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Conserved domains on  [gi|334302921|sp|P06493|]
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RecName: Full=Cyclin-dependent kinase 1; Short=CDK1; AltName: Full=Cell division control protein 2 homolog; AltName: Full=Cell division protein kinase 1; AltName: Full=p34 protein kinase [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-287 0e+00

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 600.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   3 DYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEF 82
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  83 LSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTH 162
Cdd:cd07861   81 LSMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 163 EVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFP 242
Cdd:cd07861  161 EVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTSLPDYKNTFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334302921 243 KWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07861  241 KWKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-293 1.72e-164

cyclin-dependent kinase A; Provisional


:

Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 461.98  E-value: 1.72e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   1 MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIF 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  81 EFLSMDLKKYLDSIPPGQyMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDK-GTIKLADFGLARAFGIPIRV 159
Cdd:PLN00009  81 EYLDLDLKKHMDSSPDFA-KNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGLARAFGIPVRT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 160 YTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKN 239
Cdd:PLN00009 160 FTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVTSLPDYKS 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334302921 240 TFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQ 293
Cdd:PLN00009 240 AFPKWPPKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDA 293
 
Name Accession Description Interval E-value
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-287 0e+00

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 600.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   3 DYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEF 82
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  83 LSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTH 162
Cdd:cd07861   81 LSMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 163 EVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFP 242
Cdd:cd07861  161 EVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTSLPDYKNTFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334302921 243 KWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07861  241 KWKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-293 1.72e-164

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 461.98  E-value: 1.72e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   1 MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIF 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  81 EFLSMDLKKYLDSIPPGQyMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDK-GTIKLADFGLARAFGIPIRV 159
Cdd:PLN00009  81 EYLDLDLKKHMDSSPDFA-KNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGLARAFGIPVRT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 160 YTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKN 239
Cdd:PLN00009 160 FTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVTSLPDYKS 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334302921 240 TFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQ 293
Cdd:PLN00009 240 AFPKWPPKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDA 293
Pkinase pfam00069
Protein kinase domain;
4-287 3.36e-104

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 307.64  E-value: 3.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921    4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   84 SM-DLKKYLDSippGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTH 162
Cdd:pfam00069  81 EGgDLFDYLSR---GGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  163 EVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWpeveslqdykntfP 242
Cdd:pfam00069 158 FVGTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDE-------------P 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 334302921  243 KWKPGSlashvknldENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:pfam00069 225 KSDSGS---------EEAKDLIKKCLNKDPSKRPTAEEILQHPWF 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-287 3.83e-102

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 302.14  E-value: 3.83e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921     4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLEsEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921    84 SM-DLKKYLDSippGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGiPIRVYTH 162
Cdd:smart00220  80 EGgDLFDLLKK---RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD-PGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   163 EVVTLWYRSPEVLLGSaRYSTPVDIWSIGTIFAELATKKPLFHGDseiDQLFRIFRALGTPNNEVWPeveslqdykntfp 242
Cdd:smart00220 156 FVGTPEYMAPEVLLGK-GYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFPP------------- 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 334302921   243 kwkpgslasHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:smart00220 219 ---------PEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2-288 4.27e-92

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 279.34  E-value: 4.27e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   2 EDYTKIEK-IGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPS------------TAIREISLLKELRHPNIVSLQD 68
Cdd:PTZ00024   8 ERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKdrqlvgmcgihfTTLRELKIMNEIKHENIMGLVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  69 VLMQDSRLYLIFEFLSMDLKKYLDSippGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFG 148
Cdd:PTZ00024  88 VYVEGDFINLVMDIMASDLKKVVDR---KIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 149 LARAFGIPI--------------RVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLF 214
Cdd:PTZ00024 165 LARRYGYPPysdtlskdetmqrrEEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLG 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334302921 215 RIFRALGTPNNEVWPEVESLQDYkNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFN 288
Cdd:PTZ00024 245 RIFELLGTPNEDNWPQAKKLPLY-TEFTPRKPKDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
3-291 5.80e-54

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: 181.86  E-value: 5.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   3 DYTKIEKIGEGTYGVVYKGRHKttgQVVAMKKIRLESEEEG-VPSTAIREISLLKELRHP-NIVSLQDVLMQDSRLYLIF 80
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSkEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  81 EFLS-MDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGT-IKLADFGLARAFG---- 154
Cdd:COG0515   78 EYVDgGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPdpgs 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 155 --IPIRVYTHEVVTLWYRSPEVLLGS--ARYSTPVDIWSIGTIFAELATKKPLFHGDSE---IDQLFRIFRALGTPNnev 227
Cdd:COG0515  158 tsSIPALPSTSVGTPGYMAPEVLLGLslAYASSSSDIWSLGITLYELLTGLPPFEGEKNssaTSQTLKIILELPTPS--- 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334302921 228 wpeveslqdYKNTFPKWKPGSLASHVKnldenglDLLSKMLIYDPAKRISGKMALNHPYFNDLD 291
Cdd:COG0515  235 ---------LASPLSPSNPELISKAAS-------DLLKKLLAKDPKNRLSSSSDLSHDLLAHLK 282
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
4-290 1.22e-25

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 103.80  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKirleseeeGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKI--------GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIPPGQYMDSSLVksYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARaFGIPIRVYTHE 163
Cdd:PHA03209 140 SSDLYTYLTKRSRPLPIDQALI--IEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQ-FPVVAPAFLGL 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVlLGSARYSTPVDIWSIGTI-FAELATKKPLFHGD---------SEIDQLFRIFRALGTpNNEVWPE--- 230
Cdd:PHA03209 217 AGTVETNAPEV-LARDKYNSKADIWSAGIVlFEMLAYPSTIFEDPpstpeeyvkSCHSHLLKIISTLKV-HPEEFPRdpg 294
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334302921 231 ---VESLQDYKNTfpKWKPGSLASHVK--NLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDL 290
Cdd:PHA03209 295 srlVRGFIEYASL--ERQPYTRYPCFQrvNLPIDGEFLVHKMLTFDAAMRPSAEEILNYPMFAQL 357
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
26-215 7.50e-20

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: 89.13  E-value: 7.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921    26 TGQVVAMKKIR-LESEEEGVPSTAIREISLLKELRHPNIVSLQDV-LMQDSRLYLIFEFLS-MDLKKYLDS---IPPGQy 99
Cdd:TIGR03903    2 TGHEVAIKLLRtDAPEEEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPgRTLREVLAAdgaLPAGE- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   100 mdsslVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLI---DDKGTIKLADFGL------ARAFGIPIRVYTHEVV-TLWY 169
Cdd:TIGR03903   81 -----TGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIgtllpgVRDADVATLTRTTEVLgTPTY 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 334302921   170 RSPEVLLGSArySTP-VDIWSIGTIFAELATKKPLFHGDSEIDQLFR 215
Cdd:TIGR03903  156 CAPEQLRGEP--VTPnSDLYAWGLIFLECLTGQRVVQGASVAEILYQ 200
pknD PRK13184
serine/threonine-protein kinase; Reviewed
1-199 8.79e-17

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.43  E-value: 8.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   1 MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLE-SEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLI 79
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  80 FEFLS-MDLKKYLDSIPPGQYMDSSL-----VKSYL---YQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLA 150
Cdd:PRK13184  81 MPYIEgYTLKSLLKSVWQKESLSKELaektsVGAFLsifHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334302921 151 RA----------FGIPIRVYTHE--------VVTLWYRSPEVLLGS-ARYSTpvDIWSIGTIFAELAT 199
Cdd:PRK13184 161 IFkkleeedlldIDVDERNICYSsmtipgkiVGTPDYMAPERLLGVpASEST--DIYALGVILYQMLT 226
 
Name Accession Description Interval E-value
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-287 0e+00

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 600.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   3 DYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEF 82
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  83 LSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTH 162
Cdd:cd07861   81 LSMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 163 EVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFP 242
Cdd:cd07861  161 EVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTSLPDYKNTFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334302921 243 KWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07861  241 KWKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
4-287 0e+00

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: 582.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIPPgQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHE 163
Cdd:cd07835   81 DLDLKKYMDSSPL-TGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVPVRTYTHE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPK 243
Cdd:cd07835  160 VVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGVTSLPDYKPTFPK 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334302921 244 WKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07835  240 WARQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
4-287 0e+00

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: 523.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIPPGqyMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHE 163
Cdd:cd07829   81 DQDLKKYLDKRPGP--LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTYTHE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPK 243
Cdd:cd07829  159 VVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGVTKLPDYKPTFPK 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334302921 244 WKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07829  239 WPKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
4-287 2.61e-174

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 486.63  E-value: 2.61e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIPPGQyMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHE 163
Cdd:cd07860   82 HQDLKKFMDASALTG-IPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPK 243
Cdd:cd07860  161 VVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334302921 244 WKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07860  241 WARQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2-288 1.09e-139

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 399.21  E-value: 1.09e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   2 EDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRH-PNIVSLQDVLMQD----SRL 76
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLDVEHVEengkPLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  77 YLIFEFLSMDLKKYLDSI--PPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLID-DKGTIKLADFGLARAF 153
Cdd:cd07837   81 YLVFEYLDTDLKKFIDSYgrGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLGLGRAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 154 GIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVES 233
Cdd:cd07837  161 TIPIKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEVWPGVSK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334302921 234 LQDYkNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFN 288
Cdd:cd07837  241 LRDW-HEYPQWKPQDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYFD 294
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
4-287 1.57e-139

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 398.34  E-value: 1.57e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIppGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHE 163
Cdd:cd07839   82 DQDLKKYFDSC--NGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATK-KPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKnTFP 242
Cdd:cd07839  160 VVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVSKLPDYK-PYP 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 334302921 243 KWKPGSLASH-VKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07839  239 MYPATTSLVNvVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
4-287 2.06e-138

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 395.70  E-value: 2.06e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEeGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEE-GTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHE 163
Cdd:cd07836   81 DKDLKKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSNE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPK 243
Cdd:cd07836  161 VVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEYKPTFPR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334302921 244 WKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07836  241 YPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-287 1.60e-134

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 385.58  E-value: 1.60e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLEsEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFL 83
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLE-HEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  84 SMDLKKYLDSIPPGQYMDSslVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHE 163
Cdd:cd07844   81 DTDLKQYMDDCGGGLSMHN--VRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYSNE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 164 VVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEI-DQLFRIFRALGTPNNEVWPEVESLQDYKN-TF 241
Cdd:cd07844  159 VVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTPTEETWPGVSSNPEFKPySF 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 334302921 242 PKWKPGSLASHVKNLD--ENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07844  239 PFYPPRPLINHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
4-287 5.71e-133

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: 382.31  E-value: 5.71e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   4 YTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEE---GVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIF 80
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEakdGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  81 EFLSMDLKKYLDsippgqymDSSLV------KSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFG 154
Cdd:cd07841   82 EFMETDLEKVIK--------DKSIVltpadiKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921 155 IPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESL 234
Cdd:cd07841  154 SPNRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPGVTSL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334302921 235 QDYkNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYF 287
Cdd:cd07841  234 PDY-VEFKPFPPTPLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYF 285
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
2-287 4.98e-132

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: 379.65  E-value: 4.98e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921   2 EDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDS--RLYLI 79
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITSLREINILLKLQHPNIVTVKEVVVGSNldKIYMV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334302921  80 FEFLSMDLKKYLDSIPPGqyMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTI