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Conserved domains on  [gi|568995944|ref|XP_006522489.1|]
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PREDICTED: glycogen synthase kinase-3 beta isoform X2 [Mus musculus]

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List of domain hits

Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1-256 0e+00

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: 532.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:cd14137   51 MRRLKHPNIVKLKYFFYSSGEKKDEVYLNLVMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHR 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  81 DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGD 160
Cdd:cd14137  131 DIKPQNLLVDPETGVLKLCDFGSAKRLVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 161 SGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKdspgaghftpgvrVFRPRTPPEAIALCSRLLEYTPTA 240
Cdd:cd14137  211 SSVDQLVEIIKVLGTPTREQIKAMNPNYTEFKFPQIKPHPWEK-------------VFPKRTPPDAIDLLSKILVYNPSK 277
                        250
                 ....*....|....*.
gi 568995944 241 RLTPLEACAHSFFDEL 256
Cdd:cd14137  278 RLTALEALAHPFFDEL 293
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1-256 0e+00

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: 532.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:cd14137   51 MRRLKHPNIVKLKYFFYSSGEKKDEVYLNLVMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHR 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  81 DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGD 160
Cdd:cd14137  131 DIKPQNLLVDPETGVLKLCDFGSAKRLVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 161 SGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKdspgaghftpgvrVFRPRTPPEAIALCSRLLEYTPTA 240
Cdd:cd14137  211 SSVDQLVEIIKVLGTPTREQIKAMNPNYTEFKFPQIKPHPWEK-------------VFPKRTPPDAIDLLSKILVYNPSK 277
                        250
                 ....*....|....*.
gi 568995944 241 RLTPLEACAHSFFDEL 256
Cdd:cd14137  278 RLTALEALAHPFFDEL 293
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
2-146 2.07e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 47.25  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   2 RKLDHCNIVRlryfFYSSGE-KKDEVYLNLVLdyVPETVYRVARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:PHA02882  78 HNIDHLGIPK----YYGCGSfKRCRMYYRFIL--LEKLVENTKEIFKRIK-CKNKKLIKNIMKDMLTTLEYIHEHGISHG 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568995944  81 DIKPQNLLLDPDTAVLkLCDFGSAKQLVRGEPNVsyicsRYYRAPELIFGATDYTSSIDVWSAGCV 146
Cdd:PHA02882 151 DIKPENIMVDGNNRGY-IIDYGIASHFIIHGKHI-----EYSKEQKDLHRGTLYYAGLDAHNGACV 210
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1-280 2.11e-124

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 367.05  E-value: 2.11e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSSGEKKDE--VYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGIC 78
Cdd:PTZ00036 113 MKNLNHINIIFLKDYYYTECFKKNEknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFIC 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  79 HRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFP 158
Cdd:PTZ00036 193 HRDLKPQNLLIDPNTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFS 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 159 GDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKdspgaghftpgvrVFRPRTPPEAIALCSRLLEYTP 238
Cdd:PTZ00036 273 GQSSVDQLVRIIQVLGTPTEDQLKEMNPNYADIKFPDVKPKDLKK-------------VFPKGTPDDAINFISQFLKYEP 339
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568995944 239 TARLTPLEACAHSFFDELRDPNVKLPNGRDT-PALFNFTTQEL 280
Cdd:PTZ00036 340 LKRLNPIEALADPFFDDLRDPCIKLPKYIDKlPDLFNFCDAEI 382
Pkinase pfam00069
Protein kinase domain;
1-253 7.79e-67

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 212.88  E-value: 7.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944    1 MRKLDHCNIVRLRYFFYSSGekkdevYLNLVLDYVPETVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:pfam00069  52 LRRLSHPNIVRLIDAFEDKD------HLYLVMEYCEGGDLF---DYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   81 DIKPQNLLLDPDTaVLKLCDFGSAKQL-VRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPG 159
Cdd:pfam00069 123 DLKPENILLDENG-VVKIADFGLAKKLtKSSSSLTTFVGTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSG 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  160 DSGVDQLVEIIKVLGTPTREQIREMNPNytefkfpqikahpwtkdspgaghftpgvrvfrprtPPEAIALCSRLLEYTPT 239
Cdd:pfam00069 202 ESILDQLQLIRRILGPPLEFDEPKSDSG-----------------------------------SEEAKDLIKKCLNKDPS 246
                         250
                  ....*....|....
gi 568995944  240 ARLTPLEACAHSFF 253
Cdd:pfam00069 247 KRPTAEEILQHPWF 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-253 1.54e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 204.30  E-value: 1.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944     1 MRKLDHCNIVRLRYFFYssgekkDEVYLNLVLDYVPetvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:smart00220  51 LKKLKHPNIVRLYDVFE------DEDKLYLVMEYCE---GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHR 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944    81 DIKPQNLLLDPDTaVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGD 160
Cdd:smart00220 122 DLKPENILLDEDG-HVKLADFGLARQLDPGEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   161 sgvDQLVEIIKVLGTPTREQIREMnpnytefkfpqikahpwtkdspgaghftpgvrvfrPRTPPEAIALCSRLLEYTPTA 240
Cdd:smart00220 200 ---DQLLELFKKIGKPKPPFPPPE-----------------------------------WDISPEAKDLIRKLLVKDPEK 241
                          250
                   ....*....|...
gi 568995944   241 RLTPLEACAHSFF 253
Cdd:smart00220 242 RLTAEEALQHPFF 254
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-258 1.09e-46

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 161.52  E-value: 1.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSsgEKKdevyLNLVLDYVPETVYRVARHYSRAKQTLPVIyvKLYMYQLFRSLAYIHSFGICHR 80
Cdd:PLN00009  55 LKEMQHGNIVRLQDVVHS--EKR----LYLVFEYLDLDLKKHMDSSPDFAKNPRLI--KTYLYQILRGIAYCHSHRVLHR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  81 DIKPQNLLLDPDTAVLKLCDFGSAKQLvrGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF 157
Cdd:PLN00009 127 DLKPQNLLIDRRTNALKLADFGLARAF--GIPVRTFtheVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLF 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 158 PGDSGVDQLVEIIKVLGTPTREQIREMN--PNYTEfKFPQikahpWTKDSPGAghftpgvrvFRPRTPPEAIALCSRLLE 235
Cdd:PLN00009 205 PGDSEIDELFKIFRILGTPNEETWPGVTslPDYKS-AFPK-----WPPKDLAT---------VVPTLEPAGVDLLSKMLR 269
                        250       260
                 ....*....|....*....|...
gi 568995944 236 YTPTARLTPLEACAHSFFDELRD 258
Cdd:PLN00009 270 LDPSKRITARAALEHEYFKDLGD 292
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
1-286 5.88e-41

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 148.35  E-value: 5.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHC-NIVRLRYFFYSSGekkdevYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICH 79
Cdd:COG0515   51 LASLNHPpNIVKLYDFFQDEG------SLYLVMEYVDGGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIH 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  80 RDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNV-------SYICSRYYRAPELIFGATD--YTSSIDVWSAGCVLAEL 150
Cdd:COG0515  125 RDIKPENILLDRDGRVVKLIDFGLAKLLPDPGSTSsipalpsTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYEL 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 151 LLGQPIFPGDSG---VDQLVEIIKVLGTPtreqiremnpnytEFKFPQIKAHPWTKdspgaghftpgvrvfrprtPPEAI 227
Cdd:COG0515  205 LTGLPPFEGEKNssaTSQTLKIILELPTP-------------SLASPLSPSNPELI-------------------SKAAS 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568995944 228 ALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPL 286
Cdd:COG0515  253 DLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEAL 311
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
1-201 4.97e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 64.11  E-value: 4.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRklDHCNIVRLRYFFYSsgeKKDEVylnLVLDYVP-----ETVyrvarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSF 75
Cdd:PHA03390  65 MK--DNPNFIKLYYSVTT---LKGHV---LIMDYIKdgdlfDLL--------KKEGKLSEAEVKKIIRQLVEALNDLHKH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  76 GICHRDIKPQNLLLDPDTAVLKLCDFGSAKqlVRGEPnvsyicSRY-----YRAPELIFGAtDYTSSIDVWSAGCVLAEL 150
Cdd:PHA03390 129 NIIHNDIKLENVLYDRAKDRIYLCDYGLCK--IIGTP------SCYdgtldYFSPEKIKGH-NYDVSFDWWAVGVLTYEL 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568995944 151 LLGQPIFPGDSG----VDQL-------VEIIKVLGTPTREQIREM---NPNYTEFKFPQIKAHPW 201
Cdd:PHA03390 200 LTGKHPFKEDEDeeldLESLlkrqqkkLPFIKNVSKNANDFVQSMlkyNINYRLTNYNEIIKHPF 264
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
3-200 5.28e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 62.55  E-value: 5.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944     3 KLDHCNIVRLryffYSSGEKKDEvYLNLVLDYVPEtvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDI 82
Cdd:TIGR03903   34 RLYHPNIVAL----LDSGEAPPG-LLFAVFEYVPG---RTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944    83 KPQNLLLDP--DTAVLKLCDFG-----------SAKQLVR-GEpnvsYICSRYYRAPELIFGATdYTSSIDVWSAGCVLA 148
Cdd:TIGR03903  106 KPQNIMVSQtgVRPHAKVLDFGigtllpgvrdaDVATLTRtTE----VLGTPTYCAPEQLRGEP-VTPNSDLYAWGLIFL 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568995944   149 ELLLGQPIFPGDSgvdqLVEIIKvlgtptreqiREMNPNytEFKFPQ-IKAHP 200
Cdd:TIGR03903  181 ECLTGQRVVQGAS----VAEILY----------QQLSPV--DVSLPPwIAGHP 217
pknD PRK13184
serine/threonine-protein kinase; Reviewed
68-151 3.25e-06

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 47.46  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  68 SLAYIHSFGICHRDIKPQNLLLDPDTAVLKLcDFGSAK-------QLVRGEPNVSYICSRYYRAPELIFGATDY------ 134
Cdd:PRK13184 125 TIEYVHSKGVLHRDLKPDNILLGLFGEVVIL-DWGAAIfkkleeeDLLDIDVDERNICYSSMTIPGKIVGTPDYmaperl 203
                         90       100
                 ....*....|....*....|..
gi 568995944 135 -----TSSIDVWSAGCVLAELL 151
Cdd:PRK13184 204 lgvpaSESTDIYALGVILYQML 225
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1-256 0e+00

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: 532.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:cd14137   51 MRRLKHPNIVKLKYFFYSSGEKKDEVYLNLVMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHR 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  81 DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGD 160
Cdd:cd14137  131 DIKPQNLLVDPETGVLKLCDFGSAKRLVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 161 SGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKdspgaghftpgvrVFRPRTPPEAIALCSRLLEYTPTA 240
Cdd:cd14137  211 SSVDQLVEIIKVLGTPTREQIKAMNPNYTEFKFPQIKPHPWEK-------------VFPKRTPPDAIDLLSKILVYNPSK 277
                        250
                 ....*....|....*.
gi 568995944 241 RLTPLEACAHSFFDEL 256
Cdd:cd14137  278 RLTALEALAHPFFDEL 293
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
5-253 3.84e-82

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: 252.16  E-value: 3.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   5 DHCNIVRLRYFFYSSGEKkdevYLNLVLDYVPETVYRVARHYSRakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKP 84
Cdd:cd05118   57 GHPNIVKLLDVFEHRGGN----HLCLVFELMGMNLYELIKDYPR---GLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKP 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  85 QNLLLDPDTAVLKLCDFGSAKQLVRGEPNVsYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD 164
Cdd:cd05118  130 ENILINLELGQLKLADFGLARSFTSPPYTP-YVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVD 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 165 QLVEIIKVLGTptreqiremnpnytefkfpqikahpwtkdspgaghftpgvrvfrprtpPEAIALCSRLLEYTPTARLTP 244
Cdd:cd05118  209 QLAKIVRLLGT------------------------------------------------PEALDLLSKMLKYDPAKRITA 240

                 ....*....
gi 568995944 245 LEACAHSFF 253
Cdd:cd05118  241 SQALAHPYF 249
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
1-260 4.06e-69

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: 221.25  E-value: 4.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYS-SGEKKDEVYLnlVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICH 79
Cdd:cd07834   53 LRHLKHENIIGLLDILRPpSPEEFNDVYI--VTELMETDLHKVIK----SPQPLTDDHIQYFLYQILRGLKYLHSAGVIH 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  80 RDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEPNV---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPI 156
Cdd:cd07834  127 RDLKPSNILVN-SNCDLKICDFGLARGVDPDEDKGfltEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 157 FPGDSGVDQLVEIIKVLGTPTREQI-REMNPNYTEF--KFPQIKAHPWTKDSPGAghftpgvrvfrprtPPEAIALCSRL 233
Cdd:cd07834  206 FPGRDYIDQLNLIVEVLGTPSEEDLkFISSEKARNYlkSLPKKPKKPLSEVFPGA--------------SPEAIDLLEKM 271
                        250       260
                 ....*....|....*....|....*..
gi 568995944 234 LEYTPTARLTPLEACAHSFFDELRDPN 260
Cdd:cd07834  272 LVFNPKKRITADEALAHPYLAQLHDPE 298
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1-253 2.85e-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: 217.35  E-value: 2.85e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSsgekKDEVYLnlVLDYVPETVyrvaRHY-SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICH 79
Cdd:cd07829   52 LKELKHPNIVKLLDVIHT----ENKLYL--VFEYCDQDL----KKYlDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  80 RDIKPQNLLLDpDTAVLKLCDFGSAKQLvrGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPI 156
Cdd:cd07829  122 RDLKPQNLLIN-RDGVLKLADFGLARAF--GIPLRTYtheVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 157 FPGDSGVDQLVEIIKVLGTPTREQIREMN--PNYTeFKFPQIKAHPWTKdspgaghftpgvrVFrPRTPPEAIALCSRLL 234
Cdd:cd07829  199 FPGDSEIDQLFKIFQILGTPTEESWPGVTklPDYK-PTFPKWPKNDLEK-------------VL-PRLDPEGIDLLSKML 263
                        250
                 ....*....|....*....
gi 568995944 235 EYTPTARLTPLEACAHSFF 253
Cdd:cd07829  264 QYNPAKRISAKEALKHPYF 282
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1-253 6.37e-65

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: 209.10  E-value: 6.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDYVPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:cd07833   54 LRQLRHENIVNLKEAFRRKGR------LYLVFEYVERTLLELLEASPGG---LPPDAVRSYIWQLLQAIAYCHSHNIIHR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  81 DIKPQNLLLDPDtAVLKLCDFGSAKQLvRGEPNV---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF 157
Cdd:cd07833  125 DIKPENILVSES-GVLKLCDFGFARAL-TARPASpltDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLF 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 158 PGDSGVDQLVEIIKVLGT-PTREQIREM-NPNYTEFKFPQIKahpwtkdspgagHFTPGVRVFRPRTPPEAIALCSRLLE 235
Cdd:cd07833  203 PGDSDIDQLYLIQKCLGPlPPSHQELFSsNPRFAGVAFPEPS------------QPESLERRYPGKVSSPALDFLKACLR 270
                        250
                 ....*....|....*...
gi 568995944 236 YTPTARLTPLEACAHSFF 253
Cdd:cd07833  271 MDPKERLTCDELLQHPYF 288
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
5-253 8.83e-65

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: 208.34  E-value: 8.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   5 DHCNIVRLRYFFyssgekKDEVYLNLVLDYVPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKP 84
Cdd:cd07832   58 GHPYVVKLRDVF------PHGTGFVLVFEYMLSSLSEVLRDEERP---LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  85 QNLLLDpDTAVLKLCDFGSAKqLVRGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 161
Cdd:cd07832  129 ANLLIS-STGVLKIADFGLAR-LFSEEDPRLYshqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGEN 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 162 GVDQLVEIIKVLGTPTREQIREMN--PNYTEFKFPQIKAHPWTKdspgagHFtpgvrvfrPRTPPEAIALCSRLLEYTPT 239
Cdd:cd07832  207 DIEQLAIVLRTLGTPNEKTWPELTslPDYNKITFPESKGIRLEE------IF--------PDCSPEAIDLLKGLLVYNPK 272
                        250
                 ....*....|....
gi 568995944 240 ARLTPLEACAHSFF 253
Cdd:cd07832  273 KRLSAEEALRHPYF 286
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
5-260 4.13e-62

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: 203.17  E-value: 4.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   5 DHCNIVRLRYFFYSSGEKkdEVYLnlVLDYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKP 84
Cdd:cd07852   65 DHPNIIKLLNVIRAENDK--DIYL--VFEYMETDLHAVIR-----ANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKP 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  85 QNLLLDPDTAVlKLCDFGSAKQLVRGEPNVS------YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFP 158
Cdd:cd07852  136 SNILLNSDCRV-KLADFGLARSLSQLEEDDEnpvltdYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFP 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 159 GDSGVDQLVEIIKVLGTPTREQIREMNPNYTEfkfPQIKAHPWTKDSPGAGHFtpgvrvfrPRTPPEAIALCSRLLEYTP 238
Cdd:cd07852  215 GTSTLNQLEKIIEVIGRPSAEDIESIQSPFAA---TMLESLPPSRPKSLDELF--------PKASPDALDLLKKLLVFNP 283
                        250       260
                 ....*....|....*....|..
gi 568995944 239 TARLTPLEACAHSFFDELRDPN 260
Cdd:cd07852  284 NKRLTAEEALRHPYVAQFHNPA 305
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1-253 1.74e-61

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: 200.11  E-value: 1.74e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFyssGEKKdevYLNLVLDYVP---ETVYRvarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGI 77
Cdd:cd07841   56 LQELKHPNIIGLLDVF---GHKS---NINLVFEFMEtdlEKVIK------DKSIVLTPADIKSYMLMTLRGLEYLHSNWI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  78 CHRDIKPQNLLLDPDtAVLKLCDFGSAKQLvrGEPNVSYIC---SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQ 154
Cdd:cd07841  124 LHRDLKPNNLLIASD-GVLKLADFGLARSF--GSPNRKMTHqvvTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRV 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 155 PIFPGDSGVDQLVEIIKVLGTPTREQIREMN--PNYTEFKFpqikahpwtkdSPGaghfTPGVRVFrPRTPPEAIALCSR 232
Cdd:cd07841  201 PFLPGDSDIDQLGKIFEALGTPTEENWPGVTslPDYVEFKP-----------FPP----TPLKQIF-PAASDDALDLLQR 264
                        250       260
                 ....*....|....*....|.
gi 568995944 233 LLEYTPTARLTPLEACAHSFF 253
Cdd:cd07841  265 LLTLNPNKRITARQALEHPYF 285
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
2-253 2.55e-60

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: 196.60  E-value: 2.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   2 RKL-DHCNIVRLRYFFYSSGEkkdevyLNLVLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR 80
Cdd:cd07830   52 RKLnEHPNIVKLKEVFRENDE------LYFVFEYMEGNLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  81 DIKPQNLLLDPDTaVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGD 160
Cdd:cd07830  124 DLKPENLLVSGPE-VVKIADFGLAREIRSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGS 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 161 SGVDQLVEIIKVLGTPTREQIRE-------MNpnyteFKFPQIKAHPWTKdspgaghftpgvrvFRPRTPPEAIALCSRL 233
Cdd:cd07830  203 SEIDQLYKICSVLGTPTKQDWPEgyklaskLG-----FRFPQFAPTSLHQ--------------LIPNASPEAIDLIKDM 263
                        250       260
                 ....*....|....*....|
gi 568995944 234 LEYTPTARLTPLEACAHSFF 253
Cdd:cd07830  264 LRWDPKKRPTASQALQHPYF 283
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
2-253 2.23e-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: 194.71  E-value: 2.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   2 RKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSrAKQTLPviYVKLYMYQLFRSLAYIHSFGICHRD 81
Cdd:cd07840   53 QKLDHPNVVRLKEIVTSKGSAKYKGSIYMVFEYMDHDLTGLLDNPE-VKFTES--QIKCYMKQLLEGLQYLHSNGILHRD 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  82 IKPQNLLLDPDtAVLKLCDFGSAKQLVRgEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFP 158
Cdd:cd07840  130 IKGSNILINND-GVLKLADFGLARPYTK-ENNADYtnrVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 159 GDSGVDQLVEIIKVLGTPTRE---QIREMnPNYTEFKFPQikahpwtkdspgaghftPGVRVFRP----RTPPEAIALCS 231
Cdd:cd07840  208 GKTELEQLEKIFELCGSPTEEnwpGVSDL-PWFENLKPKK-----------------PYKRRLREvfknVIDPSALDLLD 269
                        250       260
                 ....*....|....*....|..
gi 568995944 232 RLLEYTPTARLTPLEACAHSFF 253
Cdd:cd07840  270 KLLTLDPKKRISADQALQHEYF 291
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
1-253 3.50e-54

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: 180.95  E-value: 3.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKLDHCNIVRLRYFFYSsgEKKdevyLNLVLDYVPETVyrvaRHY--SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGIC 78
Cdd:cd07835   52 LKELNHPNIVRLLDVVHS--ENK----LYLVFEFLDLDL----KKYmdSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944  79 HRDIKPQNLLLDpDTAVLKLCDFGSAKQLvrGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQP 155
Cdd:cd07835  122 HRDLKPQNLLID-TEGALKLADFGLARAF--GVPVRTYtheVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRP 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944 156 IFPGDSGVDQLVEIIKVLGTPTREQ---IREMnPNYTEfKFPQIKAHPWTKDSPGaghftpgvrvfrprTPPEAIALCSR 232
Cdd:cd07835  199 LFPGDSEIDQLFRIFRTLGTPDEDVwpgVTSL-PDYKP-TFPKWARQDLSKVVPS--------------LDEDGLDLLSQ 262
                        250       260
                 ....*....|....*....|.
gi 568995944 233 LLEYTPTARLTPLEACAHSFF 253
Cdd:cd07835  263 MLVYDPAKRISAKAALQHPYF 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1-253 3.60e-54

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: 180.55  E-value: 3.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995944   1 MRKL-DHCNIVRLRYFFYSSGEKKdevyLNLVLDYVPETVYRVARhySRaKQTLPVIYVKLYMYQLFRSLAYIHSFGICH 79
Cdd:cd07831   51 LRRLsPHPNI