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Conserved domains on  [gi|48146199|emb|CAG33322.1|]
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CDK5 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
3-286 0e+00

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: 609.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   3 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEF 82
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  83 CDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEV 162
Cdd:cd07839  81 CDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAEV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 163 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMY 242
Cdd:cd07839 161 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVSKLPDYKPYPMY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 48146199 243 PATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07839 241 PATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-288 7.29e-142

cyclin-dependent kinase A; Provisional


:

Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 404.59  E-value: 7.29e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    1 MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVF 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   81 EFCDQDLKKYFDSC-NGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINR-NGELKLADFGLARAFGIPVRCY 158
Cdd:PLN00009  81 EYLDLDLKKHMDSSpDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFGIPVRTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  159 SAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYK- 237
Cdd:PLN00009 161 THEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQ-KPLFPGDSEIDELFKIFRILGTPNEETWPGVTSLPDYKs 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 48146199  238 PYPMYPAtTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSD 288
Cdd:PLN00009 240 AFPKWPP-KDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
 
Name Accession Description Interval E-value
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
3-286 0e+00

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: 609.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   3 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEF 82
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  83 CDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEV 162
Cdd:cd07839  81 CDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAEV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 163 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMY 242
Cdd:cd07839 161 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVSKLPDYKPYPMY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 48146199 243 PATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07839 241 PATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-288 7.29e-142

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 404.59  E-value: 7.29e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    1 MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVF 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   81 EFCDQDLKKYFDSC-NGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINR-NGELKLADFGLARAFGIPVRCY 158
Cdd:PLN00009  81 EYLDLDLKKHMDSSpDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFGIPVRTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  159 SAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYK- 237
Cdd:PLN00009 161 THEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQ-KPLFPGDSEIDELFKIFRILGTPNEETWPGVTSLPDYKs 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 48146199  238 PYPMYPAtTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSD 288
Cdd:PLN00009 240 AFPKWPP-KDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-286 1.78e-102

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 302.53  E-value: 1.78e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199      4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEgVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199     84 DQ-DLKKYFDScNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSaEV 162
Cdd:smart00220  80 EGgDLFDLLKK-RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT-FV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    163 VTLWYRPPDVLFGaKLYSTSIDMWSAGCIFAELAnAGRPLFPGndvDDQLKRIFRLLGTPTEEQWPSMTKLPDykpypmy 242
Cdd:smart00220 158 GTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELL-TGKPPFPG---DDQLLELFKKIGKPKPPFPPPEWDISP------- 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 48146199    243 pattslvnvvpklnaTGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:smart00220 226 ---------------EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
4-286 9.83e-97

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 288.38  E-value: 9.83e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199     4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    84 D-QDLKKYfDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEV 162
Cdd:pfam00069  81 EgGDLFDY-LSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLTTFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   163 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDykpypmy 242
Cdd:pfam00069 160 GTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLT-GKPPFSGESILDQLQLIRRILGPPLEFDEPKSDSGSE------- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 48146199   243 pattslvnvvpklnaTGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:pfam00069 232 ---------------EAKDLIKKCLNKDPSKRPTAEEILQHPWF 260
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2-292 6.21e-93

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 281.26  E-value: 6.21e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    2 QKYEKLEK-IGEGTYGTVFKAKNRETHEIVALKRVRLDD------------DDEGVPSSALREICLLKELKHKNIVRLHD 68
Cdd:PTZ00024   8 ERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrqlvGMCGIHFTTLRELKIMNEIKHENIMGLVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   69 VLHSDKKLTLVFEFCDQDLKKYFDScNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLA 148
Cdd:PTZ00024  88 VYVEGDFINLVMDIMASDLKKVVDR-KIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  149 RAFGIPV--------------RCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKR 214
Cdd:PTZ00024 167 RRYGYPPysdtlskdetmqrrEEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLT-GKPLFPGENEIDQLGR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  215 IFRLLGTPTEEQWPSMTKLPDYKPY-PMYPatTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDF---C 290
Cdd:PTZ00024 246 IFELLGTPNEDNWPQAKKLPLYTEFtPRKP--KDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDplpC 323

                 ..
gi 48146199  291 PP 292
Cdd:PTZ00024 324 DP 325
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
3-288 9.80e-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: 181.09  E-value: 9.80e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   3 KYEKLEKIGEGTYGTVFKAKNretHEIVALKRVRLD-DDDEGVPSSALREICLLKELKH-KNIVRLHDVLHSDKKLTLVF 80
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAKKlESKSKEVERFLREIQILASLNHpPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  81 EFCD-QDLKKYFDSC--NGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNG-ELKLADFGLARAFG---- 152
Cdd:COG0515  78 EYVDgGSLEDLLKKIgrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPdpgs 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 153 --IPVRCYSAEVVTLWYRPPDVLFGAKL--YSTSIDMWSAGCIFAELANaGRPLFPGNDVD---DQLKRIFRLLGTPtee 225
Cdd:COG0515 158 tsSIPALPSTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYELLT-GLPPFEGEKNSsatSQTLKIILELPTP--- 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48146199 226 qwpsmtklpdYKPYPMYPattslvNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSD 288
Cdd:COG0515 234 ----------SLASPLSP------SNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAH 280
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
4-288 8.37e-25

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 101.11  E-value: 8.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRvrlddddeGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKI--------GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   84 DQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARaFGIPVRCYSAEVV 163
Cdd:PHA03209 140 SSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQ-FPVVAPAFLGLAG 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  164 TLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELANAGRPLF---------PGNDVDDQLKRIFRLLGTPTEE--QWPSMTK 232
Cdd:PHA03209 219 TVETNAPEVLARDK-YNSKADIWSAGIVLFEMLAYPSTIFedppstpeeYVKSCHSHLLKIISTLKVHPEEfpRDPGSRL 297
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48146199  233 LPDY--------KPYPMYPATTSLvnvvpKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSD 288
Cdd:PHA03209 298 VRGFieyaslerQPYTRYPCFQRV-----NLPIDGEFLVHKMLTFDAAMRPSAEEILNYPMFAQ 356
pknD PRK13184
serine/threonine-protein kinase; Reviewed
1-191 1.75e-13

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 69.03  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    1 MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLD-DDDEGVPSSALREICLLKELKHKNIVRLHDVlHSDKKL--- 76
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlSENPLLKKRFLREAKIAADLIHPGIVPVYSI-CSDGDPvyy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   77 TLVF---EFCDQDLKKYF--DSCNGDL-DPEIVKSFLFQLLK---GLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGL 147
Cdd:PRK13184  80 TMPYiegYTLKSLLKSVWqkESLSKELaEKTSVGAFLSIFHKicaTIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48146199  148 ARA------------FGIPVRCYSAEVV------TLWYRPPDVLFGAKLySTSIDMWSAGCI 191
Cdd:PRK13184 160 AIFkkleeedlldidVDERNICYSSMTIpgkivgTPDYMAPERLLGVPA-SESTDIYALGVI 220
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
25-214 1.29e-12

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 66.79  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199     25 ETHEIVALKRVRLDD-DDEGVPSSALREICLLKELKHKNIVRLHDVLHS-DKKLTLVFEFCDQDLKKYFDSCNGDLDPEI 102
Cdd:TIGR03903    1 MTGHEVAIKLLRTDApEEEHQRARFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199    103 VKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNG---ELKLADFGLArAFGIPVRCYSAEVVTL--------WYRPPD 171
Cdd:TIGR03903   81 TGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIG-TLLPGVRDADVATLTRttevlgtpTYCAPE 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 48146199    172 VLFGAKLYSTSiDMWSAGCIFAELAnAGRPLFPGNDVDDQLKR 214
Cdd:TIGR03903  160 QLRGEPVTPNS-DLYAWGLIFLECL-TGQRVVQGASVAEILYQ 200
 
Name Accession Description Interval E-value
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
3-286 0e+00

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: 609.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   3 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEF 82
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  83 CDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEV 162
Cdd:cd07839  81 CDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAEV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 163 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMY 242
Cdd:cd07839 161 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVSKLPDYKPYPMY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 48146199 243 PATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07839 241 PATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
4-286 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: 507.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  84 DQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEVV 163
Cdd:cd07829  81 DQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTYTHEVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 164 TLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKP-YPMY 242
Cdd:cd07829 161 TLWYRAPEILLGSKHYSTAVDIWSVGCIFAELIT-GKPLFPGDSEIDQLFKIFQILGTPTEESWPGVTKLPDYKPtFPKW 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 48146199 243 PAtTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07829 240 PK-NDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
4-286 1.24e-169

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: 474.47  E-value: 1.24e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  84 DQDLKKYFDSCNGD-LDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEV 162
Cdd:cd07835  81 DLDLKKYMDSSPLTgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVPVRTYTHEV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 163 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKP-YPM 241
Cdd:cd07835 161 VTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVT-RRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGVTSLPDYKPtFPK 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 48146199 242 YPATTsLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07835 240 WARQD-LSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
4-286 1.36e-154

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: 436.53  E-value: 1.36e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAE-EGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  84 DQDLKKYFDS--CNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAE 161
Cdd:cd07836  81 DKDLKKYMDThgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSNE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 162 VVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKP-YP 240
Cdd:cd07836 161 VVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMI-TGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEYKPtFP 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 48146199 241 MYPaTTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07836 240 RYP-PQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-286 1.30e-150

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: 426.41  E-value: 1.30e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHE-EGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  84 DQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEVV 163
Cdd:cd07844  81 DTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYSNEVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 164 TLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPG-NDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPY--P 240
Cdd:cd07844 161 TLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMA-TGRPLFPGsTDVEDQLHKIFRVLGTPTEETWPGVSSNPEFKPYsfP 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 48146199 241 MYPAtTSLVNVVPKLN--ATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07844 240 FYPP-RPLINHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
4-286 1.23e-147

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: 418.83  E-value: 1.23e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   4 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFC 83
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  84 DQDLKKYFDSCN-GDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSAEV 162
Cdd:cd07860  82 HQDLKKFMDASAlTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 163 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKP-YPM 241
Cdd:cd07860 162 VTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR-RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPsFPK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 48146199 242 YPaTTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07860 241 WA-RQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-286 1.73e-143

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: 408.35  E-value: 1.73e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   3 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEF 82
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  83 CDQDLKKYFDSCNGD--LDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSA 160
Cdd:cd07861  81 LSMDLKKYLDSLPKGkyMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 161 EVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKP-Y 239
Cdd:cd07861 161 EVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATK-KPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTSLPDYKNtF 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 48146199 240 PMYpATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07861 240 PKW-KKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
3-292 4.06e-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: 4.06e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   3 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDD---DDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLV 79
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGErkeAKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  80 FEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYS 159
Cdd:cd07841  81 FEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNRKMT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 160 AEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPY 239
Cdd:cd07841 161 HQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLL-RVPFLPGDSDIDQLGKIFEALGTPTEENWPGVTSLPDYVEF 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 48146199 240 PMYPAtTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP 292
Cdd:cd07841 240 KPFPP-TPLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYFSNDPAP 291
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-286 9.96e-132

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares 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 PCTAIRE-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: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 378.58  E-value: 9.96e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   1 MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVF 80
Cdd:cd07871   4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHE-EGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  81 EFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSA 160
Cdd:cd07871  83 EYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 161 EVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPY- 239
Cdd:cd07871 163 EVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMA-TGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSNEEFRSYl 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 48146199 240 -PMYpATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYF 286
Cdd:cd07871 242 fPQY-RAQPLINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-286 1.08e-130

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares 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 PCTAIRE-1 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: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 376.27  E-value: 1.08e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199   1 MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVF 80
Cdd:cd07873   1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHE-EGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199  81 EFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNPLINRNGELKLADFGLARAFGIPVRCYSA 160
Cdd:cd07873  80 EYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146199 161 EVVTLWYRPPDVLF