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Conserved domains on  [gi|21361340|ref|NP_002084|]
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glycogen synthase kinase-3 beta isoform 1 [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 ...
51-356 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  Cd Length: 293  Bit Score: 639.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  51 PQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 131 VLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14137 161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361340 291 FKFPQIKAHPWTKdssgtghftsgvrVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 356
Cdd:cd14137 241 FKFPQIKPHPWEK-------------VFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
51-356 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  Cd Length: 293  Bit Score: 639.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  51 PQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 131 VLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14137 161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361340 291 FKFPQIKAHPWTKdssgtghftsgvrVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 356
Cdd:cd14137 241 FKFPQIKPHPWEK-------------VFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
29-380 1.90e-148

glycogen synthase kinase; Provisional


Pssm-ID: 173333  Cd Length: 440  Bit Score: 433.69  E-value: 1.90e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340   29 SRDKDGSKVTTVVATPGQGPDRpqevSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN 108
Cdd:PTZ00036  45 NAGEDEDEEKMIDNDINRSPNK----SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHIN 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  109 IVRLRYFFYSSGEKKDE--VYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN 186
Cdd:PTZ00036 121 IIFLKDYYYTECFKKNEknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQN 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  187 LLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:PTZ00036 201 LLIDPNTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  267 VEIIKVLGTPTREQIREMNPNYTEFKFPQIKahpwTKDSSgtghftsgvRVFRPRTPPEAIALCSRLLEYTPTARLTPLE 346
Cdd:PTZ00036 281 VRIIQVLGTPTEDQLKEMNPNYADIKFPDVK----PKDLK---------KVFPKGTPDDAINFISQFLKYEPLKRLNPIE 347
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 21361340  347 ACAHSFFDELRDPNVKLPNGRDT-PALFNFTTQEL 380
Cdd:PTZ00036 348 ALADPFFDDLRDPCIKLPKYIDKlPDLFNFCDAEI 382
Pkinase pfam00069
Protein kinase domain;
56-353 1.82e-82

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 257.53  E-value: 1.82e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLN 129
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAFE------DKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340   130 LVLDYVPETVYrvARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVR 209
Cdd:pfam00069  75 LVLEYVEGGSL--FDLLSEKG-AFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDED-GNLKITDFGLARQLNS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340   210 GEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIkvlgtptreqIREmnpnyt 289
Cdd:pfam00069 151 GSSLTSFVGTPWYMAPEVL-RGNPYGPKVDVWSLGCILYELLTGKPPFPGING-NEIYEKI----------IDQ------ 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361340   290 EFKFPqikahPWTKDSsgtghftsgvrvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:pfam00069 213 DFDSP-----RPSSIS------------------EEAKDLLKKLLKKDPSKRLTATEALQHPWF 253
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
56-353 1.80e-80

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 252.45  E-value: 1.80e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340     56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNL 130
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrerilREIKILKKLKHPNIVRLYDVFE------DEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    131 VLDYVPetvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRG 210
Cdd:smart00220  75 VMEYCE---GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG-HVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    211 EPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvDQLVEIIKVLGTPTREQIREMnpnyte 290
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFPPPE------ 220
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361340    291 fkfpqikahpwtkdssgtghftsgvrvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:smart00220 221 -----------------------------WDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
55-386 1.39e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 186.10  E-value: 1.39e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  55 SYTDTKVIGNGSFGVVYQAKlcdSGELVAIKKVLQDKRFKN-------RELQIMRKLDHC-NIVRLRYFFYSSGekkdev 126
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLAR---DRKLVALKVLAKKLESKSkeverflREIQILASLNHPpNIVKLYDFFQDEG------ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 127 YLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQ 206
Cdd:COG0515  72 SLYLVMEYVDGGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVKLIDFGLAKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 207 LVRGEPNV-------SYICSRYYRAPELIFGATD--YTSSIDVWSAGCVLAELLLGQPIFPGDSG---VDQLVEIIKVLG 274
Cdd:COG0515 152 LPDPGSTSsipalpsTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYELLTGLPPFEGEKNssaTSQTLKIILELP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 275 TPtreqiremnpnytEFKFPQIKAHPWTKdssgtghftsgvrvfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFFD 354
Cdd:COG0515 232 TP-------------SLASPLSPSNPELI-------------------SKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA 279
                       330       340       350
                ....*....|....*....|....*....|..
gi 21361340 355 ELRDPNVKLPNGRDTPALFNFTTQELSSNPPL 386
Cdd:COG0515 280 HLKLKESDLSDLLKPDDSAPLRLSLPPSLEAL 311
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
77-300 1.43e-14

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  Cd Length: 1266  Bit Score: 76.04  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340     77 DSGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEvYLNLVLDYVPEtvyRVARHYSR 148
Cdd:TIGR03903    1 MTGHEVAIKLLRTDapeeehqrARFR-RETALCARLYHPNIVAL----LDSGEAPPG-LLFAVFEYVPG---RTLREVLA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    149 AKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFG-----------SAKQLVR-GEpnv 214
Cdd:TIGR03903   72 ADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQtgVRPHAKVLDFGigtllpgvrdaDVATLTRtTE--- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    215 sYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVEIIKvlgtptreqiREMNPnyTEFKFP 294
Cdd:TIGR03903  149 -VLGTPTYCAPEQLRGEP-VTPNSDLYAWGLIFLECLTGQRVVQGAS----VAEILY----------QQLSP--VDVSLP 210

                   ....*..
gi 21361340    295 Q-IKAHP 300
Cdd:TIGR03903  211 PwIAGHP 217
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
51-356 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  Cd Length: 293  Bit Score: 639.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  51 PQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 131 VLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14137 161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361340 291 FKFPQIKAHPWTKdssgtghftsgvrVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 356
Cdd:cd14137 241 FKFPQIKPHPWEK-------------VFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
29-380 1.90e-148

glycogen synthase kinase; Provisional


Pssm-ID: 173333  Cd Length: 440  Bit Score: 433.69  E-value: 1.90e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340   29 SRDKDGSKVTTVVATPGQGPDRpqevSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN 108
Cdd:PTZ00036  45 NAGEDEDEEKMIDNDINRSPNK----SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHIN 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  109 IVRLRYFFYSSGEKKDE--VYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN 186
Cdd:PTZ00036 121 IIFLKDYYYTECFKKNEknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQN 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  187 LLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:PTZ00036 201 LLIDPNTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  267 VEIIKVLGTPTREQIREMNPNYTEFKFPQIKahpwTKDSSgtghftsgvRVFRPRTPPEAIALCSRLLEYTPTARLTPLE 346
Cdd:PTZ00036 281 VRIIQVLGTPTEDQLKEMNPNYADIKFPDVK----PKDLK---------KVFPKGTPDDAINFISQFLKYEPLKRLNPIE 347
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 21361340  347 ACAHSFFDELRDPNVKLPNGRDT-PALFNFTTQEL 380
Cdd:PTZ00036 348 ALADPFFDDLRDPCIKLPKYIDKlPDLFNFCDAEI 382
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
56-353 1.31e-102

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  Cd Length: 249  Bit Score: 309.16  E-value: 1.31e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN---RELQIMRKL----DHCNIVRLRYFFYSSGEKkdevYL 128
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKHLndveGHPNIVKLLDVFEHRGGN----HL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 129 NLVLDYVPETVYRVARHYSRakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLV 208
Cdd:cd05118  77 CLVFELMGMNLYELIKDYPR---GLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLADFGLARSFT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 209 RGEPNVsYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTptreqiremnpny 288
Cdd:cd05118 154 SPPYTP-YVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGT------------- 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361340 289 tefkfpqikahpwtkdssgtghftsgvrvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:cd05118 220 -----------------------------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
56-360 1.33e-84

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  Cd Length: 329  Bit Score: 265.54  E-value: 1.33e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLqdKRFKN--------RELQIMRKLDHCNIVRLRYFFYS-SGEKKDEV 126
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIS--NVFDDlidakrilREIKILRHLKHENIIGLLDILRPpSPEEFNDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 127 YLnlVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd07834  80 YI--VTELMETDLHKVIK----SPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVN-SNCDLKICDFGLARG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 207 LVRGEPNV---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI-R 282
Cdd:cd07834 153 VDPDEDKGfltEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLkF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 283 EMNPNYTEF--KFPQIKAHPWTKdssgtghftsgvrVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 360
Cdd:cd07834 233 ISSEKARNYlkSLPKKPKKPLSE-------------VF-PGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPE 298
Pkinase pfam00069
Protein kinase domain;
56-353 1.82e-82

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 257.53  E-value: 1.82e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLN 129
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAFE------DKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340   130 LVLDYVPETVYrvARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVR 209
Cdd:pfam00069  75 LVLEYVEGGSL--FDLLSEKG-AFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDED-GNLKITDFGLARQLNS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340   210 GEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIkvlgtptreqIREmnpnyt 289
Cdd:pfam00069 151 GSSLTSFVGTPWYMAPEVL-RGNPYGPKVDVWSLGCILYELLTGKPPFPGING-NEIYEKI----------IDQ------ 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361340   290 EFKFPqikahPWTKDSsgtghftsgvrvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:pfam00069 213 DFDSP-----RPSSIS------------------EEAKDLLKKLLKKDPSKRLTATEALQHPWF 253
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
56-353 9.44e-82

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  Cd Length: 282  Bit Score: 256.64  E-value: 9.44e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRfKN-------RELQIMRKLDHCNIVRLRYFFYSsgekKDEVYL 128
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNE-EEgipstalREISLLKELKHPNIVKLLDVIHT----ENKLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 129 nlVLDYVPETVyrvaRHY-SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd07829  76 --VFEYCDQDL----KKYlDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN-RDGVLKLADFGLARAF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 208 vrGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd07829 149 --GIPLRTYtheVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGV 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361340 285 N--PNYTeFKFPQIKAHPWTKdssgtghftsgvrVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:cd07829 227 TklPDYK-PTFPKWPKNDLEK-------------VL-PRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
56-353 1.80e-80

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 252.45  E-value: 1.80e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340     56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNL 130
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrerilREIKILKKLKHPNIVRLYDVFE------DEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    131 VLDYVPetvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRG 210
Cdd:smart00220  75 VMEYCE---GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG-HVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340    211 EPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvDQLVEIIKVLGTPTREQIREMnpnyte 290
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFPPPE------ 220
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361340    291 fkfpqikahpwtkdssgtghftsgvrvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:smart00220 221 -----------------------------WDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
61-353 7.64e-77

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  Cd Length: 288  Bit Score: 244.15  E-value: 7.64e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQ---DKRFKN---RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDY 134
Cdd:cd07833   8 VVGEGAYGVVLKCRNKATGEIVAIKKFKEsedDEDVKKtalREVKVLRQLRHENIVNLKEAFRRKGR------LYLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 135 VPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLvRGEPNV 214
Cdd:cd07833  82 VERTLLELLEASPGG---LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSES-GVLKLCDFGFARAL-TARPAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 215 ---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT-PTREQIREM-NPNYT 289
Cdd:cd07833 157 pltDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPlPPSHQELFSsNPRFA 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361340 290 EFKFPQIKaHPWTKDssgtghftsgvRVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:cd07833 237 GVAFPEPS-QPESLE-----------RRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
56-353 4.02e-76

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  Cd Length: 287  Bit Score: 242.23  E-value: 4.02e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKL-------DHCNIVRLRYFFyssgekKDEVYL 128
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIkalqacqGHPYVVKLRDVF------PHGTGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 129 NLVLDYVPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqLV 208
Cdd:cd07832  76 VLVFEYMLSSLSEVLRDEERP---LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS-STGVLKIADFGLAR-LF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 209 RGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN 285
Cdd:cd07832 151 SEEDPRLYshqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKTWPELT 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 286 --PNYTEFKFPQIKAHPWTKdssgtgHFtsgvrvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:cd07832 231 slPDYNKITFPESKGIRLEE------IF--------PDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
56-353 1.72e-75

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  Cd Length: 283  Bit Score: 240.51  E-value: 1.72e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQdkRFKN-------RELQIMRKL-DHCNIVRLRYFFYSSGEkkdevy 127
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKK--KFYSweecmnlREVKSLRKLnEHPNIVKLKEVFRENDE------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 128 LNLVLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQL 207
Cdd:cd07830  73 LYFVFEYMEGNLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE-VVKIADFGLAREI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 208 VRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIRE---- 283
Cdd:cd07830 150 RSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPEgykl 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361340 284 ---MNpnyteFKFPQIKAHPWTKdssgtghftsgvrvFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:cd07830 230 askLG-----FRFPQFAPTSLHQ--------------LIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
56-353 1.49e-73

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  Cd Length: 298  Bit Score: 235.93  E-value: 1.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN---------RELQIMRKLDHCNIVRLRYFFyssGEKKdev 126
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdginftalREIKLLQELKHPNIIGLLDVF---GHKS--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 127 YLNLVLDYVP---ETVYRvarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGS 203
Cdd:cd07841  76 NINLVFEFMEtdlEKVIK------DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASD-GVLKLADFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 204 AKQLvrGEPNVSYIC---SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQ 280
Cdd:cd07841 149 ARSF--GSPNRKMTHqvvTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEEN 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361340 281 IREMN--PNYTEFKFpqIKAHPWTKdssgtghftsgvrVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 353
Cdd:cd07841 227 WPGVTslPDYVEFKP--FPPTPLKQ-------------IF-PAASDDALDLLQRLLTLNPNKRITARQALEHPYF 285
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
62-353 3.56e-71

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  Cd Length: 291  Bit Score: 229.37  E-value: 3.56e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN----------RELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLV 131
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKKI----RMENekegfpitaiREIKLLQKLDHPNVVRLKEIVTSKGSAKYKGSIYMV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 132 LDYVPETVYRVARHYSrAKQTLPviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVRgE 211
Cdd:cd07840  83 FEYMDHDLTGLLDNPE-VKFTES--QIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND-GVLKLADFGLARPYTK-E 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361340 212 PNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQiremnpny