPELLKGERVTPKADIYSFGITLWQMLTR 202
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
226-533 4.93e-14

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: 72.30  E-value: 4.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKA--YDHKvhqHVALKmvRNEKRFHRQAAEEIRILEHlrkqdKDNTMNVIHMLENFTFRNHICMTFEL 303
Cdd:cd13982    7 KVLGYGSEGTIVFRgtFDGR---PVAVK--RLLPEFFDFADREVQLLRE-----SDEHPNVIRYFCTEKDRQFLYIALEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSMNLYELIKKNkfqgfslPLVRKFAHSILQC----------LDALHKNRIIHCDLKPENILLKQQGRSG---IKVIDFG 370
Cdd:cd13982   77 CAASLQDLVESP-------RESKLFLRPGLEPvrllrqiasgLAHLHSLNIVHRDLKPQNILISTPNAHGnvrAMISDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEHQRVYTYIQSRF------YRAPEVILGARYGMP---IDMWSLGCILAELLTG--YPLlpgedeGDQLacmiellg 439
Cdd:cd13982  150 LCKKLDVGRSSFSRRSGvagtsgWIAPEMLSGSTKRRQtraVDIFSLGCVFYYVLSGgsHPF------GDKL-------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 440 mpsqklldasKRAKNFVSSKgyprYCTVTTLSDGSvvlnggrsrrgklrgppesrewgnalkgcDDPLFLDFLKQCLEWD 519
Cdd:cd13982  216 ----------EREANILKGK----YSLDKLLSLGE-----------------------------HGPEAQDLIERMIDFD 252
                        330
                 ....*....|....
gi 153281169 520 PAVRMTPGQALRHP 533
Cdd:cd13982  253 PEKRPSAEEVLNHP 266
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
221-417 5.18e-14

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: 72.08  E-value: 5.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQV--VKaydHKV--HQHVALKM-VRNEKRFHRQAAE-EIRILEHLRKQdkdntmNVIHMLENFTFR 294
Cdd:cd08223    1 EYQFLRVIGKGSYGEVwlVR---HKRdrKQYVIKKLnLKNASKRERKAAEqEAKLLSKLKHP------NIVSYKESFEGE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 N---HICMTFeLLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG- 370
Cdd:cd08223   72 DgflYIVMGF-CEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKS--NIIKVGDLGi 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 371 -----SSCyehQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd08223  149 arvleSSS---DMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMAT 197
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
225-537 5.90e-14

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 72.60  E-value: 5.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE--KRFHRQAAEEIRILEhlrkqdKDNTMNVIHMLENFTFRNHICMTFE 302
Cdd:cd06619    6 QEILGHGNGGTVYKAYHLLTRRILAVKVIPLDitVELQKQIMSELEILY------KCDSPYIIGFYGAFFVENRISICTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LL---SMNLYELIKKnkfqgfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSCYEHQR 378
Cdd:cd06619   80 FMdggSLDVYRKIPE--------HVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQ--VKLCDFGvSTQLVNSI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG---YPLLpgedEGDQLACM-IELLgmpsQKLLDASKrakn 454
Cdd:cd06619  150 AKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGrfpYPQI----QKNQGSLMpLQLL----QCIVDEDP---- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 455 fvsskgyPRyctvttLSDGSVvlnggrsrrgklrgppesrewgnalkgcdDPLFLDFLKQCLEWDPAVRMTPGQALRHPW 534
Cdd:cd06619  218 -------PV------LPVGQF-----------------------------SEKFVHFITQCMRKQPKERPAPENLMDHPF 255

                 ...
gi 153281169 535 LRR 537
Cdd:cd06619  256 IVQ 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
221-429 5.97e-14

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: 71.94  E-value: 5.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEI---RILEHlrkqdkdntMNVIHMLENFTFRNHI 297
Cdd:cd14665    1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIinhRSLRH---------PNIVRFKEVILTPTHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFG--SSCY 374
Cdd:cd14665   72 AIVMEYAAGgELFERICNAG--RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGysKSSV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG-YPLLPGEDEGD 429
Cdd:cd14665  150 LHSQPKSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGaYPFEDPEEPRN 206
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
226-426 7.51e-14

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: 71.88  E-value: 7.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE---EIRILEHLRKQDK--------DNTMNVIHMLEnFTFR 294
Cdd:cd14198   14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEilhEIAVLELAKSNPRvvnlhevyETTSEIILILE-YAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHIcmtFELLSMNLYELIKKNKFqgfsLPLVRKfahsILQCLDALHKNRIIHCDLKPENILLKQQGRSG-IKVIDFGSSc 373
Cdd:cd14198   93 GEI---FNLCVPDLAEMVSENDI----IRLIRQ----ILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGdIKIVDFGMS- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 374 yehQRVYTYIQSRF------YRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:cd14198  161 ---RKIGHACELREimgtpeYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGED 216
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
222-537 8.37e-14

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 72.78  E-value: 8.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAydhkVHQHVALKMVRneKRFHRQAAEEIR--ILEHLRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd06650    7 FEKISELGAGNGGVVFKV----SHKPSGLVMAR--KLIHLEIKPAIRnqIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKnkfqGFSLP--LVRKFAHSILQCLDAL-HKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSCY 374
Cdd:cd06650   81 CMEHMDGgSLDQVLKK----AGRIPeqILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGE--IKLCDFGvSGQL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEDEGDQLACMIELLGMPSQKLLdASKRAK 453
Cdd:cd06650  155 IDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGrYPIPPPDAKELELMFGCQVEGDAAETPP-RPRTPG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFVSSKGYPRYCTVTTLSDGSVVLNggrsrrgklRGPPESREWGNALKgcddplFLDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd06650  234 RPLSSYGMDSRPPMAIFELLDYIVN---------EPPPKLPSGVFSLE------FQDFVNKCLIKNPAERADLKQLMVHA 298

                 ....
gi 153281169 534 WLRR 537
Cdd:cd06650  299 FIKR 302
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
222-431 9.54e-14

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: 71.39  E-value: 9.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHE------RIMALHEAYITPRYLVLIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMN--LYELIkkNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIKVIDFGSSCYEH--- 376
Cdd:cd14111   79 EFCSGKelLHSLI--DRFR-YSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMV--TNLNAIKIVDFGSAQSFNpls 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 377 -QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYplLPGEDEGDQL 431
Cdd:cd14111  154 lRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGR--SPFEDQDPQE 207
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
220-432 1.07e-13

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: 71.55  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVIGKGSFGQVVKAYDHKVHQHVALK--MVRNEKRFhRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFR--N 295
Cdd:cd14037    3 HHVTIEKYLAEGGFAHVYLVKTSNGGNRAALKrvYVNDEHDL-NVCKREIEIMKRLSGHK-----NIVGYIDSSANRsgN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM----NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALH--KNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd14037   77 GVYEVLLLMEYckggGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGN--YKLCDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 370 GSSCYEHQRV---------------YTYIQsrfYRAPEVI---LGARYGMPIDMWSLGCILAELLtgYPLLPGEdEGDQL 431
Cdd:cd14037  155 GSATTKILPPqtkqgvtyveedikkYTTLQ---YRAPEMIdlyRGKPITEKSDIWALGCLLYKLC--FYTTPFE-ESGQL 228

                 .
gi 153281169 432 A 432
Cdd:cd14037  229 A 229
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
221-412 1.22e-13

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 71.54  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKmVRNEKRFHRQAA----------------------------EEIRILeh 272
Cdd:cd14199    3 QYKLKDEIGKGSYGVVKLAYNEDDNTYYAMK-VLSKKKLMRQAGfprrppprgaraapegctqprgpiervyQEIAIL-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 273 lRKQDKDNTMNVIHMLENFTfRNHICMTFELLSMNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPE 352
Cdd:cd14199   80 -KKLDHPNVVKLVEVLDDPS-EDHLYMVFELVKQGPVMEVPTLK--PLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 353 NILLKQQGRsgIKVIDFG-SSCYEHQRVY--TYIQSRFYRAPEVILGAR---YGMPIDMWSLGCIL 412
Cdd:cd14199  156 NLLVGEDGH--IKIADFGvSNEFEGSDALltNTVGTPAFMAPETLSETRkifSGKALDVWAMGVTL 219
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
222-416 1.41e-13

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: 70.98  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrneKRFHRQAAEEIRILEHLrkqDKDNTMNVIHMLENFTF-------- 293
Cdd:cd14047    8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV---KLNNEKAEREVKALAKL---DHPNIVRYNGCWDGFDYdpetsssn 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 --RNHICMTFelLSMNLYE-------LIKKNKFQGFSLPLVRKFaHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgI 364
Cdd:cd14047   82 ssRSKTKCLF--IQMEFCEkgtleswIEKRNGEKLDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK--V 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 365 KVIDFGSScyehQRVYTYIQ------SRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14047  157 KIGDFGLV----TSLKNDGKrtkskgTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
223-420 1.42e-13

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: 71.64  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAyDHKVHQHV-ALK-MVRNekrfhrQAAEEI-RILEHLRKQDKDNTMNVI-----HMLENFTFR 294
Cdd:cd06618   18 ENLGEIGSGTCGQVYKM-RHKKTGHVmAVKqMRRS------GNKEENkRILMDLDVVLKSHDCPYIvkcygYFITDSDVF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 nhICMtfELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDAL-HKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSc 373
Cdd:cd06618   91 --ICM--ELMSTCLDKLLKRIQ-GPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGN--VKLCDFGIS- 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 374 yeHQRVYTYIQSR-----FYRAPEVI---LGARYGMPIDMWSLGCILAELLTG-YP 420
Cdd:cd06618  163 --GRLVDSKAKTRsagcaAYMAPERIdppDNPKYDIRADVWSLGISLVELATGqFP 216
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
225-422 1.44e-13

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 72.01  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNvihmLENFTFRNH---ICMT 300
Cdd:cd06635   30 LREIGHGSFGAVYFARDVRTSEVVAIKkMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIE----YKGCYLREHtawLVME 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQrVY 380
Cdd:cd06635  106 YCLGSASDLLEVHKKPLQEIEIAAI---THGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ--VKLADFGSASIASP-AN 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 381 TYIQSRFYRAPEVILG---ARYGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd06635  180 SFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPL 224
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
226-448 1.51e-13

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: 70.73  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEI--RILEHLRKQDKdntmNVIHMLENFTFRNHICMTFEL 303
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIvnEIELHRDLHHK----HVVKFSHHFEDAENIYIFLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH---QRVY 380
Cdd:cd14189   83 CSRKSLAHIWKAR-HTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENME--LKVGDFGLAARLEppeQRKK 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL-------LGMPSQKLLDA 448
Cdd:cd14189  160 TICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVkytlpasLSLPARHLLAG 234
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
221-420 1.72e-13

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 70.73  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK--RFHRQAAEEIRILEHlRKQDKDNTMNVIHMLENFTFrnhIC 298
Cdd:cd14187    8 RYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLllKPHQKEKMSMEIAIH-RSLAHQHVVGFHGFFEDNDF---VY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC---Y 374
Cdd:cd14187   84 VVLELCRRrSLLELHKRRK--ALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDME--VKIGDFGLATkveY 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14187  160 DGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKP 205
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
221-418 1.86e-13

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: 71.50  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-----MVRNEKRFHRqAAEEIRILehlrkqdkdNTMN---VIHMLENFT 292
Cdd:cd05574    2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKvldkeEMIKRNKVKR-VLTEREIL---------ATLDhpfLPTLYASFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLS-MNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG- 370
Cdd:cd05574   72 TSTHLCFVMDYCPgGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGH--IMLTDFDl 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 371 ---SSCYEHQRVYTYIQSRF----------------------------YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05574  150 skqSSVTPPPVRKSLRKGSRrssvksieketfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYG 228
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
228-422 2.09e-13

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 71.10  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVR------NEKRFHRqaaeEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRlelsvkNKDRWCH----EIQIMKKL------NHPNVVKACDVPEEMNFLVNDV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSM------NLYELIKK-NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGI-KVIDFGSSC 373
Cdd:cd14039   71 PLLAMeycsggDLRKLLNKpENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAK 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 374 YEHQ--RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLL 422
Cdd:cd14039  151 DLDQgsLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFrPFL 202
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
228-418 2.10e-13

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: 70.22  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKvhQHVALKMVRNEKrfhrqaaeEIRIlEHLRKQdkdNTMNVIHMLENFTFRNHICMTFELLSM- 306
Cdd:cd14059    1 LGSGAQGAVFLGKFRG--EEVAVKKVRDEK--------ETDI-KHLRKL---NHPNIIKFKGVCTQAPCYCILMEYCPYg 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKknkfQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSS--CYEHQRVYTY 382
Cdd:cd14059   67 QLYEVLR----AGREITpsLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYN--DVLKISDFGTSkeLSEKSTKMSF 140
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153281169 383 IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14059  141 AGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTG 176
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
222-466 2.44e-13

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 71.63  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkDNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd05627    4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVE--ADGAWVVKMFYSFQDKRNLYLIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLS----MNLyeLIKKNKfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG------- 370
Cdd:cd05627   82 EFLPggdmMTL--LMKKDT---LSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH--VKLSDFGlctglkk 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ---SSCYEH----------------------------QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY 419
Cdd:cd05627  155 ahrTEFYRNlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGY 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 420 PLLPGEDEGDQLACMI---ELLGMPSQklLDASKRAKNFVSskgypRYCT 466
Cdd:cd05627  235 PPFCSETPQETYRKVMnwkETLVFPPE--VPISEKAKDLIL-----RFCT 277
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
222-538 2.68e-13

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: 70.81  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGqVVKAYDHKVHQ-HVALKMVRNEKRfhrQAAEEIRILehLRKQDKDNTMNVIHMLENFTFrnhICMT 300
Cdd:cd14178    5 YEIKEDIGIGSYS-VCKRCVHKATStEYAVKIIDKSKR---DPSEEIEIL--LRYGQHPNIITLKDVYDDGKF---VYLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELL-SMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRS--GIKVIDFGSSCY--- 374
Cdd:cd14178   76 MELMrGGELLDRILRQKC--FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNpeSIRICDFGFAKQlra 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGY-PLLPGEDEgdqlacmiellgMPSQKLldaskrak 453
Cdd:cd14178  154 ENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFtPFANGPDD------------TPEEIL-------- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 nfvsskgypryctvTTLSDGSVVLNGGrsrrgklrgppesrEWGNALKGCDdplflDFLKQCLEWDPAVRMTPGQALRHP 533
Cdd:cd14178  214 --------------ARIGSGKYALSGG--------------NWDSISDAAK-----DIVSKMLHVDPHQRLTAPQVLRHP 260

                 ....*
gi 153281169 534 WLRRR 538
Cdd:cd14178  261 WIVNR 265
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
227-418 2.82e-13

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 70.34  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAyDHKVhQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNT-------MNVIHMLE--NFTFRNHI 297
Cdd:cd14000    1 LLGDGGFGSVYRA-SYKG-EPVAVKIFNKHTSSNFANVPADTMLRHLRATDAMKNfrllrqeLTVLSHLHhpSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLY------ELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENIL---LKQQGRSGIKV 366
Cdd:cd14000   79 GIHPLMLVLELAplgsldHLLQQDSRSFASLGrtLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSAIIIKI 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 367 IDFGSSCYE-HQRVYTYIQSRFYRAPEVILGA-RYGMPIDMWSLGCILAELLTG 418
Cdd:cd14000  159 ADYGISRQCcRMGAKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSG 212
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
222-420 2.94e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 71.16  E-value: 2.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKA-YDHKVHQHVALKmvrnekRFHRQAAEEIRILEHLRKQDKD-NTMN---VIHMLENFTFRNH 296
Cdd:PTZ00426  32 FNFIRTLGTGSFGRVILAtYKNEDFPPVAIK------RFEKSKIIKQKQVDHVFSERKIlNYINhpfCVNLYGSFKDESY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFE-LLSMNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYE 375
Cdd:PTZ00426 106 LYLVLEfVIGGEFFTFLRRNK--RFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGF--IKMTDFGFAKVV 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 376 HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:PTZ00426 182 DTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCP 226
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
222-417 3.40e-13

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: 69.64  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKM----VRNEKRFHRQAaEEIRILEHLRKQDkdntmNVIHMLENFTFRNHI 297
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRsrsrFRGEKDRKRKL-EEVERHEKLGEHP-----NCVRFIKAWEEKGIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKfqgfSLPLVR--KFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYE 375
Cdd:cd14050   77 YIQTELCDTSLQQYCEETH----SLPESEvwNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGV--CKLGDFGLVVEL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 376 HQRVYTYIQ---SRfYRAPEVILGaRYGMPIDMWSLGCILAELLT 417
Cdd:cd14050  151 DKEDIHDAQegdPR-YMAPELLQG-SFTKAADIFSLGITILELAC 193
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
226-429 4.21e-13

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: 70.60  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAydhkvhqhvalkmvrnekrfHRQAAEEIRILEHLRK----QDKD--NTM---NVIHMLENFTFRNH 296
Cdd:cd05591    1 KVLGKGSFGKVMLA--------------------ERKGTDEVYAIKVLKKdvilQDDDvdCTMtekRILALAAKHPFLTA 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFE-----LLSMN-------LYELIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgI 364
Cdd:cd05591   61 LHSCFQtkdrlFFVMEyvnggdlMFQIQRARKFDE---PRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH--C 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 365 KVIDFGSsCYE----HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGD 429
Cdd:cd05591  136 KLADFGM-CKEgilnGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 203
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
226-424 4.21e-13

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 70.06  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEIRILEHLRK-QDKDNTMNVIHMLENFTfrnHICMTFE-L 303
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKII--EKNAGHSRSRVFREVETLYQcQGNKNILELIEFFEDDT---RFYLVFEkL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-SGIKVIDF--------GSSC- 373
Cdd:cd14174   83 RGGSILAHIQKRKH--FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvSPVKICDFdlgsgvklNSACt 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 374 -YEHQRVYTYIQSRFYRAPEVI-----LGARYGMPIDMWSLGCILAELLTGYPLLPG 424
Cdd:cd14174  161 pITTPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVG 217
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
222-418 4.86e-13

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: 71.19  E-value: 4.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVvKAYDHKVHQHV-ALKMVRNEKRFHRQAA----EEIRILEHLrkqdkdNTMNVIHMLENFTFRNH 296
Cdd:cd05622   75 YEVVKVIGRGAFGEV-QLVRHKSTRKVyAMKLLSKFEMIKRSDSaffwEERDIMAFA------NSPWVVQLFYAFQDDRY 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSMNlyELIkkNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 374
Cdd:cd05622  148 LYMVMEYMPGG--DLV--NLMSNYDVPekWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH--LKLADFGTCMK 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 375 EHQ----RVYTYIQSRFYRAPEVILG----ARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05622  222 MNKegmvRCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVG 273
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
222-429 5.91e-13

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: 69.44  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQV-----VKAYDHKVHQHVALKMVRNEKRFHRQAA----EEIRILEHLRKQdkdntmNVIHMLENFT 292
Cdd:cd14076    3 YILGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENCQTskimREINILKGLTHP------NIVRLLDVLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSM-NLYELIKKNKFQGFSLPlVRKFAHSIlQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG- 370
Cdd:cd14076   77 TKKYIGIVLEFVSGgELFDYILARRRLKDSVA-CRLFAQLI-SGVAYLHKKGVVHRDLKLENLLLDKN--RNLVITDFGf 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 371 SSCYEHQR---VYTYIQSRFYRAPE-VILGARY-GMPIDMWSLGCILAELLTGYplLPGEDEGD 429
Cdd:cd14076  153 ANTFDHFNgdlMSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGY--LPFDDDPH 214
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
222-418 5.97e-13

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: 68.90  E-value: 5.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK---RFHRQAAEEIRILEHLrkqdkdNTMNVIHM---LENFTfRN 295
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKldqKTQRLLSREISSMEKL------HHPNIIRLyevVETLS-KL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTF----ELLSmnlyELIKKNKF-QGFSLPLvrkFAHsILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd14075   77 HLVMEYasggELYT----KISTEGKLsESEAKPL---FAQ-IVSAVKHMHENNIIHRDLKAENVFYASNNC--VKVGDFG 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 371 SSCY--EHQRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG 418
Cdd:cd14075  147 FSTHakRGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTG 197
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
226-535 6.09e-13

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: 69.67  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQHVALKMVrnEKRFHRQAAEEIRILEHLRKQDKDNtmNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd14173    8 EVLGEGAYARVQTCINLITNKEYAVKII--EKRPGHSRSRVFREVEMLYQCQGHR--NVLELIEFFEEEDKFYLVFEKMR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MN--LYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-SGIKVIDF----------GSS 372
Cdd:cd14173   84 GGsiLSHIHRRRHFNELEASVV---VQDIASALDFLHNKGIAHRDLKPENILCEHPNQvSPVKICDFdlgsgiklnsDCS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 CYEHQRVYTYIQSRFYRAPEVI-----LGARYGMPIDMWSLGCILAELLTGYPLLPGE-------DEGDQL-ACmiellg 439
Cdd:cd14173  161 PISTPELLTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEACpAC------ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 440 mpsQKLLdaskraknFVSSKgypryctvttlsdgsvvlnggrsrRGKLRGPpeSREWGNALKGCDdplflDFLKQCLEWD 519
Cdd:cd14173  235 ---QNML--------FESIQ------------------------EGKYEFP--EKDWAHISCAAK-----DLISKLLVRD 272
                        330
                 ....*....|....*.
gi 153281169 520 PAVRMTPGQALRHPWL 535
Cdd:cd14173  273 AKQRLSAAQVLQHPWV 288
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
216-463 7.66e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 70.88  E-value: 7.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 216 DHVAYRYEVLKVIGKGSFGQV----VKAYDH----------------KVHQHVAlKMVRNEKRFHRQAAEEIRILEHLrk 275
Cdd:PHA03210 144 DEFLAHFRVIDDLPAGAFGKIficaLRASTEeaearrgvnstnqgkpKCERLIA-KRVKAGSRAAIQLENEILALGRL-- 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 276 qdkdNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLV---RKFAHSILQCLDALHKNRIIHCDLKPE 352
Cdd:PHA03210 221 ----NHENILKIEEILRSEANTYMITQKYDFDLYSFMYDEAFDWKDRPLLkqtRAIMKQLLCAVEYIHDKKLIHRDIKLE 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 353 NILLKQQGRsgIKVIDFGSSC-YEHQRV---YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTgYPLLP----G 424
Cdd:PHA03210 297 NIFLNCDGK--IVLGDFGTAMpFEKEREafdYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLS-HDFCPigdgG 373
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 153281169 425 EDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPR 463
Cdd:PHA03210 374 GKPGKQLLKIIDSLSVCDEEFPDPPCKLFDYIDSAEIDH 412
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
221-412 8.12e-13

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: 69.08  E-value: 8.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLRKQDkdntmNVIHML--------ENF 291
Cdd:cd14036    1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQEINFMKKLSGHP-----NIVQFCsaasigkeESD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLSMNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNR--IIHCDLKPENILLKQQGRsgIKVID 368
Cdd:cd14036   76 QGQAEYLLLTELCKGQLVDFVKKVEAPGpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ--IKLCD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 369 FGSSCYE-HQRVYTYIQSR--------------FYRAPEVI-LGARYgmPI----DMWSLGCIL 412
Cdd:cd14036  154 FGSATTEaHYPDYSWSAQKrslvedeitrnttpMYRTPEMIdLYSNY--PIgekqDIWALGCIL 215
pknD PRK13184
serine/threonine-protein kinase PknD;
221-417 8.38e-13

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 71.34  E-value: 8.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNE----KRFHRQAAEEIRILEHLRK----------QDKDNTMNVIH 286
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlsenPLLKKRFLREAKIAADLIHpgivpvysicSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 287 MLENFTFRnHIcmtfeLLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRSGIKV 366
Cdd:PRK13184  83 YIEGYTLK-SL-----LKSVWQKESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILL---GLFGEVV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 367 I-DFGSSCYEHQRVYTYIQSRF---------------------YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:PRK13184 154 IlDWGAAIFKKLEEEDLLDIDVdernicyssmtipgkivgtpdYMAPERLLGVPASESTDIYALGVILYQMLT 226
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
222-437 8.74e-13

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: 68.72  E-value: 8.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFH-------RQAAEEIRILEHLrkQDKDNTMNVIHMLENFTFR 294
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklpgvNPVPNEVALLQSV--GGGPGHRGVIRLLDWFEIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTFE--LLSMNLYELIKKnkfQGfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFG 370
Cdd:cd14101   80 EGFLLVLErpQHCQDLFDYITE---RG-ALDesLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLR-TGDIKLIDFG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 371 SSCYEHQRVYT-YIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTGYplLPGEDEGDQLACMIEL 437
Cdd:cd14101  155 SGATLKDSMYTdFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGD--IPFERDTDILKAKPSF 221
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
228-370 9.94e-13

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 65.54  E-value: 9.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAE-EIRILEHLRKQDKdNTMNVIHMLENFTFRNhicMTFELLS- 305
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLEsEMDILRRLKGLEL-NIPKVLVTEDVDGPNI---LLMELVKg 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 306 MNLYELIKKN-KFQGfslpLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd13968   77 GTLIAYTQEEeLDEK----DVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGN--VKLIDFG 136
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
221-429 1.05e-12

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 68.26  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEI---RILEHlrkqdkdntMNVIHMLENFTFRNHI 297
Cdd:cd14662    1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIinhRSLRH---------PNIIRFKEVVLTPTHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNlyELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFG--SSCY 374
Cdd:cd14662   72 AIVMEYAAGG--ELFERICNAGrFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGysKSSV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG-YPLlpgEDEGD 429
Cdd:cd14662  150 LHSQPKSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGaYPF---EDPDD 203
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
222-419 1.22e-12

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: 69.32  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAEEIRILEH--LRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL-DKKRIKMKQGETLALNERimLSLVSTGDCPFIVCMTYAFHTPDKLCF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELlsMNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFGSSC-YEHQ 377
Cdd:cd05633   86 ILDL--MNGGDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV--RISDLGLACdFSKK 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 378 RVYTYIQSRFYRAPEVIL-GARYGMPIDMWSLGCILAELLTGY 419
Cdd:cd05633  162 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGH 204
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
221-457 1.50e-12

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: 67.73  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEI-------RILEHlrkqdkdntMNVIHMLENFTF 293
Cdd:cd14188    2 RYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIdkeielhRILHH---------KHVVQFYHYFED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLSM-NLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:cd14188   73 KENIYILLEYCSRrSMAHILKARKV--LTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENME--LKVGDFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 C----YEHQRvYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIEL-LGMPSQKLLD 447
Cdd:cd14188  149 ArlepLEHRR-RTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREArYSLPSSLLAP 227
                        250
                 ....*....|
gi 153281169 448 ASKRAKNFVS 457
Cdd:cd14188  228 AKHLIASMLS 237
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
225-422 1.76e-12

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 68.51  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNvihmLENFTFRNH---ICMT 300
Cdd:cd06634   20 LREIGHGSFGAVYFARDVRNNEVVAIKkMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIE----YRGCYLREHtawLVME 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYeHQRVY 380
Cdd:cd06634   96 YCLGSASDLLEVHKKPLQEVEIAAI---THGALQGLAYLHSHNMIHRDVKAGNILLTEPGL--VKLGDFGSASI-MAPAN 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 381 TYIQSRFYRAPEVILG---ARYGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd06634  170 SFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPL 214
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
222-418 1.97e-12

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: 68.87  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVvKAYDHKVHQHV-ALKMVRNEKRFHRQAA----EEIRILEHLrkqdkdNTMNVIHMLENFTFRNH 296
Cdd:cd05621   54 YDVVKVIGRGAFGEV-QLVRHKASQKVyAMKLLSKFEMIKRSDSaffwEERDIMAFA------NSPWVVQLFCAFQDDKY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSMNlyELIkkNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 374
Cdd:cd05621  127 LYMVMEYMPGG--DLV--NLMSNYDVPekWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGH--LKLADFGTCMK 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 375 EHQ----RVYTYIQSRFYRAPEVILG----ARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05621  201 MDEtgmvHCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLFEMLVG 252
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
222-418 2.25e-12

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: 68.49  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFG--QVVKaydHKVHQHV-ALKMVRNEKRFHRQAA----EEIRILE----------HLRKQDKDNTMNV 284
Cdd:cd05601    3 FEVKNVIGRGHFGevQVVK---EKATGDIyAMKVLKKSETLAQEEVsffeEERDIMAkanspwitklQYAFQDSENLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 285 ihmlenftfrnhicMTF----ELLS-MNLYELIkknkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQ 359
Cdd:cd05601   80 --------------MEYhpggDLLSlLSRYDDI-------FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRT 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 360 GRsgIKVIDFGSSCYEHQRvyTYIQSRF------YRAPEVIL------GARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05601  139 GH--IKLADFGSAAKLSSD--KTVTSKMpvgtpdYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYG 205
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
221-421 2.25e-12

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: 67.41  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKmvRNEKRF-----HRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRN 295
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVK--KSKKPFrgpkeRARALREVEAHAALGQHP-----NIVRYYSSWEEGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSM-NLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGssc 373
Cdd:cd13997   74 HLYIQMELCENgSLQDALEELSPISkLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT--CKIGDFG--- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 374 yehqrVYTYIQSRF--------YRAPEVILG-ARYGMPIDMWSLGCILAELLTGYPL 421
Cdd:cd13997  149 -----LATRLETSGdveegdsrYLAPELLNEnYTHLPKADIFSLGVTVYEAATGEPL 200
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
222-415 3.36e-12

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 67.36  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR----NEKRFHRQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHI 297
Cdd:cd08229   26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQifdlMDAKARADCIKEIDLLKQL------NHPNVIKYYASFIEDNEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYELIKKNKFQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 374
Cdd:cd08229  100 NIVLELADAgDLSRMIKHFKKQKRLIPekTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGV--VKLGDLGLGRF 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 375 EHQRV---YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAEL 415
Cdd:cd08229  178 FSSKTtaaHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM 221
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
214-420 3.41e-12

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: 67.37  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 214 PHDHVAYRYEVLKvIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA-EEIRILEHLRKQdkdntmNVIHMLENFT 292
Cdd:cd06658   17 PGDPREYLDSFIK-IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLfNEVVIMRDYHHE------NVVDMYNSYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSMN-LYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGS 371
Cdd:cd06658   90 VGDELWVVMEFLEGGaLTDIVTHTRMNEEQIATV---CLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR--IKLSDFGF 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 372 SCYEHQRV---YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd06658  165 CAQVSKEVpkrKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEP 216
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
222-419 3.56e-12

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: 67.77  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVrNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTF 301
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL-DKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC-YEHQRV 379
Cdd:cd14223   81 ILDLMNGGDLHYHLSQHGvFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH--VRISDLGLACdFSKKKP 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 380 YTYIQSRFYRAPEVIL-GARYGMPIDMWSLGCILAELLTGY 419
Cdd:cd14223  159 HASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGH 199
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
222-420 3.90e-12

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 68.14  E-value: 3.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVvKAYDHKVHQHV-ALKMVRNEKRFHRQAAEEIRILEHLRKQDkdNTMNVIHMLENFTFRNHICMT 300
Cdd:cd05628    3 FESLKVIGRGAFGEV-RLVQKKDTGHVyAMKILRKADMLEKEQVGHIRAERDILVEA--DSLWVVKMFYSFQDKLNLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLS----MNLyeLIKKNKFQGFSLPLVrkFAHSILqCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG------ 370
Cdd:cd05628   80 MEFLPggdmMTL--LMKKDTLTEEETQFY--IAETVL-AIDSIHQLGFIHRDIKPDNLLLDSKGH--VKLSDFGlctglk 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ----SSCYEH----------------------------QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05628  153 kahrTEFYRNlnhslpsdftfqnmnskrkaetwkrnrrQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIG 232

                 ..
gi 153281169 419 YP 420
Cdd:cd05628  233 YP 234
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
228-418 4.85e-12

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 66.53  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKvHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKdntmnvihmLENFT-FRNH---------- 296
Cdd:cd14067    1 LGQGGSGTVIYRARYQ-GQPVAVKRFHIKKCKKRTDGSADTMLKHLRAADA---------MKNFSeFRQEasmlhslqhp 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ------------ICMTFEL-----LSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL---L 356
Cdd:cd14067   71 civyligisihpLCFALELaplgsLNTVLEENHKGSSFMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 357 KQQGRSGIKVIDFGSSCYE-HQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14067  151 DVQEHINIKLSDYGISRQSfHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSG 213
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
222-418 8.14e-12

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: 67.34  E-value: 8.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLenFTFRNHICMTF 301
Cdd:cd05624   74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYA--FQDENYLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 EL-LSMNLYELIkkNKFQGfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGsSCYEHQR 378
Cdd:cd05624  152 DYyVGGDLLTLL--SKFED-KLPedMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGH--IRLADFG-SCLKMND 225
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 379 VYTyIQSRF------YRAPEVILG-----ARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05624  226 DGT-VQSSVavgtpdYISPEILQAmedgmGKYGPECDWWSLGVCMYEMLYG 275
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
222-418 8.57e-12

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: 67.02  E-value: 8.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVvKAYDHKVHQHV-ALKMV-------RNEKRFHrqaAEEIRILEHlrkqdkDNTMNVIHMLENFTF 293
Cdd:cd05596   28 FDVIKVIGRGAFGEV-QLVRHKSTKKVyAMKLLskfemikRSDSAFF---WEERDIMAH------ANSEWIVQLHYAFQD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNHICMTFELLS-------MNLYELIKKnkfqgfslpLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKV 366
Cdd:cd05596   98 DKYLYMVMDYMPggdlvnlMSNYDVPEK---------WARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGH--LKL 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 367 IDFGsSCYEHQ-----RVYTYIQSRFYRAPEVILGAR----YGMPIDMWSLGCILAELLTG 418
Cdd:cd05596  167 ADFG-TCMKMDkdglvRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVG 226
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
222-372 9.36e-12

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: 66.23  E-value: 9.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYD---HKVHQHVALKMVRNEKRFhrqaaeEI----RILEHLRKQDKDNTMNVIHMLENFTFR 294
Cdd:cd13981    2 YVISKELGEGGYASVYLAKDddeQSDGSLVALKVEKPPSIW------EFyicdQLHSRLKNSRLRESISGAHSAHLFQDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTF----ELLsmNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL------KQQGRS-- 362
Cdd:cd13981   76 SILVMDYssqgTLL--DVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicaDWPGEGen 153
                        170
                 ....*....|....*
gi 153281169 363 -----GIKVIDFGSS 372
Cdd:cd13981  154 gwlskGLKLIDFGRS 168
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
222-431 9.97e-12

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 66.44  E-value: 9.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKdnTMNVIHMLENFTFRNHICMTF 301
Cdd:cd05610    6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSK--SPFIVHLYYSLQSANNVYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 E-LLSMNLYELIkkNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQR-- 378
Cdd:cd05610   84 EyLIGGDVKSLL--HIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGH--IKLTDFGLSKVTLNRel 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 ------------------------VYTYIQS-------------------------RF-----YRAPEVILGARYGMPID 404
Cdd:cd05610  160 nmmdilttpsmakpkndysrtpgqVLSLISSlgfntptpyrtpksvrrgaarvegeRIlgtpdYLAPELLLGKPHGPAVD 239
                        250       260
                 ....*....|....*....|....*..
gi 153281169 405 MWSLGCILAELLTGYPllPGEDEGDQL 431
Cdd:cd05610  240 WWALGVCLFEFLTGIP--PFNDETPQQ 264
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
222-418 1.22e-11

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 64.99  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEK-----RFHRQAAEEIRILehLRKQDKDNTMNVIHMLENFTFRNH 296
Cdd:cd14100    2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRvsewgELPNGTRVPMEIV--LLKKVGSGFRGVIRLLDWFERPDS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFEL--LSMNLYELIKKNKfqgfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgRSGIKVIDFGSS 372
Cdd:cd14100   80 FVLVLERpePVQDLFDFITERG----ALPeeLARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLN-TGELKLIDFGSG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 373 CYEHQRVYT-YIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG 418
Cdd:cd14100  155 ALLKDTVYTdFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCG 202
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
222-430 1.34e-11

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: 66.21  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMnVIHMLENFTFRNHICMTF 301
Cdd:cd05618   22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPF-LVGLHSCFQTESRLFFVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMN--LYELIKKNKfqgfsLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYEHQ 377
Cdd:cd05618  101 EYVNGGdlMFHMQRQRK-----LPeeHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH--IKLTDYGM-CKEGL 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 378 R----VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG---YPLLPGEDEGDQ 430
Cdd:cd05618  173 RpgdtTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGrspFDIVGSSDNPDQ 232
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
228-418 1.49e-11

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: 65.66  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAEeIRILEhlrkqdkdNTMNVIHMLENFTFRNHICMTFELL- 304
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIIsrRMEANTQREVAA-LRLCQ--------SHPNIVALHEVLHDQYHTYLVMELLr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQG-RSGIKVIDFGSSCYEHQR---VY 380
Cdd:cd14180   85 GGELLDRIKKKAR--FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdGAVLKVIDFGFARLRPQGsrpLQ 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153281169 381 TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14180  163 TPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSG 200
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
225-417 1.79e-11

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: 65.04  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKA-YD---HKVHQHVALKMVRNEKRFH-RQAAEEIRILEHLRKQDKDNTMNVIHMlenfTFRNHICM 299
Cdd:cd14205    9 LQQLGKGNFGSVEMCrYDplqDNTGEVVAVKKLQHSTEEHlRDFEREIEILKSLQHDNIVKYKGVCYS----AGRRNLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSCYEHQ 377
Cdd:cd14205   85 IMEYLPYgSLRDYLQKHK-ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENR--VKIGDFGlTKVLPQD 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 378 RVYTYIQSR-----FYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd14205  162 KEYYKVKEPgespiFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
214-420 2.29e-11

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: 65.04  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 214 PHDHVAYRYEVLKvIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA-EEIRILEHLRKQdkdntmNVIHMLENFT 292
Cdd:cd06657   15 PGDPRTYLDNFIK-IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHE------NVVEMYNSYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 FRNHICMTFELLSMN-LYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG- 370
Cdd:cd06657   88 VGDELWVVMEFLEGGaLTDIVTHTRMNEEQIAAV---CLAVLKALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGf 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 371 --SSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd06657  163 caQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEP 214
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
227-419 2.38e-11

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: 64.77  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVV---KAYDHKVHqhvALKMVrNEKRFHRQAAEEI----RILEHLRKQDKDNTMnVIHMLENFTFRNHICM 299
Cdd:cd05606    1 IIGRGGFGEVYgcrKADTGKMY---AMKCL-DKKRIKMKQGETLalneRIMLSLVSTGGDCPF-IVCMTYAFQTPDKLCF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELlsMN----LYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSC-Y 374
Cdd:cd05606   76 ILDL--MNggdlHYHLSQHGVF---SEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGH--VRISDLGLACdF 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153281169 375 EHQRVYTYIQSRFYRAPEVIL-GARYGMPIDMWSLGCILAELLTGY 419
Cdd:cd05606  149 SKKKPHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGH 194
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
222-535 2.48e-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: 64.79  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVL--KVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfhrqAAEEIRIleHLRKQDKDNTMNVIHMLEN-FTF----- 293
Cdd:cd14171    6 YEVNwtQKLGTGISGPVRVCVKKSTGERFALKILLDRPK----ARTEVRL--HMMCSGHPNIVQIYDVYANsVQFpgess 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 -RNHICMTFELlsMNLYELIKK-NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGR-SGIKVIDFG 370
Cdd:cd14171   80 pRARLLIVMEL--MEGGELFDRiSQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdAPIKLCDFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 SSCYEHQRVYTYIQSRFYRAPEVILGAR-----------------YGMPIDMWSLGCILAELLTGYPLLPGEdegdqlac 433
Cdd:cd14171  158 FAKVDQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSE-------- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 434 miellgMPSQKLLDASKRaknfvsskgypryctvttlsdgsvvlnggRSRRGKLRGPpeSREWgnalKGCDDPLfLDFLK 513
Cdd:cd14171  230 ------HPSRTITKDMKR-----------------------------KIMTGSYEFP--EEEW----SQISEMA-KDIVR 267
                        330       340
                 ....*....|....*....|..
gi 153281169 514 QCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14171  268 KLLCVDPEERMTIEEVLHHPWL 289
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
228-420 2.79e-11

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: 64.27  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAyDHKVHQH-VALKMVRNE----KRFHRqaaeEIRILEHLRKQDkdntmNVIHMLEN-FTFRNHICMTF 301
Cdd:cd13987    1 LGEGTYGKVLLA-VHKGSGTkMALKFVPKPstklKDFLR----EYNISLELSVHP-----HIIKTYDVaFETEDYYVFAQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 EL-LSMNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSScyehQRVY 380
Cdd:cd13987   71 EYaPYGDLFSIIPPQV--GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLT----RRVG 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 381 TYIQSRF----YRAPEV---ILGARYGM--PIDMWSLGCILAELLTGYP 420
Cdd:cd13987  145 STVKRVSgtipYTAPEVceaKKNEGFVVdpSIDVWAFGVLLFCCLTGNF 193
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
259-418 2.99e-11

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: 63.92  E-value: 2.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 259 FHRQAAEEIRILEHLRKQDKDN-----TMNVIHMLENFTFRNHICMTFeLLSMNLYELIkknkFQGFSLPL--VRKFAHS 331
Cdd:cd14012   38 GKKQIQLLEKELESLKKLRHPNlvsylAFSIERRGRSDGWKVYLLTEY-APGGSLSELL----DSVGSVPLdtARRWTLQ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 332 ILQCLDALHKNRIIHCDLKPENILLKQQGRSGI-KVIDFGSS----CYEHQRVYTYIQSRFYRAPEVILGA-RYGMPIDM 405
Cdd:cd14012  113 LLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIvKLTDYSLGktllDMCSRGSLDEFKQTYWLPPELAQGSkSPTRKTDV 192
                        170
                 ....*....|...
gi 153281169 406 WSLGCILAELLTG 418
Cdd:cd14012  193 WDLGLLFLQMLFG 205
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
220-417 2.99e-11

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: 64.32  E-value: 2.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 220 YRYEVLKVI---GKGSFGQVVKA-YD---HKVHQHVALKMVRNEKR------FHRqaaeEIRILEHLrkqDKDNTMNVIH 286
Cdd:cd05038    1 FEERHLKFIkqlGEGHFGSVELCrYDplgDNTGEQVAVKSLQPSGEeqhmsdFKR----EIEILRTL---DHEYIVKYKG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 287 MLENFTFRNH-ICMTFeLLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIK 365
Cdd:cd05038   74 VCESPGRRSLrLIMEY-LPSGSLRDYLQRHRDQ-IDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDL--VK 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 366 VIDFG-SSCYEHQRVYTYIQSR-----FYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05038  150 ISDFGlAKVLPEDKEYYYVKEPgespiFWYAPECLRESRFSSASDVWSFGVTLYELFT 207
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
330-417 3.73e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 65.42  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 330 HSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRVYTYIQSRF-----YRAPEVILGARYGMPID 404
Cdd:PTZ00267 176 YQIVLALDEVHSRKMMHRDLKSANIFLMPTGI--IKLGDFGFSKQYSDSVSLDVASSFcgtpyYLAPELWERKRYSKKAD 253
                         90
                 ....*....|...
gi 153281169 405 MWSLGCILAELLT 417
Cdd:PTZ00267 254 MWSLGVILYELLT 266
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
221-412 3.74e-11

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 64.20  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKR-----FHR-------QAA---------------EEIRILehl 273
Cdd:cd14200    1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygFPRrppprgsKAAqgeqakplaplervyQEIAIL--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 274 RKQDKDNTMNVIHMLENfTFRNHICMTFELLSMNlyELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPEN 353
Cdd:cd14200   78 KKLDHVNIVKLIEVLDD-PAEDNLYMVFDLLRKG--PVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSN 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 354 ILLKQQGRsgIKVIDFG-SSCYE--HQRVYTYIQSRFYRAPEVILGARY---GMPIDMWSLGCIL 412
Cdd:cd14200  155 LLLGDDGH--VKIADFGvSNQFEgnDALLSSTAGTPAFMAPETLSDSGQsfsGKALDVWAMGVTL 217
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
215-418 4.51e-11

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 64.31  E-value: 4.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 215 HDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKM------VRNEKR--FHRQAAEEIRI---LEHLRkqdkdntmn 283
Cdd:cd14041    1 HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqlnknWRDEKKenYHKHACREYRIhkeLDHPR--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 284 VIHMLENFTF-RNHICMTFELLSMNLYEL-IKKNKFqgfslpLVRKFAHS-ILQCLDALH-----KNRIIHCDLKPENIL 355
Cdd:cd14041   72 IVKLYDYFSLdTDSFCTVLEYCEGNDLDFyLKQHKL------MSEKEARSiIMQIVNALKylneiKPPIIHYDLKPGNIL 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 356 LKQQGRSG-IKVIDFGSSCYEHQRVYTYIQ----------SRFYRAPEV-ILGA---RYGMPIDMWSLGCILAELLTG 418
Cdd:cd14041  146 LVNGTACGeIKITDFGLSKIMDDDSYNSVDgmeltsqgagTYWYLPPECfVVGKeppKISNKVDVWSVGVIFYQCLYG 223
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
221-432 5.71e-11

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: 63.47  E-value: 5.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAA-EEIRIlehlrkQDKDNTMNVIHMLEN--FTFRNHI 297
Cdd:cd13986    1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAmREIEN------YRLFNHPNILRLLDSqiVKEAGGK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM----NLYELIKKNKFQG--FSLPLVRKFAHSILQCLDALHKNRII---HCDLKPENILLKQQGRSGIkvID 368
Cdd:cd13986   75 KEVYLLLPYykrgSLQDEIERRLVKGtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPIL--MD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSCyehqRVYTYIQSR----------------FYRAPE---VILGARYGMPIDMWSLGCILAELLTGY-PLLPGEDEG 428
Cdd:cd13986  153 LGSMN----PARIEIEGRrealalqdwaaehctmPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGEsPFERIFQKG 228

                 ....
gi 153281169 429 DQLA 432
Cdd:cd13986  229 DSLA 232
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
222-418 7.60e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 65.14  E-value: 7.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRN---EKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRN--- 295
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYrglKEREKSQLVIEVNVMRELKHK------NIVRYIDRFLNKAnqk 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169  296 -HICMTF---ELLSMNL---YELIKKNKFQGFsLPLVRKFAHSILQC---LDALHKNRIIHCDLKPENILLKQ------- 358
Cdd:PTZ00266   89 lYILMEFcdaGDLSRNIqkcYKMFGKIEEHAI-VDITRQLLHALAYChnlKDGPNGERVLHRDLKPQNIFLSTgirhigk 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169  359 --------QGRSGIKVIDFGSS--CYEHQRVYTYIQSRFYRAPEVIL--GARYGMPIDMWSLGCILAELLTG 418
Cdd:PTZ00266  168 itaqannlNGRPIAKIGDFGLSknIGIESMAHSCVGTPYYWSPELLLheTKSYDDKSDMWALGCIIYELCSG 239
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
222-456 8.19e-11

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: 64.27  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLenFTFRNHICMTF 301
Cdd:cd05623   74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYA--FQDDNNLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 EL-LSMNLYELIkkNKFQGfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGsSCYEHQR 378
Cdd:cd05623  152 DYyVGGDLLTLL--SKFED-RLPedMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGH--IRLADFG-SCLKLME 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTyIQSRF------YRAPEVILG-----ARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMI---ELLGMPSQk 444
Cdd:cd05623  226 DGT-VQSSVavgtpdYISPEILQAmedgkGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhkERFQFPTQ- 303
                        250
                 ....*....|..
gi 153281169 445 LLDASKRAKNFV 456
Cdd:cd05623  304 VTDVSENAKDLI 315
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
222-418 8.80e-11

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: 62.67  E-value: 8.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRI-LE-HLRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd14102    2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVpLEiVLLKKVGSGFRGVIKLLDWYERPDGFLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFEL--LSMNLYELIKKNKfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgRSG-IKVIDFGSSCYEH 376
Cdd:cd14102   82 VMERpePVKDLFDFITEKG--ALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDL--RTGeLKLIDFGSGALLK 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153281169 377 QRVYT-YIQSRFYRAPEVILGARY-GMPIDMWSLGCILAELLTG 418
Cdd:cd14102  158 DTVYTdFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCG 201
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
221-454 1.17e-10

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: 62.96  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR-NEKRFHRQAAEEIRILEHLRKQDKdntmNVIHMLENFTFRNHIC- 298
Cdd:cd13977    1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcNAPENVELALREFWALSSIQRQHP----NVIQLEECVLQRDGLAq 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 -MTFELLSMNLYELIKKNKFQG---------FSLPLVRKFA-------------------HSILQCLDA----LHKNRII 345
Cdd:cd13977   77 rMSHGSSKSDLYLLLVETSLKGercfdprsaCYLWFVMEFCdggdmneyllsrrpdrqtnTSFMLQLSSalafLHRNQIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 346 HCDLKPENILL-KQQGRSGIKVIDFGSS--C------------YEHQRVYTYIQSRFYRAPEVILGaRYGMPIDMWSLGC 410
Cdd:cd13977  157 HRDLKPDNILIsHKRGEPILKVADFGLSkvCsgsglnpeepanVNKHFLSSACGSDFYMAPEVWEG-HYTAKADIFALGI 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 411 ILAELLTGYPLLPGEDEGDQLACMIE-----------LLGMPSQKLLDASKRAKN 454
Cdd:cd13977  236 IIWAMVERITFRDGETKKELLGTYIQqgkeivplgeaLLENPKLELQIPLKKKKS 290
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
223-435 1.21e-10

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: 62.34  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAydhKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLE--NFTFRNHICmt 300
Cdd:cd14150    3 SMLKRIGTGSFGTVFRG---KWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTrpNFAIITQWC-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 fELLSMNLYELIKKNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLkQQGRSgIKVIDFGSSCYE----- 375
Cdd:cd14150   78 -EGSSLYRHLHVTETRFDTMQLIDV---ARQTAQGMDYLHAKNIIHRDLKSNNIFL-HEGLT-VKIGDFGLATVKtrwsg 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 376 HQRVYTYIQSRFYRAPEVIL---GARYGMPIDMWSLGCILAELLTGypLLPGEDEG--DQLACMI 435
Cdd:cd14150  152 SQQVEQPSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSG--TLPYSNINnrDQIIFMV 214
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
226-418 1.49e-10

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: 61.98  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYdhKVHQHVALKMVRnekrfhRQAAEEI-RILEHLRKQDKDNTM----NVIHMLENFTFRNHICMT 300
Cdd:cd14145   12 EIIGIGGFGKVYRAI--WIGDEVAVKAAR------HDPDEDIsQTIENVRQEAKLFAMlkhpNIIALRGVCLKEPNLCLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELL---SMNlyelikkNKFQGFSLP--LVRKFAHSILQCLDALHKNRI---IHCDLKPENILLKQQGRSG------IKV 366
Cdd:cd14145   84 MEFArggPLN-------RVLSGKRIPpdILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKVENGdlsnkiLKI 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 367 IDFGSSCYEHQRVYTYIQSRF-YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14145  157 TDFGLAREWHRTTKMSAAGTYaWMAPEVIRSSMFSKGSDVWSYGVLLWELLTG 209
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
320-422 1.58e-10

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: 62.18  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 320 FSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGA 397
Cdd:cd05576  108 FYIPeeCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGH--IQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGIS 185
                         90       100
                 ....*....|....*....|....*
gi 153281169 398 RYGMPIDMWSLGCILAELLTGYPLL 422
Cdd:cd05576  186 EETEACDWWSLGALLFELLTGKALV 210
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
221-425 1.69e-10

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 61.78  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHK--VHQHVALKMvrnekrFH--RQAAEEIRILEHLRKQDKDNtmnVIHMLENFTFRNH 296
Cdd:cd14112    4 RFSFGSEIFRGRFSVIVKAVDSTteTDAHCAVKI------FEvsDEASEAVREFESLRTLQHEN---VQRLIAAFKPSNF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSScyeh 376
Cdd:cd14112   75 AYLVMEKLQEDVFTRFSSNDY--YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRA---- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 377 QRVYTYIQ-----SRFYRAPEVILGARYGMP-IDMWSLGCILAELLTGYPLLPGE 425
Cdd:cd14112  149 QKVSKLGKvpvdgDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSE 203
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
219-427 1.81e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 62.97  E-value: 1.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 219 AYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMvrnekrfhrqAAEEIRILEHLRKQDKdNTMNVIHMLENFTFRNHIC 298
Cdd:PHA03209  65 SLGYTVIKTLTPGSEGRVFVATKPGQPDPVVLKI----------GQKGTTLIEAMLLQNV-NHPSVIRMKDTLVSGAITC 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSMNLYELIKKNKFQgfsLPLVRKFA--HSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSScyeh 376
Cdd:PHA03209 134 MVLPHYSSDLYTYLTKRSRP---LPIDQALIieKQILEGLRYLHAQRIIHRDVKTENIFINDV--DQVCIGDLGAA---- 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 377 qrVYTYIQSRFY--------RAPEVILGARYGMPIDMWSLGCILAELLtGYPLLPGEDE 427
Cdd:PHA03209 205 --QFPVVAPAFLglagtvetNAPEVLARDKYNSKADIWSAGIVLFEML-AYPSTIFEDP 260
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
228-463 2.02e-10

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: 61.87  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQV-VKAYD---HKVHQHVALKMVRNEKRFHRQA--AEEIRILEhlrkqdkdntmNVIHmlENFTFRNHIC--- 298
Cdd:cd05079   12 LGEGHFGKVeLCRYDpegDNTGEQVAVKSLKPESGGNHIAdlKKEIEILR-----------NLYH--ENIVKYKGICted 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 --------MTFeLLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG 370
Cdd:cd05079   79 ggngikliMEF-LPSGSLKEYLPRNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ--VKIGDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 --SSCYEHQRVYTYIQSR----FYRAPEVILGARYGMPIDMWSLGCILAELLTgYpllpGEDEGDQLACMIELLGmPSQK 444
Cdd:cd05079  155 ltKAIETDKEYYTVKDDLdspvFWYAPECLIQSKFYIASDVWSFGVTLYELLT-Y----CDSESSPMTLFLKMIG-PTHG 228
                        250
                 ....*....|....*....
gi 153281169 445 LLDASKRAKNFVSSKGYPR 463
Cdd:cd05079  229 QMTVTRLVRVLEEGKRLPR 247
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
222-537 2.05e-10

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 62.37  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVvkaydHKVhQHVALKMVRNEKRFHRQAAEEIR--ILEHLRKQDKDNTMNVIHMLENFTFRNHICM 299
Cdd:cd06649    7 FERISELGAGNGGVV-----TKV-QHKPSGLIMARKLIHLEIKPAIRnqIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKNKfqgfSLP--LVRKFAHSILQCLDAL-HKNRIIHCDLKPENILLKQQGRsgIKVIDFG-SSCY 374
Cdd:cd06649   81 CMEHMDGgSLDQVLKEAK----RIPeeILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGE--IKLCDFGvSGQL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTG-YPLLPGEDEgdqlacmiELLGMPSQKLLDASKRAK 453
Cdd:cd06649  155 IDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGrYPIPPPDAK--------ELEAIFGRPVVDGEEGEP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 454 NFVSSKGYPryctvttlsDGSVVLNGGRSRRGKL----------RGPPESREwgnalKGCDDPLFLDFLKQCLEWDPAVR 523
Cdd:cd06649  227 HSISPRPRP---------PGRPVSGHGMDSRPAMaifelldyivNEPPPKLP-----NGVFTPDFQEFVNKCLIKNPAER 292
                        330
                 ....*....|....
gi 153281169 524 MTPGQALRHPWLRR 537
Cdd:cd06649  293 ADLKMLMNHTFIKR 306
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
228-426 2.12e-10

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: 62.20  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALK------MVRNEKRFHRQAAEEIrilehLRKQDKDNTMNVIHMleNFTFRNHICMTF 301
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKvlskkvIVAKKEVAHTIGERNI-----LVRTALDESPFIVGL--KFSFQTPTDLYL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYELIKKNKFQG-FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS---CYEHQ 377
Cdd:cd05586   74 VTDYMSGGELFWHLQKEGrFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGH--IALCDFGLSkadLTDNK 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 378 RVYTYIQSRFYRAPEVILGAR-YGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:cd05586  152 TTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAED 201
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
228-423 2.43e-10

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 61.35  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMvrnEKRFHRQAA--EEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKE---LKRFDEQRSflKEVKLMRRLSHP------NILRFIGVCVKDNKLNFITEYVN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQ--GRSGIkVIDFG---------SSCY 374
Cdd:cd14065   72 GGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREAnrGRNAV-VADFGlarempdekTKKP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 375 EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLP 423
Cdd:cd14065  151 DRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADP 199
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
222-418 2.49e-10

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: 61.98  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQV--VK-AYDHKVHqhvALKMVRNEKRFHRqaAEEIRILEH---LRKQDKDNTMNvIHmlenFTFRN 295
Cdd:cd05597    3 FEILKVIGRGAFGEVavVKlKSTEKVY---AMKILNKWEMLKR--AETACFREErdvLVNGDRRWITK-LH----YAFQD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HicmTFELLSMNLYE----LIKKNKFQGfSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd05597   73 E---NYLYLVMDYYCggdlLTLLSKFED-RLPeeMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGH--IRLADF 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 370 GsSCYEHQRVYTyIQSRF------YRAPEvILGA------RYGMPIDMWSLGCILAELLTG 418
Cdd:cd05597  147 G-SCLKLREDGT-VQSSVavgtpdYISPE-ILQAmedgkgRYGPECDWWSLGVCMYEMLYG 204
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
221-418 3.19e-10

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: 61.20  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKmVRNEKRFHRQAAEEIRILEHLrkQDKDNTMNVIHMLENFTFrNHICMt 300
Cdd:cd14130    1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKL--QGKDHVCRFIGCGRNEKF-NYVVM- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 fELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIK--VIDFGSScyehqR 378
Cdd:cd14130   76 -QLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLA-----R 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 379 VYTYIQSRFyRAPEVILGAR---------------YGMPIDMWSLGCILAELLTG 418
Cdd:cd14130  150 QYTNTTGEV-RPPRNVAGFRgtvryasvnahknreMGRHDDLWSLFYMLVEFAVG 203
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
223-457 3.92e-10

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: 60.83  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAYdhkVHQHVALKMVrnekrfhrqaaeEIRILEhlrkQDKDNTMNVIHMLENFTFRNHI----- 297
Cdd:cd14063    3 EIKEVIGKGRFGRVHRGR---WHGDVAIKLL------------NIDYLN----EEQLEAFKEEVAAYKNTRHDNLvlfmg 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 -CMTFELLSM--------NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkQQGRsgIKVID 368
Cdd:cd14063   64 aCMDPPHLAIvtslckgrTLYSLIHERK-EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGR--VVITD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 369 FGSSC-----YEHQRVYTYIQSR---FYRAPEVILGARYGMPI----------DMWSLGCILAELLTG-YPL--LPGEDE 427
Cdd:cd14063  140 FGLFSlsgllQPGRREDTLVIPNgwlCYLAPEIIRALSPDLDFeeslpftkasDVYAFGTVWYELLAGrWPFkeQPAESI 219
                        250       260       270
                 ....*....|....*....|....*....|.
gi 153281169 428 GDQLACmiellGM-PSQKLLDASKRAKNFVS 457
Cdd:cd14063  220 IWQVGC-----GKkQSLSQLDIGREVKDILM 245
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
215-418 4.80e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 60.84  E-value: 4.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 215 HDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKM------VRNEKR--FHRQAAEEIRI---LEHLRkqdkdntmn 283
Cdd:cd14040    1 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqlnksWRDEKKenYHKHACREYRIhkeLDHPR--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 284 VIHMLENFTF-RNHICMTFELLSMNLYEL-IKKNKFqgfslpLVRKFAHSI-LQCLDALH-----KNRIIHCDLKPENIL 355
Cdd:cd14040   72 IVKLYDYFSLdTDTFCTVLEYCEGNDLDFyLKQHKL------MSEKEARSIvMQIVNALRylneiKPPIIHYDLKPGNIL 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 356 LKQQGRSG-IKVIDFGSSCYEHQRVYTY---------IQSRFYRAPEV-ILGA---RYGMPIDMWSLGCILAELLTG 418
Cdd:cd14040  146 LVDGTACGeIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPECfVVGKeppKISNKVDVWSVGVIFFQCLYG 222
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
218-420 4.88e-10

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 60.41  E-value: 4.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEkrfHRQAAEeIRILEHLRKQDKDNTMNVIHMLENFtfrnHI 297
Cdd:cd13995    2 LTYRNIGSDFIPRGAFGKVYLAQDTKTKKRMACKLIPVE---QFKPSD-VEIQACFRHENIAELYGALLWEETV----HL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKFQGFSLPLVRKfahSILQCLDALHKNRIIHCDLKPENILLKQqgrSGIKVIDFGSSCYEHQ 377
Cdd:cd13995   74 FMEAGEGGSVLEKLESCGPMREFEIIWVTK---HVLKGLDFLHSKNIIHHDIKPSNIVFMS---TKAVLVDFGLSVQMTE 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153281169 378 RVYTYIQSR---FYRAPEVILGARYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd13995  148 DVYVPKDLRgteIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSP 193
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
226-442 5.85e-10

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: 60.42  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKvhQHVALKMVRNEKRFHRQAAEEIRILEHLRKqdkDNTMNVI----HMLENFTFRNHICMTF 301
Cdd:cd14053    1 EIKARGRFGAVWKAQYLN--RLVAVKIFPLQEKQSWLTEREIYSLPGMKH---ENILQFIgaekHGESLEAEYWLITEFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSmnLYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNR----------IIHCDLKPENILLKQQGRSGIKviDFGS 371
Cdd:cd14053   76 ERGS--LCDYLKGNVI---SWNELCKIAESMARGLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACIA--DFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 372 SC-YE--------HQRVYTyiqsRFYRAPEVILGA---------RygmpIDMWSLGCILAELLTGYPLLPGEDEGDQLAC 433
Cdd:cd14053  149 ALkFEpgkscgdtHGQVGT----RRYMAPEVLEGAinftrdaflR----IDMYAMGLVLWELLSRCSVHDGPVDEYQLPF 220

                 ....*....
gi 153281169 434 MIELLGMPS 442
Cdd:cd14053  221 EEEVGQHPT 229
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
225-420 6.32e-10

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: 61.18  E-value: 6.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRIlEHLRKQDKDNTMnVIHMLENFTFRNHICMTFELL 304
Cdd:cd05626    6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKA-ERDILAEADNEW-VVKLYYSFQDKDNLYFVMDYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 S----MNLyeLIKknkFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---------- 370
Cdd:cd05626   84 PggdmMSL--LIR---MEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGH--IKLTDFGlctgfrwthn 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ------------------------SSCY--------------EHQR--VYTYIQSRFYRAPEVILGARYGMPIDMWSLGC 410
Cdd:cd05626  157 skyyqkgshirqdsmepsdlwddvSNCRcgdrlktleqratkQHQRclAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGV 236
                        250
                 ....*....|
gi 153281169 411 ILAELLTGYP 420
Cdd:cd05626  237 ILFEMLVGQP 246
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
228-418 1.45e-09

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: 59.06  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEkRFHrqaAEEI---------RILEhLRKQDKDNTMNVIHMlenftfrnhic 298
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLE-VFR---AEELmacagltspRVVP-LYGAVREGPWVNIFM----------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 mtfELLSM-NLYELIKknkfQGFSLP--LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIkVIDFGSSCYE 375
Cdd:cd13991   78 ---DLKEGgSLGQLIK----EQGCLPedRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF-LCDFGHAECL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 376 H-----QRVYT--YIQ-SRFYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd13991  150 DpdglgKSLFTgdYIPgTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNG 200
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
326-418 1.55e-09

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: 59.74  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 326 RKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSsCYEHQR----VYTYIQSRFYRAPEVILGARYGM 401
Cdd:cd05588   99 RFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH--IKLTDYGM-CKEGLRpgdtTSTFCGTPNYIAPEILRGEDYGF 175
                         90
                 ....*....|....*..
gi 153281169 402 PIDMWSLGCILAELLTG 418
Cdd:cd05588  176 SVDWWALGVLMFEMLAG 192
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
227-418 1.66e-09

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: 58.90  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKvhQHVALKMVRNEKRFHRQAAEeirilEHLRKQDKDNTM----NVIHmLENFTFRN-HICMTF 301
Cdd:cd14146    1 IIGVGGFGKVYRATWKG--QEVAVKAARQDPDEDIKATA-----ESVRQEAKLFSMlrhpNIIK-LEGVCLEEpNLCLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELL---SMNlYELIKKNKFQGFS----LP--LVRKFAHSILQCLDALHKNR---IIHCDLKPENILLKQQ------GRSG 363
Cdd:cd14146   73 EFArggTLN-RALAAANAAPGPRrarrIPphILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddiCNKT 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 364 IKVIDFGSSCYEHQRVYTYIQSRF-YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14146  152 LKITDFGLAREWHRTTKMSAAGTYaWMAPEVIKSSLFSKGSDIWSYGVLLWELLTG 207
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
229-417 1.87e-09

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: 58.43  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 229 GKGSFGQVVKAYDHKVHQHVALK-MVRNEKRfhrqaAEEIRILEHlrkqdkdntMNVIHMLENFTFRNHICMTFELLSM- 306
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKkLLKIEKE-----AEILSVLSH---------RNIIQFYGAILEAPNYGIVTEYASYg 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKN---RIIHCDLKPENILLKQQGRsgIKVIDFGSS-CYEHQRVYTY 382
Cdd:cd14060   68 SLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGV--LKICDFGASrFHSHTTHMSL 145
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153281169 383 IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd14060  146 VGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLT 180
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
203-423 1.89e-09

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: 59.04  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 203 YDDDQGSYV---QVPHDHV----AYRYEVLKVIGKGSFGQVVKAYDHKVHQ-----HVALKMVRNEKRFHRQAA--EEIR 268
Cdd:cd05055   11 INGNEYVYIdptQLPYDLKwefpRNNLSFGKTLGAGAFGKVVEATAYGLSKsdavmKVAVKMLKPTAHSSEREAlmSELK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 269 ILEHLrkqdkDNTMNVIHMLENFTFRNHICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHC 347
Cdd:cd05055   91 IMSHL-----GNHENIVNLLGACTIGGPILVITEYCCYgDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 348 DLKPENILLkQQGRSgIKVIDFG-SSCYEHQRVYTYIQSRF----YRAPEVILGARYGMPIDMWSLGCILAEL----LTG 418
Cdd:cd05055  166 DLAARNVLL-THGKI-VKICDFGlARDIMNDSNYVVKGNARlpvkWMAPESIFNCVYTFESDVWSYGILLWEIfslgSNP 243

                 ....*
gi 153281169 419 YPLLP 423
Cdd:cd05055  244 YPGMP 248
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
222-416 2.15e-09

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: 58.67  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMV---RNEKRFHRQAAEEIRILEHLrkqdkdNTMNVI--HM--LENFTFR 294
Cdd:cd14049    8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKKIlikKVTKRDCMKVLREVKVLAGL------QHPNIVgyHTawMEHVQLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHICMTfeLLSMNLYELI----KKNKFQGFS--------LPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRS 362
Cdd:cd14049   82 LYIQMQ--LCELSLWDWIvernKRPCEEEFKsapytpvdVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 363 gIKVIDFGSSC------------YEHQRVYTY---IQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14049  160 -VRIGDFGLACpdilqdgndsttMSRLNGLTHtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
325-535 2.24e-09

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: 58.29  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 325 VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgrSGIKVIDFG-SSCYEHQRVYTYIQ-SRFYRAPEVILGARYGMP 402
Cdd:cd14109  101 VAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD---DKLKLADFGqSRRLLRGKLTTLIYgSPEFVSPEIVNSYPVTLA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 403 IDMWSLGCILAELLTGYPLLPGEDEGDqlacmiellgmpsqklldaskraknfvsskgyprycTVTTLSDGSVVLnggrs 482
Cdd:cd14109  178 TDMWSVGVLTYVLLGGISPFLGDNDRE------------------------------------TLTNVRSGKWSF----- 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 483 rrgklrgppESREWGNAlkgCDDPlfLDFLKQCLEWDPAVRMTPGQALRHPWL 535
Cdd:cd14109  217 ---------DSSPLGNI---SDDA--RDFIKKLLVYIPESRLTVDEALNHPWF 255
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
225-418 2.39e-09

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: 58.23  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYdHKVHQHVALKMVR----NEKRFhrqaAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd05059    9 LKELGSGQFGVVHLGK-WRGKIDVAIKMIKegsmSEDDF----IEEAKVMMKLSHP------KLVQLYGVCTKQRPIFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMN-LYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRV 379
Cdd:cd05059   78 TEYMANGcLLNYLRERR-GKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNV--VKVSDFGLARYVLDDE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 380 YTYIQ-SRF---YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd05059  155 YTSSVgTKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSE 197
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
227-418 2.45e-09

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 58.42  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKvhQHVALKMVRNEKRFhRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMtfELLSM 306
Cdd:cd14068    1 LLGDGGFGSVYRAVYRG--EDVAVKIFNKHTSF-RLLRQELVVLSHLHHP------SLVALLAAGTAPRMLVM--ELAPK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIkknkFQGFSLPLVRKFAHSI-LQCLDAL---HKNRIIHCDLKPENIL---LKQQGRSGIKVIDFGSSCY-EHQR 378
Cdd:cd14068   70 GSLDAL----LQQDNASLTRTLQHRIaLHVADGLrylHSAMIIYRDLKPHNVLlftLYPNCAIIAKIADYGIAQYcCRMG 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 379 VYTYIQSRFYRAPEVILG-ARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14068  146 IKTSEGTPGFRAPEVARGnVIYNQQADVYSFGLLLYDILTC 186
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
228-418 2.96e-09

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: 58.66  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKmVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHI-----CMTFE 302
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVK-VFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRHKVlvmelCPCGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-----NLYELiKKNKFQGFSLPLVRKFAHsilqcldaLHKNRIIHCDLKPENIL--LKQQGRSGIKVIDFGSS--C 373
Cdd:cd13988   80 LYTVleepsNAYGL-PESEFLIVLRDVVAGMNH--------LRENGIVHRDIKPGNIMrvIGEDGQSVYKLTDFGAAreL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 374 YEHQRVYTYIQSRFYRAPEV----IL----GARYGMPIDMWSLGCILAELLTG 418
Cdd:cd13988  151 EDDEQFVSLYGTEEYLHPDMyeraVLrkdhQKKYGATVDLWSIGVTFYHAATG 203
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
231-418 3.47e-09

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: 57.89  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 231 GSFGQVVKAYdHKVHQHVALKMV-RNEKRFHRQAA--EEIRILEHLRKQDKDNTMNVIhmLENFTFRnhicMTFELLSM- 306
Cdd:cd14027    4 GGFGKVSLCF-HRTQGLVVLKTVyTGPNCIEHNEAllEEGKMMNRLRHSRVVKLLGVI--LEEGKYS----LVMEYMEKg 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKnkfqgFSLPLVRK--FAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRVYTYIQ 384
Cdd:cd14027   77 NLMHVLKK-----VSVPLSVKgrIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFH--IKIADLGLASFKMWSKLTKEE 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 385 SR----------------FYRAPEVI--LGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14027  150 HNeqrevdgtakknagtlYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFAN 201
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
198-545 3.50e-09

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 58.68  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 198 PNNGGYDDDQGSYVQVPHDHVAYRYEVL---KVIGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAEEIRILEH 272
Cdd:PLN00034  49 PPSSSSSSSSSSSASGSAPSAAKSLSELervNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICREIEILRD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 273 LrkqdkdNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSlplvrKFAHSILQCLDALHKNRIIHCDLKPE 352
Cdd:PLN00034 129 V------NHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLA-----DVARQILSGIAYLHRRHIVHRDIKPS 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 353 NILLKQQGRsgIKVIDFGSSCYEHQRV---YTYIQSRFYRAPEVI-----LGARYGMPIDMWSLGCILAELLTG-YPLLP 423
Cdd:PLN00034 198 NLLINSAKN--VKIADFGVSRILAQTMdpcNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGrFPFGV 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 424 GEdEGDQLACMiellgmpsqklldaskraknfvsskgypryCTVtTLSDgsvvlnggrsrrgklrgPPE-----SREwgn 498
Cdd:PLN00034 276 GR-QGDWASLM------------------------------CAI-CMSQ-----------------PPEapataSRE--- 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 499 alkgcddplFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRLPKPPTG 545
Cdd:PLN00034 304 ---------FRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQG 341
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
222-421 4.19e-09

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: 57.62  E-value: 4.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTF 301
Cdd:cd14110    5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHP------RIAQLHSAYLSPRHLVLIE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMN--LYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIKVIDFGSS-CYEHQR 378
Cdd:cd14110   79 ELCSGPelLYNLAERNSY---SEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMII--TEKNLLKIVDLGNAqPFNQGK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 379 VYTYIQSRFY---RAPEVILGARYGMPIDMWSLGCILAELLTG-YPL 421
Cdd:cd14110  154 VLMTDKKGDYvetMAPELLEGQGAGPQTDIWAIGVTAFIMLSAdYPV 200
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
330-418 4.71e-09

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 57.80  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 330 HSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSCY---EHQRVYTYIQSRFYRAPEVILGARY-GMPIDM 405
Cdd:cd13974  139 YDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRK-ITITNFCLGKHlvsEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDM 217
                         90
                 ....*....|...
gi 153281169 406 WSLGCILAELLTG 418
Cdd:cd13974  218 WALGVVLFTMLYG 230
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
221-418 5.44e-09

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: 57.37  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKmVRNEKRFHRQAAEEIRILEHLrkQDKDNTMNVIHMLENFTFrNHICMt 300
Cdd:cd14129    1 RWKVLRKIGGGGFGEIYDALDLLTRENVALK-VESAQQPKQVLKMEVAVLKKL--QGKDHVCRFIGCGRNDRF-NYVVM- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 fELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRsgikvidFGSSCYEHQRVY 380
Cdd:cd14129   76 -QLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM---GR-------FPSTCRKCYMLD 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153281169 381 TYIQSRF------YRAPEVILGAR---------------YGMPIDMWSLGCILAELLTG 418
Cdd:cd14129  145 FGLARQFtnscgdVRPPRAVAGFRgtvryasinahrnreMGRHDDLWSLFYMLVEFVVG 203
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
228-416 6.17e-09

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 57.27  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLrkqDKDNTMNVIHMLENFTFRNHIcmTFELLSM 306
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKeLIRFDEETQRTFLKEVKVMRCL---EHPNVLKFIGVLYKDKRLNFI--TEYIKGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQgfsLPLVRK--FAHSILQCLDALHKNRIIHCDLKPENILLKQQGrsGIKVIDFG--------SSCYEH 376
Cdd:cd14221   76 TLRGIIKSMDSH---YPWSQRvsFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENK--SVVVADFGlarlmvdeKTQPEG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 377 ---------QRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14221  151 lrslkkpdrKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
223-426 6.49e-09

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 56.98  E-value: 6.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAyDHKvHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFE 302
Cdd:cd05039    9 KLGELIGKGEFGDVMLG-DYR-GQKVAVKCLKDDSTAAQAFLAEASVMTTLRHP------NLVQLLGVVLEGNGLYIVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFG---SSCYEHQr 378
Cdd:cd05039   81 YMAKgSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVA--KVSDFGlakEASSNQD- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 379 vytyiQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGED 426
Cdd:cd05039  158 -----GGKLpikWTAPEALREKKFSTKSDVWSFGILLWEIYSfgrvPYPRIPLKD 207
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
228-418 7.00e-09

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: 57.35  E-value: 7.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAydhKVHQHVALKMV-------------RNEKRFHRQAaEEIRILEHLRKQDKDNTMNVIHMLENFTFR 294
Cdd:cd14149   20 IGSGSFGTVYKG---KWHGDVAVKILkvvdptpeqfqafRNEVAVLRKT-RHVNILLFMGYMTKDNLAIVTQWCEGSSLY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 295 NHIcmtfellsmnlyeLIKKNKFQGFSLPlvrKFAHSILQCLDALHKNRIIHCDLKPENILLkQQGRSgIKVIDFGSSCY 374
Cdd:cd14149   96 KHL-------------HVQETKFQMFQLI---DIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLT-VKIGDFGLATV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 375 E-----HQRVYTYIQSRFYRAPEVIL---GARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14149  158 KsrwsgSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTG 209
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
228-436 1.09e-08

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: 56.31  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEeirILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSM- 306
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKA---LLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKnKFQGFSLPLVRKFAHSILQCLDALH--KNRIIHCDLKPENILLKQQGRsgIKVIDFGSScyehqRVYTYIQ 384
Cdd:cd13978   78 SLKSLLER-EIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFH--VKISDFGLS-----KLGMKSI 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 385 SR-------------FYRAPEVI--LGARYGMPIDMWSLGCILAELLTGYplLPGEDEGDQLACMIE 436
Cdd:cd13978  150 SAnrrrgtenlggtpIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRK--EPFENAINPLLIMQI 214
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
228-420 1.79e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 55.78  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVAL------KMVRNEKRFHRQAAEEIRILEHlrkqdkdntMNVIHMLENF--TFRNHICM 299
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVAWcelqtrKLSKGERQRFSEEVEMLKGLQH---------PNIVRFYDSWksTVRGHKCI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TF--ELLSMNLYELIKKnKFQGFSLPLVRKFAHSILQCLDALHKNR--IIHCDLKPENILLkqQGRSG-IKVIDFGSSCY 374
Cdd:cd14033   80 ILvtELMTSGTLKTYLK-RFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFI--TGPTGsVKIGDLGLATL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 375 EHQR-VYTYIQSRFYRAPEvILGARYGMPIDMWSLG-CILAELLTGYP 420
Cdd:cd14033  157 KRASfAKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGmCILEMATSEYP 203
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
228-417 2.21e-08

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: 55.34  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYdHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS-- 305
Cdd:cd05112   12 IGSGQFGLVHLGY-WLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHP------KLVQLYGVCLEQAPICLVFEFMEhg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 -MNLYELIKKNKFQGFSLplvrkfahsILQCLDA------LHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQR 378
Cdd:cd05112   85 cLSDYLRTQRGLFSAETL---------LGMCLDVcegmayLEEASVIHRDLAARNCLVGEN--QVVKVSDFGMTRFVLDD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 379 VYTYIQ-SRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05112  154 QYTSSTgTKFpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFS 196
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
226-433 2.24e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 56.13  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQH-------VALKMVRNEKRfHRQAAEEIRILEHLRKQDKDNtmNVIHMLENFTFRNHIC 298
Cdd:cd05099   18 KPLGEGCFGQVVRAEAYGIDKSrpdqtvtVAVKMLKDNAT-DKDLADLISEMELMKLIGKHK--NIINLLGVCTQEGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKFQG--------------FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSG 363
Cdd:cd05099   95 VIVEYAAKgNLREFLRARRPPGpdytfditkvpeeqLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTED--NV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 364 IKVIDFGSSCYEHQRVYtYIQSRFYR------APEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGED------E 427
Cdd:cd05099  173 MKIADFGLARGVHDIDY-YKKTSNGRlpvkwmAPEALFDRVYTHQSDVWSFGILMWEIFTlggsPYPGIPVEElfkllrE 251

                 ....*.
gi 153281169 428 GDQLAC 433
Cdd:cd05099  252 GHRMDK 257
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
212-441 2.80e-08

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: 55.43  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 212 QVPHDHVayryEVLKVIGKGSFGQVVKAYDHKVHQhVALKMVRNEKRFHRQAAEEIRILEHLrKQDKdntmnVIHMLENF 291
Cdd:cd05072    3 EIPRESI----KLVKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSVQAFLEEANLMKTL-QHDK-----LVRLYAVV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFG 370
Cdd:cd05072   72 TKEEPIYIITEYMAKgSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMC--KIADFG 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 371 SSCYEHQRVYTYIQ-SRF---YRAPEVILGARYGMPIDMWSLGCILAELLT-GYPLLPGEDEGDQLACMIELLGMP 441
Cdd:cd05072  150 LARVIEDNEYTAREgAKFpikWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGYRMP 225
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
218-416 3.36e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 56.01  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 218 VAYRYEVLKVIGKGSFGQV--VKAYDHKVHQHVALKMVRNEKRFHRqaaeEIRILEHLrkqdkdNTMNVIHMLENFTFRN 295
Cdd:PHA03207  90 VRMQYNILSSLTPGSEGEVfvCTKHGDEQRKKVIVKAVTGGKTPGR----EIDILKTI------SHRAIINLIHAYRWKS 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSMNLYELIKKNKfqgfSLPLVRKFA--HSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKviDFGSSC 373
Cdd:PHA03207 160 TVCMVMPKYKCDLFTYVDRSG----PLPLEQAITiqRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLG--DFGAAC 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 374 Y--EHQ---RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:PHA03207 234 KldAHPdtpQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMS 281
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
227-418 3.93e-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: 54.71  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKvhQHVALKMVRNE-KRFHRQAAE----EIRILEHLRKQdkdntmNVIHMLENFTFRNHICmtf 301
Cdd:cd14061    1 VIGVGGFGKVYRGIWRG--EEVAVKAARQDpDEDISVTLEnvrqEARLFWMLRHP------NIIALRGVCLQPPNLC--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 elLSMNLYELIKKNK-FQGFSLPLVRKF--AHSILQCLDALHKNR---IIHCDLKPENILLKQQGRSG------IKVIDF 369
Cdd:cd14061   70 --LVMEYARGGALNRvLAGRKIPPHVLVdwAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEdlenktLKITDF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 370 GSScYEHQRVY------TYIqsrfYRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14061  148 GLA-REWHKTTrmsaagTYA----WMAPEVIKSSTFSKASDVWSYGVLLWELLTG 197
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
226-417 4.30e-08

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: 54.49  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAydHKVHQHVALKMVRNEkrFHRQA-AEEIRILEHLRKQDKDNTMNVIhmlenftFRNHICMTFELL 304
Cdd:cd05083   12 EIIGEGEFGAVLQG--EYMGQKVAVKNIKCD--VTAQAfLEETAVMTKLQHKNLVRLLGVI-------LHNGLYIVMELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFGSSCYEHQRVYTYI 383
Cdd:cd05083   81 SKgNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVA--KISDFGLAKVGSMGVDNSR 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 153281169 384 QSRFYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05083  159 LPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFS 192
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
228-416 4.72e-08

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 54.56  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAyDHKVHQHVAL--KMVRNEKRFHRQAAEEIRILehlRKQDKDNTMNVIHMLenftfrnhicmtFELLS 305
Cdd:cd14222    1 LGKGFFGQAIKV-THKATGKVMVmkELIRCDEETQKTFLTEVKVM---RSLDHPNVLKFIGVL------------YKDKR 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLY-ELIKKNKFQGF-----SLPLVRK--FAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCY--- 374
Cdd:cd14222   65 LNLLtEFIEGGTLKDFlraddPFPWQQKvsFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKT--VVVADFGLSRLive 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 375 --------------------EHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14222  143 ekkkpppdkpttkkrtlrknDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
228-420 5.26e-08

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 54.37  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNE--KRFHRQAAEEIRILehlrKQ-DKDNTMNVIHMLenfTFRNHICMTFELL 304
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETlpPDLKRKFLQEARIL----KQyDHPNIVKLIGVC---VQKQPIMIVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SM-NLYELIKKNKFQgfsLPlVRKFAHsilQCLDA------LHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQ 377
Cdd:cd05041   76 PGgSLLTFLRKKGAR---LT-VKQLLQ---MCLDAaagmeyLESKNCIHRDLAARNCLVGENNV--LKISDFGMSREEED 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 378 RVYTyIQSRF------YRAPEVILGARYGMPIDMWSLGCILAELLTG----YP 420
Cdd:cd05041  147 GEYT-VSDGLkqipikWTAPEALNYGRYTSESDVWSFGILLWEIFSLgatpYP 198
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
222-416 6.57e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 54.11  E-value: 6.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR--NEKRFHRQAAEEIRILEHLR-------------------KQDKDN 280
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRlpNNELAREKVLREVRALAKLDhpgivryfnawlerppegwQEKMDE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 281 TMNVIHM-------LENFTFRNHICMTFELLSMnlyelikKNKFQgfslplvrkfahSILQCLDALHKNRIIHCDLKPEN 353
Cdd:cd14048   88 VYLYIQMqlcrkenLKDWMNRRCTMESRELFVC-------LNIFK------------QIASAVEYLHSKGLIHRDLKPSN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 354 ILLKQQGRsgIKVIDFG-------------------SSCYEHQRVYTyiqsRFYRAPEVILGARYGMPIDMWSLGCILAE 414
Cdd:cd14048  149 VFFSLDDV--VKVGDFGlvtamdqgepeqtvltpmpAYAKHTGQVGT----RLYMSPEQIHGNQYSEKVDIFALGLILFE 222

                 ..
gi 153281169 415 LL 416
Cdd:cd14048  223 LI 224
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
227-420 7.51e-08

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: 53.89  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHK--VHQHVALKMVRN--EKRFHRQAAEEIRILEHLRKQdkDNTMNVIHMLENftfRNHICMTFE 302
Cdd:cd05047    2 VIGEGNFGQVLKARIKKdgLRMDAAIKRMKEyaSKDDHRDFAGELEVLCKLGHH--PNIINLLGACEH---RGYLYLAIE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-NLYELIKKNKF--------------QGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVI 367
Cdd:cd05047   77 YAPHgNLLDFLRKSRVletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA--KIA 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 368 DFGSSCYEHqrvyTYIQSRFYRAP------EVILGARYGMPIDMWSLGCILAEL--LTGYP 420
Cdd:cd05047  155 DFGLSRGQE----VYVKKTMGRLPvrwmaiESLNYSVYTTNSDVWSYGVLLWEIvsLGGTP 211
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
225-423 8.33e-08

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: 53.92  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKA-----YDHKVHQHVALKMVRNEKRFHRQA--AEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd05048   10 LEELGEGAFGKVYKGellgpSSEESAISVAIKTLKENASPKTQQdfRREAELMSDLQHP------NIVCLLGVCTKEQPQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSM-NLYE-LIKKNKFQGFSLPLVRKFAHSILQCLDALH-------------KNRIIHCDLKPENILLKQqgRS 362
Cdd:cd05048   84 CMLFEYMAHgDLHEfLVRHSPHSDVGVSSDDDGTASSLDQSDFLHiaiqiaagmeylsSHHYVHRDLAARNCLVGD--GL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 363 GIKVIDFGSS--CYEHQrvYTYIQSRF-----YRAPEVILGARYGMPIDMWSLGCILAELLTgYPLLP 423
Cdd:cd05048  162 TVKISDFGLSrdIYSSD--YYRVQSKSllpvrWMPPEAILYGKFTTESDVWSFGVVLWEIFS-YGLQP 226
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
219-426 1.31e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 54.49  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 219 AYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVR----NEKRFHRQAAEEIRIL-----------EHLRKQDKDNTMN 283
Cdd:PTZ00283  31 AKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDmegmSEADKNRAQAEVCCLLncdffsivkchEDFAKKDPRNPEN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 284 VIHMLENFTFRNhicmtfellSMNLYELIKKNKFQGfslplvRKFAHS-----ILQCLDALH---KNRIIHCDLKPENIL 355
Cdd:PTZ00283 111 VLMIALVLDYAN---------AGDLRQEIKSRAKTN------RTFREHeagllFIQVLLAVHhvhSKHMIHRDIKSANIL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 356 LKQQGRsgIKVIDFGSSCYEHQRVY-----TYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGED 426
Cdd:PTZ00283 176 LCSNGL--VKLGDFGFSKMYAATVSddvgrTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGEN 249
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
283-446 1.55e-07

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: 53.09  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 283 NVIHMLENFTFRNHicmtfELLSMNLYELIKKnkfqgfslplvrkfaHSILQCLDAL---HKN-RIIHCDLKPENILLKQ 358
Cdd:cd14011   91 NVLGERDNMPSPPP-----ELQDYKLYDVEIK---------------YGLLQISEALsflHNDvKLVHGNICPESVVINS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 359 QGRSgiKVIDFGSSCYEHQRVYTYIQSRFYR--------------APEVILGARYGMPIDMWSLGCILAELL-TGYPLLP 423
Cdd:cd14011  151 NGEW--KLAGFDFCISSEQATDQFPYFREYDpnlpplaqpnlnylAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFD 228
                        170       180
                 ....*....|....*....|...
gi 153281169 424 GEDEGDQLACMIELLGMPSQKLL 446
Cdd:cd14011  229 CVNNLLSYKKNSNQLRQLSLSLL 251
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
225-420 1.65e-07

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 53.51  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRIlEHLRKQDKDNTMnVIHMLENFTFRNHICMTFELL 304
Cdd:cd05625    6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKA-ERDILAEADNEW-VVRLYYSFQDKDNLYFVMDYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 S----MNLyeLIKKNKFQGfslPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG---------- 370
Cdd:cd05625   84 PggdmMSL--LIRMGVFPE---DLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH--IKLTDFGlctgfrwthd 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 371 ------------------------SSC--------------YEHQR--VYTYIQSRFYRAPEVILGARYGMPIDMWSLGC 410
Cdd:cd05625  157 skyyqsgdhlrqdsmdfsnewgdpENCrcgdrlkplerraaRQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGV 236
                        250
                 ....*....|
gi 153281169 411 ILAELLTGYP 420
Cdd:cd05625  237 ILFEMLVGQP 246
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
228-416 1.95e-07

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 52.48  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMvrNEKRFHR-QAAEEIRILEHLRKQDKDNTMNV------IHMLENFtfrnhicmt 300
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM--NTLSSNRaNMLREVQLMNRLSHPNILRFMGVcvhqgqLHALTEY--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 feLLSMNLYELIKKNKFqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVI-DFG------SSC 373
Cdd:cd14155   70 --INGGNLEQLLDSNEP--LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVgDFGlaekipDYS 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 374 YEHQRVYTyIQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14155  146 DGKEKLAV-VGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
227-418 2.20e-07

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: 52.30  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHKvhQHVALKMVRNEKRfhrqaaEEIRIL-EHLRKQDKDNTM----NVIHMLENFTFRNHICMTF 301
Cdd:cd14148    1 IIGVGGFGKVYKGLWRG--EEVAVKAARQDPD------EDIAVTaENVRQEARLFWMlqhpNIIALRGVCLNPPHLCLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 302 ELLSMNLYElikkNKFQGFSLP--LVRKFAHSILQCLDALHKNR---IIHCDLKPENILLKQQGRSG------IKVIDFG 370
Cdd:cd14148   73 EYARGGALN----RALAGKKVPphVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPIENDdlsgktLKITDFG 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 371 SSCYEHQRVYTYIQSRF-YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14148  149 LAREWHKTTKMSAAGTYaWMAPEVIRLSLFSKSSDVWSFGVLLWELLTG 197
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
227-417 2.23e-07

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: 52.69  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHK--VHQHVALKMVRN--EKRFHRQAAEEIRILEHLRKQdkDNTMNVIHMLENftfRNHICMTFE 302
Cdd:cd05089    9 VIGEGNFGQVIKAMIKKdgLKMNAAIKMLKEfaSENDHRDFAGELEVLCKLGHH--PNIINLLGACEN---RGYLYIAIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-NLYELIKKNKF----------QGFSLPLVR----KFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVI 367
Cdd:cd05089   84 YAPYgNLLDFLRKSRVletdpafakeHGTASTLTSqqllQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVS--KIA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 368 DFGSSCYEHqrvyTYIQSRFYRAP------EVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05089  162 DFGLSRGEE----VYVKKTMGRLPvrwmaiESLNYSVYTTKSDVWSFGVLLWEIVS 213
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
221-417 3.27e-07

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 52.03  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAY----DHKVHQHVALKMVRNEKrfHRQAAEEIrilehLRKQDKDNTMNVIHMLENFTfrnh 296
Cdd:cd05057    8 ELEKGKVLGSGAFGTVYKGVwipeGEKVKIPVAIKVLREET--GPKANEEI-----LDEAYVMASVDHPHLVRLLG---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMT--FELLSM-----NLYELIKKNKFQGFSLPLVrKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgRSGIKVIDF 369
Cdd:cd05057   77 ICLSsqVQLITQlmplgCLLDYVRNHRDNIGSQLLL-NWCVQIAKGMSYLEEKRLVHRDLAARNVLVKT--PNHVKITDF 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 370 G--------SSCYEHQRVYTYIQsrfYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05057  154 GlaklldvdEKEYHAEGGKVPIK---WMALESIQYRIYTHKSDVWSYGVTVWELMT 206
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
321-414 3.64e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 52.97  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 321 SLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIKVIDFGSSCYehqrVYTYIQSRFY---------RAP 391
Cdd:PHA03211 258 GLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLV--NGPEDICLGDFGAACF----ARGSWSTPFHygiagtvdtNAP 331
                         90       100
                 ....*....|....*....|...
gi 153281169 392 EVILGARYGMPIDMWSLGCILAE 414
Cdd:PHA03211 332 EVLAGDPYTPSVDIWSAGLVIFE 354
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
225-417 4.75e-07

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: 51.42  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGqVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELL 304
Cdd:cd05113    9 LKELGTGQFG-VVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHE------KLVQLYGVCTKQRPIFIITEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRVYTY-I 383
Cdd:cd05113   82 ANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGV--VKVSDFGLSRYVLDDEYTSsV 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153281169 384 QSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05113  160 GSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYS 196
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
226-431 5.39e-07

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 51.16  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAyDHKVHQHVALKMVRNEkrfhRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd05085    2 ELLGKGNFGEVYKG-TLKDKTPVAVKTCKED----LPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQRVYTYIQS 385
Cdd:cd05085   77 GGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGEN--NALKISDFGMSRQEDDGVYSSSGL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153281169 386 R----FYRAPEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGEDEGDQL 431
Cdd:cd05085  155 KqipiKWTAPEALNYGRYSSESDVWSFGILLWETFSlgvcPYPGMTNQQAREQV 208
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
222-417 7.85e-07

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: 50.90  E-value: 7.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYdHKVHQHVALKMVRNE-KRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMT 300
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGL-WKNRVRVAIKILKSDdLLKQQDFQKEVQALKRLRHK------HLISLFAVCSVGEPVYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQRV 379
Cdd:cd05148   81 TELMEKgSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED--LVCKVADFGLARLIKEDV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 380 YTYIQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05148  159 YLSSDKKIpykWTAPEAASHGTFSTKSDVWSFGILLYEMFT 199
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
298-429 7.95e-07

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: 50.86  E-value: 7.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKFQG---FSLPLVRKFAHSILQCLDALHKN-RIIHCDLKPENILLKQQGRSgIKVIDFGSSC 373
Cdd:cd14001   82 CLAMEYGGKSLNDLIEERYEAGlgpFPAATILKVALSIARALEYLHNEkKILHGDIKSGNVLIKGDFES-VKLCDFGVSL 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153281169 374 --YEHQRVYT-----YIQSRFYRAPEVILGaryGMPI----DMWSLGCILAELLTGYP----LLPGEDEGD 429
Cdd:cd14001  161 plTENLEVDSdpkaqYVGTEPWKAKEALEE---GGVItdkaDIFAYGLVLWEMMTLSVphlnLLDIEDDDE 228
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
226-424 8.20e-07

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 50.79  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKvHQHVALKMVRNEKRFHRQAAEEIRILEHLrKQDKDNTMNVIhmlenfTFRNHICMTFELLS 305
Cdd:cd05073   17 KKLGAGQFGEVWMATYNK-HTKVAVKTMKPGSMSVEAFLAEANVMKTL-QHDKLVKLHAV------VTKEPIYIITEFMA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 M-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQRVYTYIQ 384
Cdd:cd05073   89 KgSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSAS--LVCKIADFGLARVIEDNEYTARE 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153281169 385 -SRF---YRAPEVILGARYGMPIDMWSLGCILAELLT-GYPLLPG 424
Cdd:cd05073  167 gAKFpikWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPG 211
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
226-417 8.41e-07

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 50.36  E-value: 8.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKvHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd05034    1 KKLGAGQFGEVWMGVWNG-TTKVAVKTLKPGTMSPEAFLQEAQIMKKLRHD------KLVQLYAVCSDEEPIYIVTELMS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 M-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRSGI-KVIDFGSSCYEHQRVYTYI 383
Cdd:cd05034   74 KgSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILV---GENNVcKVADFGLARLIEDDEYTAR 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153281169 384 Q-SRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05034  151 EgAKFpikWTAPEAALYGRFTIKSDVWSFGILLYEIVT 188
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
344-418 1.16e-06

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: 50.41  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 344 IIHCDLKPENILLKQQGRS------GIKVIDFGSSCYEHQRVYTYIQSRF-YRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14147  125 VIHRDLKSNNILLLQPIENddmehkTLKITDFGLAREWHKTTQMSAAGTYaWMAPEVIKASTFSKGSDVWSFGVLLWELL 204

                 ..
gi 153281169 417 TG 418
Cdd:cd14147  205 TG 206
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
324-392 1.22e-06

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 51.33  E-value: 1.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 324 LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSCyeHQRV-YTYIQSRF-----YRAPE 392
Cdd:PLN03225 256 IIQTIMRQILFALDGLHSTGIVHRDVKPQNIIFSEGSGS-FKIIDLGAAA--DLRVgINYIPKEFlldprYAAPE 327
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
228-436 1.56e-06

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 49.96  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDH--KVHQHVALKMVRNEkrfhrqaAEEIRILEHLRKQdkdntMNVIHMLEN-FTFRN-HICMTFE- 302
Cdd:cd05116    3 LGSGNFGTVKKGYYQmkKVVKTVAVKILKNE-------ANDPALKDELLRE-----ANVMQQLDNpYIVRMiGICEAESw 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSMNLYELIKKNKF----QGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFG-SSCYEHQ 377
Cdd:cd05116   71 MLVMEMAELGPLNKFlqknRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA--KISDFGlSKALRAD 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 378 RVYTYIQS------RFYrAPEVILGARYGMPIDMWSLGCILAELLTgYPLLPGED-EGDQLACMIE 436
Cdd:cd05116  149 ENYYKAQThgkwpvKWY-APECMNYYKFSSKSDVWSFGVLMWEAFS-YGQKPYKGmKGNEVTQMIE 212
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
212-417 1.59e-06

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 50.07  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 212 QVPHDHVayryEVLKVIGKGSFGQVVKAyDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLrKQDKdntmnvIHMLENF 291
Cdd:cd05070    5 EIPRESL----QLIKRLGNGQFGEVWMG-TWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKL-KHDK------LVQLYAV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRNHICMTFELLSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRSGI-KVIDF 369
Cdd:cd05070   73 VSEEPIYIVTEYMSKgSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILV---GNGLIcKIADF 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 370 GSSCYEHQRVYTYIQ-SRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05070  150 GLARLIEDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVT 201
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
212-423 1.66e-06

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 49.83  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 212 QVPHDHVAYryevLKVIGKGSFGQVVKA-----YDHKVHQHVALKMVRNE------KRFHRQAAeeiriLEHlrkqDKDN 280
Cdd:cd05050    1 EYPRNNIEY----VRDIGQGAFGRVFQArapglLPYEPFTMVAVKMLKEEasadmqADFQREAA-----LMA----EFDH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 281 TmNVIHMLENFTFRNHICMTFELLSM-NLYELIKKN----------------KFQGFSLPLVRKFAHSILQCLDA----L 339
Cdd:cd05050   68 P-NIVKLLGVCAVGKPMCLLFEYMAYgDLNEFLRHRspraqcslshstssarKCGLNPLPLSCTEQLCIAKQVAAgmayL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 340 HKNRIIHCDLKPENILLKQQGRsgIKVIDFGSScyehQRVYTyiqSRFYRA------------PEVILGARYGMPIDMWS 407
Cdd:cd05050  147 SERKFVHRDLATRNCLVGENMV--VKIADFGLS----RNIYS---ADYYKAsendaipirwmpPESIFYNRYTTESDVWA 217
                        250
                 ....*....|....*.
gi 153281169 408 LGCILAELLTgYPLLP 423
Cdd:cd05050  218 YGVVLWEIFS-YGMQP 232
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
228-416 2.10e-06

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 49.43  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALK-MVRNEKRFHRQAAEEIRILEHLrkqDKDNTMNVIHMLENFTFRNhicMTFELLSM 306
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKeLIRFDEEAQRNFLKEVKVMRSL---DHPNVLKFIGVLYKDKKLN---LITEYIPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG--------------SS 372
Cdd:cd14154   75 GTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVRED--KTVVVADFGlarliveerlpsgnMS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 373 CYEHQRV---------YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd14154  153 PSETLRHlkspdrkkrYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
228-435 2.81e-06

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: 48.93  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVhqhVALKM--VRNEKRFHRQA-AEEIRILehlRKQDKDNTMNVIhmleNFTFRNHICMTFELL 304
Cdd:cd14062    1 IGSGSFGTVYKGRWHGD---VAVKKlnVTDPTPSQLQAfKNEVAVL---RKTRHVNILLFM----GYMTKPQLAIVTQWC 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 S-MNLYELIK--KNKFQGFSLPLVrkfAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFG--------SSC 373
Cdd:cd14062   71 EgSSLYKHLHvlETKFEMLQLIDI---ARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLT--VKIGDFGlatvktrwSGS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 374 YEHQRVYTYIqsrFYRAPEVIL---GARYGMPIDMWSLGCILAELLTGYplLPGEDEG--DQLACMI 435
Cdd:cd14062  146 QQFEQPTGSI---LWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQ--LPYSHINnrDQILFMV 207
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
228-431 3.09e-06

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 49.30  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQhVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHmlenftfRNHICMTFELLSM- 306
Cdd:cd05071   17 LGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVS-------EEPIYIVTEYMSKg 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQRVYTYIQ-S 385
Cdd:cd05071   89 SLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGEN--LVCKVADFGLARLIEDNEYTARQgA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 386 RF---YRAPEVILGARYGMPIDMWSLGCILAELLTG----YPLLPGEDEGDQL 431
Cdd:cd05071  167 KFpikWTAPEAALYGRFTIKSDVWSFGILLTELTTKgrvpYPGMVNREVLDQV 219
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
228-420 3.43e-06

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 49.03  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYdhKVHQHVALK----MV-RNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFE 302
Cdd:cd14158   23 LGEGGFGVVFKGY--INDKNVAVKklaaMVdISTEDLTKQFEQEIQVMAKCQHE------NLVELLGYSCDGPQLCLVYT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LL---SMnLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFGSSCYEHQRV 379
Cdd:cd14158   95 YMpngSL-LDRLACLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVP--KISDFGLARASEKFS 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153281169 380 YTYIQSRF-----YRAPEVILGaRYGMPIDMWSLGCILAELLTGYP 420
Cdd:cd14158  172 QTIMTERIvgttaYMAPEALRG-EITPKSDIFSFGVVLLEIITGLP 216
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
226-417 4.02e-06

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 48.37  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQhVALKMVRNEKRFHRQAAEEIRILEHLRkQDKdntmnvIHMLENFTFRNHICMTFELLS 305
Cdd:cd14203    1 VKLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPEAFLEEAQIMKKLR-HDK------LVQLYAVVSEEPIYIVTEFMS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 M-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgRSGIKVIDFGSSCYEHQRVYTYIQ 384
Cdd:cd14203   73 KgSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGD--NLVCKIADFGLARLIEDNEYTARQ 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153281169 385 -SRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd14203  151 gAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVT 187
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
228-417 5.13e-06

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 48.53  E-value: 5.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQhVALKMVRNEKRFHRQAAEEIRILEHLRkQDKdntmnvIHMLENFTFRNHICMTFELLSM- 306
Cdd:cd05069   20 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPEAFLQEAQIMKKLR-HDK------LVPLYAVVSEEPIYIVTEFMGKg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQRVYTYIQ-S 385
Cdd:cd05069   92 SLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDN--LVCKIADFGLARLIEDNEYTARQgA 169
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153281169 386 RF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05069  170 KFpikWTAPEAALYGRFTIKSDVWSFGILLTELVT 204
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
228-423 5.26e-06

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: 48.26  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMV--RNEKRFHRQAAEeiriLEHLRK-QDKDNTMNVIHMLENFTFRNH----ICMT 300
Cdd:cd13975    8 LGRGQYGVVYACDSWGGHFPCALKSVvpPDDKHWNDLALE----FHYTRSlPKHERIVSLHGSVIDYSYGGGssiaVLLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKnkfqGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFGSSCYEHQRVY 380
Cdd:cd13975   84 MERLHRDLYTGIKA----GLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA--KITDLGFCKPEAMMSG 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 381 TYIQSRFYRAPEVILGaRYGMPIDMWSLGCILAELLTGYPLLP 423
Cdd:cd13975  158 SIVGTPIHMAPELFSG-KYDNSVDVYAFGILFWYLCAGHVKLP 199
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
325-402 6.19e-06

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 48.59  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 325 VRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgIKVIDFGSSCyeHQRV-YTYIQSRF-----YRAPEvilgaR 398
Cdd:cd14013  122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQ-FKIIDLGAAA--DLRIgINYIPKEFlldprYAPPE-----Q 193

                 ....
gi 153281169 399 YGMP 402
Cdd:cd14013  194 YIMS 197
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
227-417 6.41e-06

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 48.46  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAYDHK--VHQHVALKMVRN--EKRFHRQAAEEIRILEHLRKQDkdntmNVIHMLENFTFRNHICMTFE 302
Cdd:cd05088   14 VIGEGNFGQVLKARIKKdgLRMDAAIKRMKEyaSKDDHRDFAGELEVLCKLGHHP-----NIINLLGACEHRGYLYLAIE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 LLSM-NLYELIKKNKF--------------QGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVI 367
Cdd:cd05088   89 YAPHgNLLDFLRKSRVletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA--KIA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 368 DFGSScyEHQRVytYIQSRFYRAP------EVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05088  167 DFGLS--RGQEV--YVKKTMGRLPvrwmaiESLNYSVYTTNSDVWSYGVLLWEIVS 218
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
228-435 7.39e-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: 47.75  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVvkaYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNtmnvIHMLENFTFRNHICMTFELLS-M 306
Cdd:cd14151   16 IGSGSFGTV---YKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVN----ILLFMGYSTKPQLAIVTQWCEgS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 307 NLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG--------SSCYEHQR 378
Cdd:cd14151   89 SLYHHLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED--LTVKIGDFGlatvksrwSGSHQFEQ 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 379 VYTYIqsrFYRAPEVIL---GARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMI 435
Cdd:cd14151  166 LSGSI---LWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMV 222
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
310-424 9.30e-06

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 48.10  E-value: 9.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 310 ELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkQQGRSgIKVIDFG-SSCYEHQRVYTYIQSRF- 387
Cdd:cd05105  224 NLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLL-AQGKI-VKICDFGlARDIMHDSNYVSKGSTFl 301
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 153281169 388 ---YRAPEVILGARYGMPIDMWSLGCILAELLT-GYPLLPG 424
Cdd:cd05105  302 pvkWMAPESIFDNLYTTLSDVWSYGILLWEIFSlGGTPYPG 342
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
221-412 1.11e-05

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: 47.12  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRfHRQAAEEIRILEHLRkqdkdNTMNVIHMLENFTFRNHICMT 300
Cdd:cd14128    1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKAR-HPQLLYESKLYKILQ-----GGVGIPHIRWYGQEKDYNVLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMNLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKqQGRSGIKV--IDFG-SSCYEHQ 377
Cdd:cd14128   75 MDLLGPSLEDLFNFCS-RRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMG-IGRHCNKLflIDFGlAKKYRDS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153281169 378 RVYTYIQsrfYRAPEVILG-ARYG-----MPI------DMWSLGCIL 412
Cdd:cd14128  153 RTRQHIP---YREDKNLTGtARYAsinahLGIeqsrrdDMESLGYVL 196
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
217-417 1.20e-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: 47.20  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 217 HVAYryevLKVIGKGSFGQV-VKAYD---HKVHQHVALKMVRNEKRFHRQAAE-EIRILEHLRKQDKDNTMNVIHMLENF 291
Cdd:cd05081    5 HLKY----ISQLGKGNFGSVeLCRYDplgDNTGALVAVKQLQHSGPDQQRDFQrEIQILKALHSDFIVKYRGVSYGPGRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 TFRnhICMTFeLLSMNLYELIKKNKFQ-GFSLPLVrkFAHSILQCLDALHKNRIIHCDLKPENILLkqQGRSGIKVIDFG 370
Cdd:cd05081   81 SLR--LVMEY-LPSGCLRDFLQRHRARlDASRLLL--YSSQICKGMEYLGSRRCVHRDLAARNILV--ESEAHVKIADFG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153281169 371 -SSCYEHQRVYTYIQSR-----FYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05081  154 lAKLLPLDKDYYVVREPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
228-414 1.21e-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: 47.23  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNE--KRFHRQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMTFELLS 305
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSCRETlpPDLKAKFLQEARILKQY------SHPNIVRLIGVCTQKQPIYIVMELVQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 306 MNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgRSGIKVIDFGSSCYEHQRVYT---- 381
Cdd:cd05084   78 GGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTE--KNVLKISDFGMSREEEDGVYAatgg 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153281169 382 --YIQSRfYRAPEVILGARYGMPIDMWSLGCILAE 414
Cdd:cd05084  156 mkQIPVK-WTAPEALNYGRYSSESDVWSFGILLWE 189
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
212-444 1.36e-05

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: 47.31  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 212 QVPHDhvayRYEVLKVIGKGSFGQVV--------KAYDHKVHQhVALKMVRNEKRfHRQAAEEIRILEHLRKQDKDNtmN 283
Cdd:cd05098    9 ELPRD----RLVLGKPLGEGCFGQVVlaeaigldKDKPNRVTK-VAVKMLKSDAT-EKDLSDLISEMEMMKMIGKHK--N 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 284 VIHMLENFTFRNHICMTFELLSM-NLYELIK--------------KNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCD 348
Cdd:cd05098   81 IINLLGACTQDGPLYVIVEYASKgNLREYLQarrppgmeycynpsHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 349 LKPENILLKQQgrSGIKVIDFGSSCYEHQRVYtYIQSRFYR------APEVILGARYGMPIDMWSLGCILAELLT----G 418
Cdd:cd05098  161 LAARNVLVTED--NVMKIADFGLARDIHHIDY-YKKTTNGRlpvkwmAPEALFDRIYTHQSDVWSFGVLLWEIFTlggsP 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 153281169 419 YPLLPGED------EGDQL----ACMIELL--------GMPSQK 444
Cdd:cd05098  238 YPGVPVEElfkllkEGHRMdkpsNCTNELYmmmrdcwhAVPSQR 281
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
223-417 1.45e-05

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 47.33  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAYDHKVHQH----------------VALKMVRNEKRFH-RQAAE-EIRILEHLRKQdkdntmNV 284
Cdd:cd05051    8 EFVEKLGEGQFGEVHLCEANGLSDLtsddfigndnkdepvlVAVKMLRPDASKNaREDFLkEVKIMSQLKDP------NI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 285 IHMLENFTFRNHICMTFEllSMNLYELikkNKF----QGFSLPLVRKFAHSI-LQCL-----------DALHKNRIIHCD 348
Cdd:cd05051   82 VRLLGVCTRDEPLCMIVE--YMENGDL---NQFlqkhEAETQGASATNSKTLsYGTLlymatqiasgmKYLESLNFVHRD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 349 LKPENILLKQQGRsgIKVIDFGSSCYEHQRVYTYIQSRF-----YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05051  157 LATRNCLVGPNYT--IKIADFGMSRNLYSGDYYRIEGRAvlpirWMAWESILLGKFTTKSDVWAFGVTLWEILT 228
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
228-420 1.67e-05

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 46.97  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVAL------KMVRNEKRFHRQAAEEIRILEHlrkqdkdntMNVIHMLENF--TFRNHICM 299
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWcelqdrKLSKSERQRFKEEAGMLKGLQH---------PNIVRFYDSWesTVKGKKCI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TF--ELLSMNLYELIKKnKFQGFSLPLVRKFAHSILQCLDALHKNR--IIHCDLKPENILLkqQGRSG-IKVIDFGSSCY 374
Cdd:cd14030  104 VLvtELMTSGTLKTYLK-RFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI--TGPTGsVKIGDLGLATL 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153281169 375 EHQR-VYTYIQSRFYRAPEvILGARYGMPIDMWSLG-CILAELLTGYP 420
Cdd:cd14030  181 KRASfAKSVIGTPEFMAPE-MYEEKYDESVDVYAFGmCMLEMATSEYP 227
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
227-415 1.76e-05

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: 46.66  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKAydhKVHQH-VALKM--VRNEKRFHRQAaeEIR---ILEHlrkqdkDNTMNVIHMLENftfRNHICMT 300
Cdd:cd13998    2 VIGKGRFGEVWKA---SLKNEpVAVKIfsSRDKQSWFREK--EIYrtpMLKH------ENILQFIAADER---DTALRTE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FeLLSMNLYELIKKNKF-QGFSLPLVR--KFAHSILQCLDALH---------KNRIIHCDLKPENILLKQQGRSGIKviD 368
Cdd:cd13998   68 L-WLVTAFHPNGSL*DYlSLHTIDWVSlcRLALSVARGLAHLHseipgctqgKPAIAHRDLKSKNILVKNDGTCCIA--D 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 369 FG------SSCYE-----HQRVYTyiqsRFYRAPEVILGA-RYGMP-----IDMWSLGCILAEL 415
Cdd:cd13998  145 FGlavrlsPSTGEednanNGQVGT----KRYMAPEVLEGAiNLRDFesfkrVDIYAMGLVLWEM 204
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
236-423 1.76e-05

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: 46.74  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 236 VVKAYDHKVHQHvalKMVRnekrfhrqaaeEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELLSMNLYELIKKN 315
Cdd:cd14156   22 VVKIYKNDVDQH---KIVR-----------EISLLQKLSHP------NIVRYLGICVKDEKLHPILEYVSGGCLEELLAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 316 KfqgfSLPLVRK----FAHSILQCLDALHKNRIIHCDLKPENILLKQ--QGRSGIkVIDFGSS-------CYEHQRVYTY 382
Cdd:cd14156   82 E----ELPLSWRekveLACDISRGMVYLHSKNIYHRDLNSKNCLIRVtpRGREAV-VTDFGLArevgempANDPERKLSL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153281169 383 IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLP 423
Cdd:cd14156  157 VGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADP 197
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
225-417 1.77e-05

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 46.69  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAY-----DHKVHQHVALKMVRNEKRFHRQAAEEiRILEHLRKQdkdNTMNVIHMLENFTFRNHICM 299
Cdd:cd05046   10 ITTLGRGEFGEVFLAKakgieEEGGETLVLVKALQKTKDENLQSEFR-RELDMFRKL---SHKNVVRLLGLCREAEPHYM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFE---LLSMNLYELIKK-----NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVI---- 367
Cdd:cd05046   86 ILEytdLGDLKQFLRATKskdekLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLslsk 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 368 DFGSSCYEHQRvYTYIQSRfYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05046  166 DVYNSEYYKLR-NALIPLR-WLAPEAVQEDDFSTKSDVWSFGVLMWEVFT 213
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
221-374 1.90e-05

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 46.87  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVK---AYDHKVHQHVALKMvrnEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTF---- 293
Cdd:PHA02882  13 EWKIDKLIGCGGFGCVYEtqcASDHCINNQAVAKI---ENLENETIVMETLVYNNIYDIDKIALWKNIHNIDHLGIpkyy 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 ------RNHICMTFELLSmNLYELIKK--NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIk 365
Cdd:PHA02882  90 gcgsfkRCRMYYRFILLE-KLVENTKEifKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYI- 167

                 ....*....
gi 153281169 366 vIDFGSSCY 374
Cdd:PHA02882 168 -IDYGIASH 175
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
223-431 2.16e-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: 46.25  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAYDHKVHQhVALKMVR----NEKRFHRQAaeeiRILEHLRKQdkdntmNVIHMLENFTFRNHIC 298
Cdd:cd05068   11 KLLRKLGSGQFGEVWEGLWNNTTP-VAVKTLKpgtmDPEDFLREA----QIMKKLRHP------KLIQLYAVCTLEEPIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRSGI-KVIDFG-SSCYE 375
Cdd:cd05068   80 IITELMKHgSLLEYLQGKGRS-LQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLV---GENNIcKVADFGlARVIK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 376 HQRVYT-YIQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGEDEGDQL 431
Cdd:cd05068  156 VEDEYEaREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTygriPYPGMTNAEVLQQV 219
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
225-417 2.56e-05

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: 46.01  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGqVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELL 304
Cdd:cd05114    9 MKELGSGLFG-VVRLGKWRAQYKVAIKAIREGAMSEEDFIEEAKVMMKLTHP------KLVQLYGVCTQQKPIYIVTEFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SMN-LYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRVYTY- 382
Cdd:cd05114   82 ENGcLLNYLRQRRGK-LSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGV--VKVSDFGMTRYVLDDQYTSs 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153281169 383 IQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05114  159 SGAKFpvkWSPPEVFNYSKFSSKSDVWSFGVLMWEVFT 196
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
223-426 2.72e-05

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 46.13  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVVKAyDHKVHQhVALKMVRNEKRFHRQAAEEiRILEHLRKQDKDNTMNVIhMLENFTFrnHICMTFe 302
Cdd:cd05082    9 KLLQTIGKGEFGDVMLG-DYRGNK-VAVKCIKNDATAQAFLAEA-SVMTQLRHSNLVQLLGVI-VEEKGGL--YIVTEY- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 303 llsMNLYELIKKNKFQGFSL---PLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSgiKVIDFGSSCYEHQRV 379
Cdd:cd05082   82 ---MAKGSLVDYLRSRGRSVlggDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVA--KVSDFGLTKEASSTQ 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 380 YTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGED 426
Cdd:cd05082  157 DTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfgrvPYPRIPLKD 207
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
221-417 2.77e-05

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: 46.05  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RY-EVLKVIGKGSFGQV-VKAYD---HKVHQHVALKMVRNE-KRFHRQA-AEEIRILEHLrkqDKDNTMNVIHMLENFTF 293
Cdd:cd05080    4 RYlKKIRDLGEGHFGKVsLYCYDptnDGTGEMVAVKALKADcGPQHRSGwKQEIDILKTL---YHENIVKYKGCCSEQGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 294 RNhICMTFELLSM-NLYELIKKNKFqgfSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFG-- 370
Cdd:cd05080   81 KS-LQLIMEYVPLgSLRDYLPKHSI---GLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDND--RLVKIGDFGla 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153281169 371 ---SSCYEHQRVYTYIQSR-FYRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05080  155 kavPEGHEYYRVREDGDSPvFWYAPECLKEYKFYYASDVWSFGVTLYELLT 205
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
226-425 3.19e-05

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: 46.11  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKV-----HQHVALKMVRNekrfHRQAAEEIRILEHLRKQDKDNTMNVIHMLenftfrnHICMT 300
Cdd:cd05045    6 KTLGEGEFGKVVKATAFRLkgragYTTVAVKMLKE----NASSSELRDLLSEFNLLKQVNHPHVIKLY-------GACSQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSMnLYELIKKNKFQGFsLPLVRK--------------------------------FAHSILQCLDALHKNRIIHCD 348
Cdd:cd05045   75 DGPLLL-IVEYAKYGSLRSF-LRESRKvgpsylgsdgnrnssyldnpderaltmgdlisFAWQISRGMQYLAEMKLVHRD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 349 LKPENILLKQqGRSgIKVIDFGSS--CYEHQRVYTYIQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT----GY 419
Cdd:cd05045  153 LAARNVLVAE-GRK-MKISDFGLSrdVYEEDSYVKRSKGRIpvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnPY 230

                 ....*.
gi 153281169 420 PLLPGE 425
Cdd:cd05045  231 PGIAPE 236
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
223-536 5.63e-05

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 45.36  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFG-QVVKAYDHKVHQ-HVALKMVRNEKRFH---RQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHI 297
Cdd:cd08216    1 ELLYEIGKCFKGgGVVHLAKHKPTNtLVAVKKINLESDSKedlKFLQQEILTSRQLQHP------NILPYVTSFVVDNDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 298 CMTFELLSMNLYELIKKNKF-QGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEH 376
Cdd:cd08216   75 YVVTPLMAYGSCRDLLKTHFpEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 377 -QR---VYTY----IQSRFYRAPEV----ILGarYGMPIDMWSLGCILAELLTGYplLPGEDEGDQLAcMIELLGMPSQK 444
Cdd:cd08216  155 gKRqrvVHDFpkssEKNLPWLSPEVlqqnLLG--YNEKSDIYSVGITACELANGV--VPFSDMPATQM-LLEKVRGTTPQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 445 LLDASKraknfvsskgYPRYCTVTTLSDGSVVLNGGRSRRgklRGPPESREWGNAlkgcddplFLDFLKQCLEWDPAVRM 524
Cdd:cd08216  230 LLDCST----------YPLEEDSMSQSEDSSTEHPNNRDT---RDIPYQRTFSEA--------FHQFVELCLQRDPELRP 288
                        330
                 ....*....|..
gi 153281169 525 TPGQALRHPWLR 536
Cdd:cd08216  289 SASQLLAHSFFK 300
CotS COG0510
Thiamine kinase and related kinases [Coenzyme transport and metabolism];
310-373 6.77e-05

Thiamine kinase and related kinases [Coenzyme transport and metabolism];


Pssm-ID: 223584 [Multi-domain]  Cd Length: 269  Bit Score: 45.08  E-value: 6.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 310 ELIKKNKFQGFSLPLVRKFAHSILQCLDALHK--NRIIHCDLKPENILLKQQGRsgIKVIDFGSSC 373
Cdd:COG0510  119 LLWQQNSRAYRDNHLLRKKLKELRRALEEVPKddLVPCHNDLNPGNLLLTDKGG--LFLIDWEYAG 182
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
226-426 7.82e-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: 45.01  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQH-------VALKMVRNEKRfHRQAAEEIRILEHLRKQDKDNtmNVIHMLENFTFRNHIC 298
Cdd:cd05100   18 KPLGEGCFGQVVMAEAIGIDKDkpnkpvtVAVKMLKDDAT-DKDLSDLVSEMEMMKMIGKHK--NIINLLGACTQDGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNK-------FQGFSLP--------LVrKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrS 362
Cdd:cd05100   95 VLVEYASKgNLREYLRARRppgmdysFDTCKLPeeqltfkdLV-SCAYQVARGMEYLASQKCIHRDLAARNVLVTED--N 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 363 GIKVIDFGSSCYEHQRVYtYIQSRFYR------APEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGED 426
Cdd:cd05100  172 VMKIADFGLARDVHNIDY-YKKTTNGRlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFTlggsPYPGIPVEE 244
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
221-418 1.29e-04

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: 43.90  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 221 RYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMvRNEKRFHRQAAEEIRILEHL---------RKQDKDNTMNVihmlenf 291
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKL-ESVKTKHPQLLYESKLYKILqggvgipnvRWYGVEGDYNV------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 292 tfrnhicMTFELLSMNLYELIKknkFQG--FSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKqQGRSG--IKVI 367
Cdd:cd14125   73 -------MVMDLLGPSLEDLFN---FCSrkFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMG-LGKKGnlVYII 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153281169 368 DFG-SSCYEHQRVYTYIQsrfYRAPEVILG-ARYG-----MPI------DMWSLGCILAELLTG 418
Cdd:cd14125  142 DFGlAKKYRDPRTHQHIP---YRENKNLTGtARYAsinthLGIeqsrrdDLESLGYVLMYFNRG 202
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
226-416 1.54e-04

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: 43.95  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHK---VHQHVALKMVRNEKrfhrQAAEEIRILEH---LRKQDKDNTMNVIHMLENftfrNHICM 299
Cdd:cd05056   12 RCIGEGQFGDVYQGVYMSpenEKIAVAVKTCKNCT----SPSVREKFLQEayiMRQFDHPHIVKLIGVITE----NPVWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 300 TFELLSM-NLYELIKKNKFQGFSLPLVrKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCY-EHQ 377
Cdd:cd05056   84 VMELAPLgELRSYLQVNKYSLDLASLI-LYAYQLSTALAYLESKRFVHRDIAARNVLVSSP--DCVKLGDFGLSRYmEDE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153281169 378 RVYTYIQSRF---YRAPEVILGARYGMPIDMWSLGCILAELL 416
Cdd:cd05056  161 SYYKASKGKLpikWMAPESINFRRFTSASDVWMFGVCMWEIL 202
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
336-418 1.55e-04

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: 43.67  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 336 LDALHK--NRIIHCDLKPENILLKQQGRSGikVIDFGSSCYEHQRVYTYIQSR----FYRAPEVIL-GARYGMPIDMWSL 408
Cdd:cd14064  106 MEYLHNltQPIIHRDLNSHNILLYEDGHAV--VADFGESRFLQSLDEDNMTKQpgnlRWMAPEVFTqCTRYSIKADVFSY 183
                         90
                 ....*....|
gi 153281169 409 GCILAELLTG 418
Cdd:cd14064  184 ALCLWELLTG 193
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
225-423 1.58e-04

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 43.85  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAY------DHKvhQHVALKMVR--NEKRFHRQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNH 296
Cdd:cd05090   10 MEELGECAFGKIYKGHlylpgmDHA--QLVAIKTLKdyNNPQQWNEFQQEASLMTELHHP------NIVCLLGVVTQEQP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 297 ICMTFELLSM-NLYE-LIKKNKFQGFSLP-----LVRK------FAHSILQC---LDALHKNRIIHCDLKPENILLKQQG 360
Cdd:cd05090   82 VCMLFEFMNQgDLHEfLIMRSPHSDVGCSsdedgTVKSsldhgdFLHIAIQIaagMEYLSSHFFVHKDLAARNILVGEQL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 361 RsgIKVIDFGSSCYEHQRVYTYIQSRF-----YRAPEVILGARYGMPIDMWSLGCILAELLTgYPLLP 423
Cdd:cd05090  162 H--VKISDLGLSREIYSSDYYRVQNKSllpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS-FGLQP 226
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
327-374 1.98e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 41.91  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153281169 327 KFAHSILQCLDALHKNRI---IHCDLKPENILLKQQGR-SGIkvIDFGSSCY 374
Cdd:cd05120   93 KIADQLAEILAALHRIDSsvlTHGDLHPGNILVKPDGKlSGI--IDWEFAGY 142
STKc_Bub1_vert cd14028
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
227-372 2.13e-04

Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein Bub1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Bub1 (Budding uninhibited by benzimidazoles 1) contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding, a GLEBS motif for Bub3/kinetochore binding, and a C-terminal kinase domain. It is 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. Bub1 contributes to the inhibition of APC/C by phosphorylating its crucial cofactor, Cdc20, rendering it unable to activate APC/C. In addition, Bub1 facilitates the localization to kinetochores of other SAC and motor proteins including Mad1, Mad2, BubR1, and Plk1. It acts as the master organizer of the functional inner centromere. Bub1 also play roles in protecting sister chromatid cohesion and normal metaphase congression. The Bub1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270930 [Multi-domain]  Cd Length: 290  Bit Score: 43.68  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 227 VIGKGSFGQVVKA-----YDHKVHQHVALKMVRNEKRFhrqaaeEIRILEHLRKQDKDNTMNV-IHMLENFTFRNHICMT 300
Cdd:cd14028    7 LLGEGAFAQVYQAtqldlNDAKSNQKFVLKVQKPANPW------EFYIGTQLMERLKPSMRHLfIKFYSAHLFQNGSVLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLS----MNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENIL-----LKQQGRS------GIK 365
Cdd:cd14028   81 GELYNygtlLNAINLYKKLPEKVMPQPLVIYFAMRILYMVEQLHDCEIIHGDIKPDNFIlgerfLENDDCEeddlshGLA 160

                 ....*..
gi 153281169 366 VIDFGSS 372
Cdd:cd14028  161 LIDLGQS 167
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
228-436 2.14e-04

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: 43.11  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAY----DHKVHQhVALKMVRNEkrfHRQAAEEirilEHLRKQdkdntmNVIHMLEN--------FTFRN 295
Cdd:cd05060    3 LGHGNFGSVRKGVylmkSGKEVE-VAVKTLKQE---HEKAGKK----EFLREA------SVMAQLDHpcivrligVCKGE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HICMTFELLSMN-LYELIKKNkfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSScy 374
Cdd:cd05060   69 PLMLVMELAPLGpLLKYLKKR--REIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ--AKISDFGMS-- 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153281169 375 ehqRVY----TYIQS--------RFYrAPEVILGARYGMPIDMWSLGCILAELLTgYPLLP-GEDEGDQLACMIE 436
Cdd:cd05060  143 ---RALgagsDYYRAttagrwplKWY-APECINYGKFSSKSDVWSYGVTLWEAFS-YGAKPyGEMKGPEVIAMLE 212
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
226-426 2.16e-04

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: 43.47  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAYDHKVHQH-------VALKMVRNEKRfHRQAAEEIRILEHLRKQDKDNtmNVIHMLENFTFRNHIC 298
Cdd:cd05101   30 KPLGEGCFGQVVMAEAVGIDKDkpkeavtVAVKMLKDDAT-EKDLSDLVSEMEMMKMIGKHK--NIINLLGACTQDGPLY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-NLYELIKKNKFQG--FSLPLVR------------KFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSG 363
Cdd:cd05101  107 VIVEYASKgNLREYLRARRPPGmeYSYDINRvpeeqmtfkdlvSCTYQLARGMEYLASQKCIHRDLAARNVLVTEN--NV 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153281169 364 IKVIDFGSSCYEHQRVYtYIQSRFYR------APEVILGARYGMPIDMWSLGCILAELLT----GYPLLPGED 426
Cdd:cd05101  185 MKIADFGLARDINNIDY-YKKTTNGRlpvkwmAPEALFDRVYTHQSDVWSFGVLMWEIFTlggsPYPGIPVEE 256
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
225-417 2.17e-04

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 43.41  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 225 LKVIGKGSFGQVVKAY----DHKVHQHVALKMVRNekRFHRQAAEEIRilEHLRKQDKDNTMNVIHMLenftfrnHIC-- 298
Cdd:cd05111   12 LKVLGSGVFGTVHKGIwipeGDSIKIPVAIKVIQD--RSGRQSFQAVT--DHMLAIGSLDHAYIVRLL-------GICpg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 299 MTFELLSM-----NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSS- 372
Cdd:cd05111   81 ASLQLVTQllplgSLLDHVRQHR-GSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSP--SQVQVADFGVAd 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 373 -CYEHQRVYTYIQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05111  158 lLYPDDKKYFYSEAKTpikWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
328-442 2.53e-04

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: 43.12  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 328 FAHSILQCLDAlHKNRIIHCDLKPENILLKQQGRSGIKviDFG------SSCYEHQRV-------YTYIQSRFYRAPEVI 394
Cdd:cd14054  108 YLHTDLRRGDQ-YKPAIAHRDLNSRNVLVKADGSCVIC--DFGlamvlrGSSLVRGRPgaaenasISEVGTLRYMAPEVL 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 395 LGA-------RYGMPIDMWSLGCILAELLTGYP-LLPGEDEGD-QLACMIELLGMPS 442
Cdd:cd14054  185 EGAvnlrdceSALKQVDVYALGLVLWEIAMRCSdLYPGESVPPyQMPYEAELGNHPT 241
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
226-417 2.81e-04

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: 42.71  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKA----YDHKVHQhVALKMVRNEKRFHRQAAEE-IRILEHLRKQDKDNtmnVIHmLENFTFRNHICMT 300
Cdd:cd05040    1 EKLGDGSFGVVRRGewttPSGKVIQ-VAVKCLKSDVLSQPNAMDDfLKEVNAMHSLDHPN---LIR-LYGVVLSSPLMMV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 301 FELLSM-NLYELIKKNKfQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgRSGIKVIDFGSS------- 372
Cdd:cd05040   76 TELAPLgSLLDRLRKDQ-GHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLAS--KDKVKIGDFGLMralpqne 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153281169 373 -CY---EHQRVytyiqsRF-YRAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05040  153 dHYvmqEHRKV------PFaWCAPESLKTRKFSHASDVWMFGVTLWEMFT 196
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
226-417 3.18e-04

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 42.91  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKA---YDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHM------LENFT---- 292
Cdd:cd05035    5 KILGEGEFGSVMEAqlkQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVcftasdLNKPPspmv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 293 ---FRNHICMTFELLSMNLYELIKKnkfqgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDF 369
Cdd:cd05035   85 ilpFMKHGDLHSYLLYSRLGGLPEK-----LPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMT--VCVADF 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153281169 370 GSScyehQRVYT---YIQSRFYRAP------EVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05035  158 GLS----RKIYSgdyYRQGRISKMPvkwialESLADNVYTSKSDVWSFGVTMWEIAT 210
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
248-417 3.67e-04

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 42.66  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 248 VALKMVRNE--KRFHRQAAEEIRILEHLrkqdkdNTMNVIHMLENFTFRNHICMTFELLS---MNLY--------ELIKK 314
Cdd:cd05097   47 VAVKMLRADvtKTARNDFLKEIKIMSRL------KNPNIIRLLGVCVSDDPLCMITEYMEngdLNQFlsqreiesTFTHA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 315 NKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLkqqGRS-GIKVIDFGSSCYEHQRVYTYIQSRF-----Y 388
Cdd:cd05097  121 NNIPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLV---GNHyTIKIADFGMSRNLYSGDYYRIQGRAvlpirW 197
                        170       180
                 ....*....|....*....|....*....
gi 153281169 389 RAPEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05097  198 MAWESILLGKFTTASDVWAFGVTLWEMFT 226
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
332-374 7.66e-04

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 41.33  E-value: 7.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 153281169  332 ILQCLDALHKNRIIHCDLKPENILLKQQGRsGIKVIDFGSSCY 374
Cdd:pfam01636 157 LLALLPAELPPVLVHGDLHPGNLLVDPGGR-VSGVIDFEDAGL 198
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
226-372 7.78e-04

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 [Multi-domain]  Cd Length: 302  Bit Score: 41.75  E-value: 7.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAY--------DHKVHQhVALKMVRN-----EKRFHRQAAEEirilEHLRKQDKDNTMNVIHM----- 287
Cdd:cd14123   18 KMIGKGGFGLIYLASpqvnvpveDDAVHV-IKVEYHENgplfsELKFYQRAAKP----DTISKWMKSKQLDYLGIptywg 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 288 --LENFTFRNHICMTFELLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIK 365
Cdd:cd14123   93 sgLTEFNGTSYRFMVMDRLGTDLQKILIDNGGQ-FKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYRNPNEVY 171

                 ....*..
gi 153281169 366 VIDFGSS 372
Cdd:cd14123  172 LADYGLS 178
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
228-426 1.03e-03

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: 41.25  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKVHQHVALKMVRNE----KRFHRQAAeeirILEHLRKQdkdntmNVIHMLENFTFRNHICMTFEL 303
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDtmevEEFLKEAA----VMKEIKHP------NLVQLLGVCTREPPFYIITEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 304 LSM-NLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQgrSGIKVIDFGSSCYEHQRVYT- 381
Cdd:cd05052   84 MPYgNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGEN--HLVKVADFGLSRLMTGDTYTa 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 382 YIQSRF---YRAPEVILGARYGMPIDMWSLGCILAELLT-GYPLLPGED 426
Cdd:cd05052  162 HAGAKFpikWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGID 210
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
226-415 1.54e-03

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 40.79  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 226 KVIGKGSFGQVVKAydHKVHQHVALKMVRNEKRFHRQAAEEI---------RILEHLRKQDKDNTMNV-IHMLENFTFRN 295
Cdd:cd14141    1 EIKARGRFGCVWKA--QLLNEYVAVKIFPIQDKLSWQNEYEIyslpgmkheNILQFIGAEKRGTNLDVdLWLITAFHEKG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 296 HIC--MTFELLSMNLYELIKKNKFQGFSlplvrkFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKviDFG--- 370
Cdd:cd14141   79 SLTdyLKANVVSWNELCHIAQTMARGLA------YLHEDIPGLKDGHKPAIAHRDIKSKNVLLKNNLTACIA--DFGlal 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 371 ------SSCYEHQRVYTyiqsRFYRAPEVILGA-----RYGMPIDMWSLGCILAEL 415
Cdd:cd14141  151 kfeagkSAGDTHGQVGT----RRYMAPEVLEGAinfqrDAFLRIDMYAMGLVLWEL 202
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
332-441 1.64e-03

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 39.69  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169   332 ILQCLDALHKnriIHCDLKPENILLKQQGRsgikVIDFGSSCYehQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCI 411
Cdd:smart00750  23 CLQCLGALRE---LHRQAKSGNILLTWDGL----LKLDGSVAF--KTPEQSRPDPYFMAPEVIQGQSYTEKADIYSLGIT 93
                           90       100       110
                   ....*....|....*....|....*....|..
gi 153281169   412 LAELLTGYpllPGEDEGDQLACMIE--LLGMP 441
Cdd:smart00750  94 LYEALDYE---LPYNEERELSAILEilLNGMP 122
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
223-370 1.70e-03

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: 40.76  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 223 EVLKVIGKGSFGQVvkaYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTmnVIHMlenftfrnHICMTFE 302
Cdd:cd14153    3 EIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENV--VLFM--------GACMSPP 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 303 LLSM--------NLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQqgrSGIKVIDFG 370
Cdd:cd14153   70 HLAIitslckgrTLYSVVRDAKVV-LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN---GKVVITDFG 141
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
316-380 2.50e-03

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 40.32  E-value: 2.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153281169 316 KFQGFSLPLVRKFAHSILQCLDALHKNR-------IIHCDLKPENILLKQQGRSGIkvIDFGSSCYEHqRVY 380
Cdd:cd05153  146 RLKARLDLLAADDRALLEDELARLQALApsdlprgVIHADLFRDNVLFDGDRLSGI--IDFYDACYDP-LLY 214
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
327-428 2.68e-03

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 40.21  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 327 KFAHSILQCLDALHKNRIIHCDLKPENILLKQQ-----GRSGIKVIDFgsscyEHQRVYTYIQSRFYRA-----PEVILg 396
Cdd:cd14157   99 SISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNllpklGHSGLRLCPV-----DKKSVYTMMKTKVLQIslaylPEDFV- 172
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 153281169 397 aRYGM---PIDMWSLGCILAELLTGyplLPGEDEG 428
Cdd:cd14157  173 -RHGQlteKVDIFSCGVVLAEILTG---IKAMDEF 203
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
299-373 2.69e-03

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: 39.96  E-value: 2.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153281169 299 MTFELLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILL-KQQGRSGIKVIDFGSSC 373
Cdd:cd14015  104 LVMPRFGRDLQKIFEKNGKR-FPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLgFGKNKDQVYLVDYGLAS 178
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
222-370 2.95e-03

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: 40.10  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 222 YEVLKVIGKGSFGQVVKAYDHKVHQHVALKM---------VRNEKRFHRQ--AAEEIRILEHLRKQDKDNTMnvihmlen 290
Cdd:cd14126    2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepmksrapqLHLEYRFYKLlgQAEGLPQVYYFGPCGKYNAM-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 291 ftfrnhicmTFELLSMNLYELIKKNKFQgFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQG---RSGIKVI 367
Cdd:cd14126   74 ---------VLELLGPSLEDLFDLCDRT-FSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQStkkQHVIHII 143

                 ...
gi 153281169 368 DFG 370
Cdd:cd14126  144 DFG 146
PRK14879 PRK14879
Kae1-associated kinase Bud32;
339-370 5.64e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 38.35  E-value: 5.64e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 153281169 339 LHKNRIIHCDLKPENILLKQqgrSGIKVIDFG 370
Cdd:PRK14879 111 LHSAGIIHGDLTTSNMILSG---GKIYLIDFG 139
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
228-418 6.22e-03

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 38.63  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 228 IGKGSFGQVVKAYDHKvHQHVALK-MVRNEKRFH-RQAAEEIRILEHLRKQdkdntmNVIHMLENFTFRNHICMTFELL- 304
Cdd:cd14664    1 IGRGGAGTVYKGVMPN-GTLVAVKrLKGEGTQGGdHGFQAEIQTLGMIRHR------NIVRLRGYCSNPTTNLLVYEYMp 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 305 SMNLYELIKKNKFQGFSL--PLVRKFAHSILQCLDALHKN---RIIHCDLKPENILLKQQGRSgiKVIDFGSSC---YEH 376
Cdd:cd14664   74 NGSLGELLHSRPESQPPLdwETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEA--HVADFGLAKlmdDKD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153281169 377 QRVYTYIQSRF-YRAPEVILGARYGMPIDMWSLGCILAELLTG 418
Cdd:cd14664  152 SHVMSSVAGSYgYIAPEYAYTGKVSEKSDVYSYGVVLLELITG 194
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
328-423 6.25e-03

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: 39.12  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 328 FAHSILQCLDALHKNRIIHCDLKPENILLKQqGRSGiKVIDFGSScYEHQRVYTYI---QSRF---YRAPEVILGARYGM 401
Cdd:cd05104  219 FSYQVAKGMEFLASKNCIHRDLAARNILLTH-GRIT-KICDFGLA-RDIRNDSNYVvkgNARLpvkWMAPESIFECVYTF 295
                         90       100
                 ....*....|....*....|....*.
gi 153281169 402 PIDMWSLGCILAELL----TGYPLLP 423
Cdd:cd05104  296 ESDVWSYGILLWEIFslgsSPYPGMP 321
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
324-372 7.84e-03

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 38.90  E-value: 7.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 153281169 324 LVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRsgIKVIDFGSS 372
Cdd:PLN03224 310 VIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQ--VKIIDFGAA 356
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
217-417 9.99e-03

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: 38.22  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 217 HVAYRYEVLK-VIGKGSFGQVVKAYDHKVHQH-----VALKMVRN------EKRFHRQAaEEIRILEHlrkqdkdntMNV 284
Cdd:cd05049    1 HIKRDTIVLKrELGEGAFGKVFLGECYNLEPEqdkmlVAVKTLKDasspdaRKDFEREA-ELLTNLQH---------ENI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153281169 285 IHMLENFTFRNHICMTFELLS---MNLY--------ELIKKNKFQGFSLPLVR--KFAHSILQCLDALHKNRIIHCDLKP 351
Cdd:cd05049   71 VKFYGVCTEGDPLLMVFEYMEhgdLNKFlrshgpdaAFLASEDSAPGELTLSQllHIAVQIASGMVYLASQHFVHRDLAT 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153281169 352 ENILLKQQgrSGIKVIDFGSScyehQRVYTyiqSRFYR------------APEVILGARYGMPIDMWSLGCILAELLT 417
Cdd:cd05049  151 RNCLVGTN--LVVKIGDFGMS----RDIYS---TDYYRvgghtmlpirwmPPESILYRKFTTESDVWSFGVVLWEIFT 219
 
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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