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Conserved domains on  [gi|49574532|ref|NP_063937.2|]
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glycogen synthase kinase-3 alpha [Homo sapiens]

Protein Classification

STKc_GSK3 domain-containing protein (domain architecture ID 10197641)

STKc_GSK3 domain-containing protein

Graphical summary

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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 ...
114-406 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: 638.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 114 SQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNL 193
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 194 VLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRG 273
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 274 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 353
Cdd:cd14137 161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 49574532 354 FKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDEL 406
Cdd:cd14137 241 FKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
114-406 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: 638.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 114 SQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNL 193
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 194 VLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRG 273
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 274 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 353
Cdd:cd14137 161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 49574532 354 FKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDEL 406
Cdd:cd14137 241 FKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
123-309 2.51e-09

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 57.27  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532  123 KVIGNGSFGVVYQARLAE----TRELVAIKKVLQDKRF------------KNRELQIMR--KLDHCNIVRlryfFYSSGE 184
Cdd:PHA02882  18 KLIGCGGFGCVYETQCASdhciNNQAVAKIENLENETIvmetlvynniydIDKIALWKNihNIDHLGIPK----YYGCGS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532  185 -KKDELYLNLVLEyvpETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLkLCD 263
Cdd:PHA02882  94 fKRCRMYYRFILL---EKLVENTKEIFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGY-IID 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 49574532  264 FGSAKQLVRGEPNVsyicsRYYRAPELIFGATDYTSSIDVWSAGCV 309
Cdd:PHA02882 170 YGIASHFIIHGKHI-----EYSKEQKDLHRGTLYYAGLDAHNGACV 210
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
113-430 4.73e-143

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 420.60  E-value: 4.73e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532  113 RSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDE--LY 190
Cdd:PTZ00036  62 RSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHINIIFLKDYYYTECFKKNEknIF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532  191 LNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQL 270
Cdd:PTZ00036 142 LNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKLCDFGSAKNL 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532  271 VRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPN 350
Cdd:PTZ00036 222 LAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPTEDQLKEMNPN 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532  351 YTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNN-RPLPPLFNFSAGE 429
Cdd:PTZ00036 302 YADIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDPCIKLPKYiDKLPDLFNFCDAE 381

                 .
gi 49574532  430 L 430
Cdd:PTZ00036 382 I 382
Pkinase pfam00069
Protein kinase domain;
119-403 1.91e-86

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 268.31  E-value: 1.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532   119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFyssgEKKDELYLn 192
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAVKKIKKEKIKKKkdknvlREIKILKKLNHPNIVRLYDVF----EDKDHLYL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532   193 lVLEYVP----ETVYRVARHFTKAkltipilYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDtAVLKLCDFGSAK 268
Cdd:pfam00069  76 -VLEYVEggslFDLLSEKGAFSER-------EAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDED-GNLKITDFGLAK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532   269 QLVRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIkvlgtptreqIREmn 348
Cdd:pfam00069 147 QLSSGSKLTTFVGTPWYMAPEVL-RGNPYGPKVDVWSLGCILYELLTGKPPFPGING-DTLYELI----------IDQ-- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 49574532   349 pnyTEFKFPqikahPWTKVfksrtPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:pfam00069 213 ---LDLSSP-----RPSSI-----SEEAKDLLKKLLKKDPSKRLTATQALQHPWF 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
119-403 4.13e-81

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 254.38  E-value: 4.13e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532    119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFyssgEKKDELYLnl 193
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrerilREIKILKKLKHPNIVRLYDVF----EDEDKLYL-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532    194 VLEYVPetvYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTaVLKLCDFGSAKQLVRG 273
Cdd:smart00220  75 VMEYCE---GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG-HVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532    274 EPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvDQLVEIIKVLGTPTREQIREMNPnyte 353
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFPPPEWD---- 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 49574532    354 fkfpqikahpwtkvfksrTPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:smart00220 223 ------------------ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
119-483 9.27e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 186.87  E-value: 9.27e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYqarLAETRELVAIKKVLQDKRFKN-------RELQIMRKLDHC-NIVRLRYFFYSSGekkdelY 190
Cdd:COG0515   2 YRILRKLGEGSFGEVY---LARDRKLVALKVLAKKLESKSkeverflREIQILASLNHPpNIVKLYDFFQDEG------S 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 191 LNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQL 270
Cdd:COG0515  73 LYLVMEYVDGGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVKLIDFGLAKLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 271 VRGEPNV-------SYICSRYYRAPELIFGATD--YTSSIDVWSAGCVLAELLLGQPIFPGDSG---VDQLVEIIKVLGT 338
Cdd:COG0515 153 PDPGSTSsipalpsTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYELLTGLPPFEGEKNssaTSQTLKIILELPT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 339 PtreqiremnpnytefkfpqIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRP 418
Cdd:COG0515 233 P-------------------SLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLK 293
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49574532 419 LPPLFNFSageLSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS 483
Cdd:COG0515 294 PDDSAPLR---LSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLST 355
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
140-372 2.24e-16

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: 81.04  E-value: 2.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532    140 ETRELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDELyLNLVLEYVPEtvyRVARHFTK 211
Cdd:TIGR03903    1 MTGHEVAIKLLRTDapeeehqrARFR-RETALCARLYHPNIVAL----LDSGEAPPGL-LFAVFEYVPG---RTLREVLA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532    212 AKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDP--DTAVLKLCDFG-----------SAKQLVR-GEpnv 277
Cdd:TIGR03903   72 ADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQtgVRPHAKVLDFGigtllpgvrdaDVATLTRtTE--- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532    278 sYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVEIIKvlgtptreqiREMNPNytEFKFP 357
Cdd:TIGR03903  149 -VLGTPTYCAPEQLRGEP-VTPNSDLYAWGLIFLECLTGQRVVQGAS----VAEILY----------QQLSPV--DVSLP 210
                          250
                   ....*....|....*.
gi 49574532    358 Q-IKAHPWTKVFKSRT 372
Cdd:TIGR03903  211 PwIAGHPLGQVLRKAL 226
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
114-406 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: 638.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 114 SQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNL 193
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 194 VLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRG 273
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 274 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 353
Cdd:cd14137 161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 49574532 354 FKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDEL 406
Cdd:cd14137 241 FKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
119-403 9.67e-100

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: 302.62  E-value: 9.67e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKN---RELQIMRKL----DHCNIVRLRYFFYSSGEKkdelYL 191
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKHLndveGHPNIVKLLDVFEHRGGN----HL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 192 NLVLEYVPETVYRVARHFtkaKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLV 271
Cdd:cd05118  77 CLVFELMGMNLYELIKDY---PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLADFGLARSFT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 272 RGEPNVsYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTptreqiremnpny 351
Cdd:cd05118 154 SPPYTP-YVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGT------------- 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 49574532 352 tefkfpqikahpwtkvfksrtpPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd05118 220 ----------------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
119-403 1.18e-84

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: 264.73  E-value: 1.18e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRfKN-------RELQIMRKLDHCNIVRLRYFFYSsgekKDELYL 191
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNE-EEgipstalREISLLKELKHPNIVKLLDVIHT----ENKLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 192 nlVLEYVPetvYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDpDTAVLKLCDFGSAKQLv 271
Cdd:cd07829  76 --VFEYCD---QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN-RDGVLKLADFGLARAF- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 272 rGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN 348
Cdd:cd07829 149 -GIPLRTYtheVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGVT 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 49574532 349 --PNYTeFKFPQIKAHPWTKVFKSRTpPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd07829 228 klPDYK-PTFPKWPKNDLEKVLPRLD-PEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
119-407 2.73e-83

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: 262.85  E-value: 2.73e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLqdKRFKN--------RELQIMRKLDHCNIVRLRYFFYS-SGEKKDEL 189
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIS--NVFDDlidakrilREIKILRHLKHENIIGLLDILRPpSPEEFNDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 190 YLnlVLEYVPETVYRVARhfTKAKLTIpiLYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDpDTAVLKLCDFGSAKQ 269
Cdd:cd07834  80 YI--VTELMETDLHKVIK--SPQPLTD--DHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVN-SNCDLKICDFGLARG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 270 LVRGEPNV---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI-R 345
Cdd:cd07834 153 VDPDEDKGfltEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLkF 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49574532 346 EMNPNYTEF--KFPQIKAHPWTKVFKsRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELR 407
Cdd:cd07834 233 ISSEKARNYlkSLPKKPKKPLSEVFP-GASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLH 295
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
119-403 2.46e-79

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: 250.91  E-value: 2.46e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQdkRFKN-------RELQIMRKL-DHCNIVRLRYFFYssgeKKDELY 190
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKK--KFYSweecmnlREVKSLRKLnEHPNIVKLKEVFR----ENDELY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 191 LnlVLEYVPETVYRVARHFTKAKLTIPIlyVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTaVLKLCDFGSAKQL 270
Cdd:cd07830  75 F--VFEYMEGNLYQLMKDRKGKPFSESV--IRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE-VVKIADFGLAREI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 271 VRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIRE---- 346
Cdd:cd07830 150 RSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPEgykl 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 347 ---MNpnyteFKFPQIKAHPWTKVFkSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd07830 230 askLG-----FRFPQFAPTSLHQLI-PNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
119-414 4.27e-79

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: 250.95  E-value: 4.27e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKN---------RELQIMRKLDHCNIVRLRYFFyssGEKKdel 189
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdginftalREIKLLQELKHPNIIGLLDVF---GHKS--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 190 YLNLVLEYVP---ETVYR-VARHFTKAkltipilYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDtAVLKLCDFG 265
Cdd:cd07841  76 NINLVFEFMEtdlEKVIKdKSIVLTPA-------DIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASD-GVLKLADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 266 SAKQLvrGEPNVSYIC---SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE 342
Cdd:cd07841 148 LARSF--GSPNRKMTHqvvTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEE 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49574532 343 QIREMN--PNYTEFKFpqIKAHPWTKVFKSRtPPEAIALCSSLLEYTPSSRLSPLEACAHSFF--DELRCLGTQLP 414
Cdd:cd07841 226 NWPGVTslPDYVEFKP--FPPTPLKQIFPAA-SDDALDLLQRLLTLNPNKRITARQALEHPYFsnDPAPTPPSQLP 298
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
118-403 1.45e-78

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: 249.16  E-value: 1.45e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 118 AYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQ---DKRFKN---RELQIMRKLDHCNIVRLRYFFYSSGEkkdeLYL 191
Cdd:cd07833   2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKEsedDEDVKKtalREVKVLRQLRHENIVNLKEAFRRKGR----LYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 192 nlVLEYVPETVYRVARHFTKAkltIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDtAVLKLCDFGSAKQLv 271
Cdd:cd07833  78 --VFEYVERTLLELLEASPGG---LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSES-GVLKLCDFGFARAL- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 272 RGEPNV---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT-PTREQIREM 347
Cdd:cd07833 151 TARPASpltDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPlPPSHQELFS 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 49574532 348 -NPNYTEFKFPQIKaHPWT--KVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd07833 231 sNPRFAGVAFPEPS-QPESleRRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
119-403 1.94e-78

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: 248.78  E-value: 1.94e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKL-------DHCNIVRLRYFFyssgekKDELYL 191
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIkalqacqGHPYVVKLRDVF------PHGTGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 192 NLVLEYVPETVYRVARHFTKAkltIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDpDTAVLKLCDFGSAKqLV 271
Cdd:cd07832  76 VLVFEYMLSSLSEVLRDEERP---LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS-STGVLKIADFGLAR-LF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 272 RGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN 348
Cdd:cd07832 151 SEEDPRLYshqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKTWPELT 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 49574532 349 --PNYTEFKFPQIKAHPWTKVFKSrTPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd07832 231 slPDYNKITFPESKGIRLEEIFPD-CSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
119-403 5.34e-77

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: 245.17  E-value: 5.34e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVlqdkRFKN----------RELQIMRKLDHCNIVRLRYFFYSSGEKKDE 188
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKI----RMENekegfpitaiREIKLLQKLDHPNVVRLKEIVTSKGSAKYK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 189 LYLNLVLEYVPETVYRVARHfTKAKLTIPilYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDtAVLKLCDFGSAK 268
Cdd:cd07840  77 GSIYMVFEYMDHDLTGLLDN-PEVKFTES--QIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND-GVLKLADFGLAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 269 QLVRgEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE--- 342
Cdd:cd07840 153 PYTK-ENNADYtnrVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEEnwp 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49574532 343 QIREMnPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd07840 232 GVSDL-PWFENLKPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
122-403 5.20e-71

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: 230.91  E-value: 5.20e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 122 IKVIGNGSFGVVYQARLAETRELVAIKKVLQdkRFKN--------RELQIMRKL-DHCNIVRLRYFFYSSGEKkdELYLn 192
Cdd:cd07852  12 LKKLGKGAYGIVWKAIDKKTGEVVALKKIFD--AFRNatdaqrtfREIMFLQELnDHPNIIKLLNVIRAENDK--DIYL- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 193 lVLEYVPETVYRVARhftkAKLTIPIlYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVlKLCDFGSAKQLVR 272
Cdd:cd07852  87 -VFEYMETDLHAVIR----ANILEDI-HKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRV-KLADFGLARSLSQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 273 GEPNVS------YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIRE 346
Cdd:cd07852 160 LEEDDEnpvltdYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGRPSAEDIES 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 347 MNPNYTE---FKFPQIKAHPWTKVFKSrTPPEAIALCSSLLEYTPSSRLSPLEACAHSFF 403
Cdd:cd07852 240 IQSPFAAtmlESLPPSRPKSLDELFPK-ASPDALDLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
119-403 3.45e-68

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: 221.78  E-value: 3.45e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 119 YTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYSsgEKKdeLYLn 192
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGvpstaiREISLLKELNHPNIVRLLDVVHS--ENK--LYL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 193 lVLEYVPETVYRVARHFTKAKLTIPIlyVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDpDTAVLKLCDFGSAKQLvr 272
Cdd:cd07835  76 -VFEFLDLDLKKYMDSSPLTGLDPPL--IKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLID-TEGALKLADFGLARAF-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49574532 273 GEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEI