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Conserved domains on  [gi|14532736|gb|AAK64069|]
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putative protein kinase [Arabidopsis thaliana]

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List of domain hits

Name Accession Description Interval E-value
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
213-497 4.82e-144

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: 426.60  E-value: 4.82e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVS----SSLY 288
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKGSakykGSIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 289 LVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSV 368
Cdd:cd07840  81 MVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 369 SLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSA 447
Cdd:cd07840 161 DYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGvSDLPWFE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14532736 448 GFKTAIPYRRKVSEMFKDF-PASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07840 241 NLKPKKPYKRRLREVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
213-497 2.92e-85

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 272.10  E-value: 2.92e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvsSSLYLVFE 292
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    293 YMDH-DLLGLSSLPGvKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPakSVSLT 371
Cdd:smart00220  78 YCEGgDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    372 SHVVTLWYRPPELLLGaSHYGVGVDLWSTGCILGELYAGKPILPGKtevEQLHKIFKLCGSPTENYWrkqklpssagfkt 451
Cdd:smart00220 155 TFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFP------------- 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 14532736    452 aiPYRRKVSEMFKDFpasvlslLETLLSIDPDHRSSADRALESEYF 497
Cdd:smart00220 218 --PPEWDISPEAKDL-------IRKLLVKDPEKRLTAEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
213-497 4.82e-144

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: 426.60  E-value: 4.82e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVS----SSLY 288
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKGSakykGSIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 289 LVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSV 368
Cdd:cd07840  81 MVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 369 SLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSA 447
Cdd:cd07840 161 DYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGvSDLPWFE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14532736 448 GFKTAIPYRRKVSEMFKDF-PASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07840 241 NLKPKKPYKRRLREVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
213-497 2.92e-85

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 272.10  E-value: 2.92e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvsSSLYLVFE 292
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    293 YMDH-DLLGLSSLPGvKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPakSVSLT 371
Cdd:smart00220  78 YCEGgDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    372 SHVVTLWYRPPELLLGaSHYGVGVDLWSTGCILGELYAGKPILPGKtevEQLHKIFKLCGSPTENYWrkqklpssagfkt 451
Cdd:smart00220 155 TFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFP------------- 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 14532736    452 aiPYRRKVSEMFKDFpasvlslLETLLSIDPDHRSSADRALESEYF 497
Cdd:smart00220 218 --PPEWDISPEAKDL-------IRKLLVKDPEKRLTAEEALQHPFF 254
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
219-510 2.69e-83

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 270.09  E-value: 2.69e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  219 IGQGTYSSVYRARDLLHNKIVALKKVR-----------FDLNDMESVKFMA-REIIVMRRLDHPNVLkleGLITAPVSSS 286
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKiieisndvtkdRQLVGMCGIHFTTlRELKIMNEIKHENIM---GLVDVYVEGD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  287 -LYLVFEYMDHDLLGLSSlPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF--- 362
Cdd:PTZ00024  94 fINLVMDIMASDLKKVVD-RKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYgyp 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  363 ----------DPAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGS 432
Cdd:PTZ00024 173 pysdtlskdeTMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELLGT 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14532736  433 PTENYW-RKQKLPSSAGFKTAIPyrRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLP 510
Cdd:PTZ00024 253 PNEDNWpQAKKLPLYTEFTPRKP--KDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDPLPCDPSQLP 329
Pkinase pfam00069
Protein kinase domain;
213-497 2.03e-79

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 256.79  E-value: 2.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736   213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvsSSLYLVFE 292
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDK--DHLYLVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736   293 YMDH-DLLGLSSlPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDpAKSVSLT 371
Cdd:pfam00069  79 YCEGgDLFDYLS-RGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLT-KSSSSLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736   372 SHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWrkqklpssagfkt 451
Cdd:pfam00069 157 TFVGTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDE------------- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 14532736   452 aiPYRRKVSEMFKDFpasvlslLETLLSIDPDHRSSADRALESEYF 497
Cdd:pfam00069 224 --PKSDSGSEEAKDL-------IKKCLNKDPSKRPTAEEILQHPWF 260
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
213-498 4.86e-74

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 243.57  E-value: 4.86e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDmESVKFMA-REIIVMRRLDHPNVLKLEGLITApvSSSLYLVF 291
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQED-EGVPSTAiREISLLKEMQHGNIVRLQDVVHS--EKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  292 EYMDHDLLG-LSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLID-SKGVLKIADFGLATFFD-PAKSv 368
Cdd:PLN00009  81 EYLDLDLKKhMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARAFGiPVRT- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  369 sLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSsa 447
Cdd:PLN00009 160 -FTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGvTSLPD-- 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14532736  448 gFKTAIPYRRKvsemfKDFPASV-------LSLLETLLSIDPDHRSSADRALESEYFK 498
Cdd:PLN00009 237 -YKSAFPKWPP-----KDLATVVptlepagVDLLSKMLRLDPSKRITARAALEHEYFK 288
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
213-582 2.14e-45

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


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 166.46  E-value: 2.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDllhNKIVALKKVRFDL-NDMESVKFMAREIIVMRRLDHP-NVLKLEGLITapVSSSLYLV 290
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLeSKSKEVERFLREIQILASLNHPpNIVKLYDFFQ--DEGSLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 291 FEYMDHDLLGL---SSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKG-VLKIADFGLATFFDPAK 366
Cdd:COG0515  77 MEYVDGGSLEDllkKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDPG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 367 SVS-----LTSHVVTLWYRPPELLLGAS--HYGVGVDLWSTGCILGELYAGKPILPGKTE---VEQLHKIFKLCGSPTEN 436
Cdd:COG0515 157 STSsipalPSTSVGTPGYMAPEVLLGLSlaYASSSSDIWSLGITLYELLTGLPPFEGEKNssaTSQTLKIILELPTPSLA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 437 YWRKQKLPSsagfktaipyrrkvsemfkDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLPKYPPSK 516
Cdd:COG0515 237 SPLSPSNPE-------------------LISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDS 297
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14532736 517 EIDAKmrDEAKRQQPMRAEKQERQDSMTRISHERKFVPPVKANNSLSMTMEKQYKDLRSRNDSFKS 582
Cdd:COG0515 298 APLRL--SLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRS 361
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
242-428 1.64e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 84.75  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  242 KKVRfdlNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSSL------YLVFEYMDHDLLGLSSLPGVKftepQVK 315
Cdd:PHA03210 198 KRVK---AGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMitqkydFDLYSFMYDEAFDWKDRPLLK----QTR 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  316 CYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSVSLTSHVVTLWYRPPELLLGASHYGVgV 395
Cdd:PHA03210 271 AIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDYGWVGTVATNSPEILAGDGYCEI-T 349
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 14532736  396 DLWSTGCILGELYAgKPILP----GKTEVEQLHKIFK 428
Cdd:PHA03210 350 DIWSCGLILLDMLS-HDFCPigdgGGKPGKQLLKIID 385
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
239-425 1.59e-13

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: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 72.96  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    239 VALKKVRFD-LNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvSSSLYLVFEYMD-HDLLGLSSLPGVKFTEPQVKc 316
Cdd:TIGR03903    6 VAIKLLRTDaPEEEHQRARFRRETALCARLYHPNIVALLDSGEAP-PGLLFAVFEYVPgRTLREVLAADGALPAGETGR- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    317 YMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGV---LKIADFGLATFF------DPAKSVSLTSHVVTLWYRPPELLLG 387
Cdd:TIGR03903   84 LMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLpgvrdaDVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 14532736    388 AShYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHK 425
Cdd:TIGR03903  164 EP-VTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ 200
pknD PRK13184
serine/threonine-protein kinase; Reviewed
213-361 1.63e-11

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 66.33  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVK--FMaREIIVMRRLDHPNVLkleglitaPV------S 284
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKkrFL-REAKIAADLIHPGIV--------PVysicsdG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  285 SSLYLVFEYMDHDLLG--------LSSLPGVKFTEPQVKCYMR---QLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKI 353
Cdd:PRK13184  75 DPVYYTMPYIEGYTLKsllksvwqKESLSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVI 154

                 ....*...
gi 14532736  354 ADFGLATF 361
Cdd:PRK13184 155 LDWGAAIF 162
 
Name Accession Description Interval E-value
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
213-497 4.82e-144

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: 426.60  E-value: 4.82e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVS----SSLY 288
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKGSakykGSIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 289 LVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSV 368
Cdd:cd07840  81 MVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 369 SLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSA 447
Cdd:cd07840 161 DYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGvSDLPWFE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14532736 448 GFKTAIPYRRKVSEMFKDF-PASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07840 241 NLKPKKPYKRRLREVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
213-497 6.54e-114

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: 348.32  E-value: 6.54e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPvsSSLYLVF 291
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLD-NEEEGIPSTAlREISLLKELKHPNIVKLLDVIHTE--NKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 292 EYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLA-TFFDPAKsvSL 370
Cdd:cd07829  78 EYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLArAFGIPLR--TY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 371 TSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPssaGF 449
Cdd:cd07829 156 THEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGvTKLP---DY 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 14532736 450 KTAIPYRRK--VSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07829 233 KPTFPKWPKndLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
213-510 2.23e-109

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: 337.24  E-value: 2.23e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDL--NDMESVKFMA-REIIVMRRLDHPNVLKLEGLITApvSSSLYL 289
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGErkEAKDGINFTAlREIKLLQELKHPNIIGLLDVFGH--KSNINL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 290 VFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF-DPakSV 368
Cdd:cd07841  80 VFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFgSP--NR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 369 SLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSA 447
Cdd:cd07841 158 KMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPGvTSLPDYV 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14532736 448 GFK--TAIPYRrkvsEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLP 510
Cdd:cd07841 238 EFKpfPPTPLK----QIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYFSNDPAPTPPSQLP 298
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
213-497 2.10e-102

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 319.26  E-value: 2.10e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVrFDLNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVSS------ 285
Cdd:cd07866  10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKI-LMHNEKDGFPITAlREIKILKKLKHPNVVPLIDMAVERPDKskrkrg 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 286 SLYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFD-- 363
Cdd:cd07866  89 SVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDgp 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 364 --------PAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTE 435
Cdd:cd07866 169 ppnpkgggGGGTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPTE 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14532736 436 NYWRK-QKLPSSAGFKTAIPYRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07866 249 ETWPGwRSLPGCEGVHSFTNYPRTLEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
208-513 9.47e-101

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 315.08  E-value: 9.47e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 208 RRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVSSS 286
Cdd:cd07845   4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMD-NERDGIPISSlREITLLLNLRHPNIVELKEVVVGKHLDS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 287 LYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLA-TFFDPA 365
Cdd:cd07845  83 IFLVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLArTYGLPA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 366 KSvsLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLP 444
Cdd:cd07845 163 KP--MTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIWPGfSDLP 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14532736 445 SSAGFK-TAIPY---RRKvsemFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLPKYP 513
Cdd:cd07845 241 LVGKFTlPKQPYnnlKHK----FPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEKPLPCEPEMMPTFP 309
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
208-497 2.05e-97

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 305.69  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 208 RRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVSSS 286
Cdd:cd07843   2 RSVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKME-KEKEGFPITSlREINILLKLQHPNIVTVKEVVVGSNLDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 287 LYLVFEYMDHDLLGL-SSLPGvKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF-DP 364
Cdd:cd07843  81 IYMVMEYVEHDLKSLmETMKQ-PFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYgSP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 365 AKSvsLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKL 443
Cdd:cd07843 160 LKP--YTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKIWPGfSEL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14532736 444 PSSAGFKTAIPyrrKVSEMFKDFPASVLS-----LLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07843 238 PGAKKKTFTKY---PYNQLRKKFPALSLSdngfdLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
213-497 1.18e-94

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: 298.05  E-value: 1.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDmESVKFMA-REIIVMRRLDHPNVLKLEGLITApvSSSLYLVF 291
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETED-EGVPSTAiREISLLKELNHPNIVRLLDVVHS--ENKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 292 EYMDHDLLG-LSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFD-PAKSvs 369
Cdd:cd07835  78 EFLDLDLKKyMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGvPVRT-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 370 LTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSsag 448
Cdd:cd07835 156 YTHEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGvTSLPD--- 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14532736 449 FKTAIP--YRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07835 233 YKPTFPkwARQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
205-496 1.53e-93

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 295.94  E-value: 1.53e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 205 WAPRRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPV 283
Cdd:cd07864   1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-NEKEGFPITAiREIKILRQLNHRSVVNLKEIVTDKQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 284 SS--------SLYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIAD 355
Cdd:cd07864  80 DAldfkkdkgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLAD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 356 FGLATFFDPAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTE 435
Cdd:cd07864 160 FGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCP 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14532736 436 NYWRK-QKLPSSAGFKTAIPYRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEY 496
Cdd:cd07864 240 AVWPDvIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
213-497 2.40e-88

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 281.47  E-value: 2.40e-88
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gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKI