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

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List of domain hits

Description PssmId Multi-dom E-value
STKc_CDK9_like[cd07840], Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, ...
143345 yes 1.35e-142

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing.


:

Cd Length: 287  Bit Score: 422.72  E-value: 1.35e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSSLYLVFE 292
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLRHPNIVRLKEIVTSKGKGSIYMVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 293 YMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSVSLTS 372
Cdd:cd07840  81 YMDHDLTGLLDSPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKRNSADYTN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 373 HVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSAGFKT 451
Cdd:cd07840 161 RVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFLGKPIFQGSTELEQLEKIFELCGSPTDENWPGvSKLPWFENLKP 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14532736 452 AIPYRRKVSEMFKDF-PASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07840 241 KKPYKRRLREFFKHLiDPSALDLLDKLLTLDPKKRISADQALQHEYF 287
S_TKc[smart00220], Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.
214567 yes 2.92e-85

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


:

Cd Length: 254  Bit Score: 272.10  E-value: 2.92e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvsSSLYLVFE 292
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    293 YMDH-DLLGLSSLPGvKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPakSVSLT 371
Cdd:smart00220  78 YCEGgDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    372 SHVVTLWYRPPELLLGaSHYGVGVDLWSTGCILGELYAGKPILPGKtevEQLHKIFKLCGSPTENYWrkqklpssagfkt 451
Cdd:smart00220 155 TFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFP------------- 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 14532736    452 aiPYRRKVSEMFKDFpasvlslLETLLSIDPDHRSSADRALESEYF 497
Cdd:smart00220 218 --PPEWDISPEAKDL-------IRKLLVKDPEKRLTAEEALQHPFF 254
 
Description PssmId Multi-dom E-value
STKc_CDK9_like[cd07840], Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, ...
143345 yes 1.35e-142

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing.


Cd Length: 287  Bit Score: 422.72  E-value: 1.35e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSSLYLVFE 292
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLRHPNIVRLKEIVTSKGKGSIYMVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 293 YMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSVSLTS 372
Cdd:cd07840  81 YMDHDLTGLLDSPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKRNSADYTN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 373 HVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSAGFKT 451
Cdd:cd07840 161 RVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFLGKPIFQGSTELEQLEKIFELCGSPTDENWPGvSKLPWFENLKP 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14532736 452 AIPYRRKVSEMFKDF-PASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07840 241 KKPYKRRLREFFKHLiDPSALDLLDKLLTLDPKKRISADQALQHEYF 287
PHA02882[PHA02882], putative serine/threonine kinase; Provisional
165211 no 2.55e-05

putative serine/threonine kinase; Provisional


Cd Length: 294  Bit Score: 45.33  E-value: 2.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14532736  309 FTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF 362
Cdd:PHA02882 123 KNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIIDYGIASHF 176
S_TKc[smart00220], Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.
214567 yes 2.92e-85

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


Cd Length: 254  Bit Score: 272.10  E-value: 2.92e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvsSSLYLVFE 292
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    293 YMDH-DLLGLSSLPGvKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPakSVSLT 371
Cdd:smart00220  78 YCEGgDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    372 SHVVTLWYRPPELLLGaSHYGVGVDLWSTGCILGELYAGKPILPGKtevEQLHKIFKLCGSPTENYWrkqklpssagfkt 451
Cdd:smart00220 155 TFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFP------------- 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 14532736    452 aiPYRRKVSEMFKDFpasvlslLETLLSIDPDHRSSADRALESEYF 497
Cdd:smart00220 218 --PPEWDISPEAKDL-------IRKLLVKDPEKRLTAEEALQHPFF 254
PTZ00024[PTZ00024], cyclin-dependent protein kinase; Provisional
240233 yes 2.69e-83

cyclin-dependent protein kinase; Provisional


Cd Length: 335  Bit Score: 270.09  E-value: 2.69e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  219 IGQGTYSSVYRARDLLHNKIVALKKVR-----------FDLNDMESVKFMA-REIIVMRRLDHPNVLkleGLITAPVSSS 286
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKiieisndvtkdRQLVGMCGIHFTTlRELKIMNEIKHENIM---GLVDVYVEGD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  287 -LYLVFEYMDHDLLGLSSlPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF--- 362
Cdd:PTZ00024  94 fINLVMDIMASDLKKVVD-RKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYgyp 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  363 ----------DPAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGS 432
Cdd:PTZ00024 173 pysdtlskdeTMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELLGT 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14532736  433 PTENYW-RKQKLPSSAGFKTAIPyrRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLP 510
Cdd:PTZ00024 253 PNEDNWpQAKKLPLYTEFTPRKP--KDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDPLPCDPSQLP 329
Pkinase[pfam00069], Protein kinase domain;
249558 yes 2.03e-79

Protein kinase domain;


Cd Length: 260  Bit Score: 256.79  E-value: 2.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736   213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvsSSLYLVFE 292
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDK--DHLYLVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736   293 YMDH-DLLGLSSlPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDpAKSVSLT 371
Cdd:pfam00069  79 YCEGgDLFDYLS-RGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLT-KSSSSLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736   372 SHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWrkqklpssagfkt 451
Cdd:pfam00069 157 TFVGTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDE------------- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 14532736   452 aiPYRRKVSEMFKDFpasvlslLETLLSIDPDHRSSADRALESEYF 497
Cdd:pfam00069 224 --PKSDSGSEEAKDL-------IKKCLNKDPSKRPTAEEILQHPWF 260
PLN00009[PLN00009], cyclin-dependent kinase A; Provisional
177649 yes 4.86e-74

cyclin-dependent kinase A; Provisional


Cd Length: 294  Bit Score: 243.57  E-value: 4.86e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDmESVKFMA-REIIVMRRLDHPNVLKLEGLITApvSSSLYLVF 291
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQED-EGVPSTAiREISLLKEMQHGNIVRLQDVVHS--EKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  292 EYMDHDLLG-LSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLID-SKGVLKIADFGLATFFD-PAKSv 368
Cdd:PLN00009  81 EYLDLDLKKhMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARAFGiPVRT- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  369 sLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSsa 447
Cdd:PLN00009 160 -FTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGvTSLPD-- 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14532736  448 gFKTAIPYRRKvsemfKDFPASV-------LSLLETLLSIDPDHRSSADRALESEYFK 498
Cdd:PLN00009 237 -YKSAFPKWPP-----KDLATVVptlepagVDLLSKMLRLDPSKRITARAALEHEYFK 288
SPS1[COG0515], Serine/threonine protein kinase [General function prediction only / Signal transduction ...
223589 yes 2.14e-45

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


Cd Length: 384  Bit Score: 166.46  E-value: 2.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDllhNKIVALKKVRFDL-NDMESVKFMAREIIVMRRLDHP-NVLKLEGLITapVSSSLYLV 290
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLeSKSKEVERFLREIQILASLNHPpNIVKLYDFFQ--DEGSLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 291 FEYMDHDLLGL---SSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKG-VLKIADFGLATFFDPAK 366
Cdd:COG0515  77 MEYVDGGSLEDllkKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDPG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 367 SVS-----LTSHVVTLWYRPPELLLGAS--HYGVGVDLWSTGCILGELYAGKPILPGKTE---VEQLHKIFKLCGSPTEN 436
Cdd:COG0515 157 STSsipalPSTSVGTPGYMAPEVLLGLSlaYASSSSDIWSLGITLYELLTGLPPFEGEKNssaTSQTLKIILELPTPSLA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 437 YWRKQKLPSsagfktaipyrrkvsemfkDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLPKYPPSK 516
Cdd:COG0515 237 SPLSPSNPE-------------------LISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDS 297
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14532736 517 EIDAKmrDEAKRQQPMRAEKQERQDSMTRISHERKFVPPVKANNSLSMTMEKQYKDLRSRNDSFKS 582
Cdd:COG0515 298 APLRL--SLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRS 361
PHA03210[PHA03210], serine/threonine kinase US3; Provisional
165476 yes 1.64e-17

serine/threonine kinase US3; Provisional


Cd Length: 501  Bit Score: 84.75  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  242 KKVRfdlNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSSL------YLVFEYMDHDLLGLSSLPGVKftepQVK 315
Cdd:PHA03210 198 KRVK---AGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMitqkydFDLYSFMYDEAFDWKDRPLLK----QTR 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736  316 CYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSVSLTSHVVTLWYRPPELLLGASHYGVgV 395
Cdd:PHA03210 271 AIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDYGWVGTVATNSPEILAGDGYCEI-T 349
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 14532736  396 DLWSTGCILGELYAgKPILP----GKTEVEQLHKIFK 428
Cdd:PHA03210 350 DIWSCGLILLDMLS-HDFCPigdgGGKPGKQLLKIID 385
TOMM_kin_cyc[TIGR03903], TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in ...
234389 yes 1.59e-13

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


Cd Length: 1266  Bit Score: 72.95  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    239 VALKKVRFD-LNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPvSSSLYLVFEYMD-HDLLGLSSLPGVKFTEPQVKc 316
Cdd:TIGR03903    6 VAIKLLRTDaPEEEHQRARFRRETALCARLYHPNIVALLDSGEAP-PGLLFAVFEYVPgRTLREVLAADGALPAGETGR- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736    317 YMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGV---LKIADFGLATFF------DPAKSVSLTSHVVTLWYRPPELLLG 387
Cdd:TIGR03903   84 LMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLpgvrdaDVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 14532736    388 AShYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHK 425
Cdd:TIGR03903  164 EP-VTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ 200
pknD[PRK13184], serine/threonine-protein kinase; Reviewed
183880 yes 1.63e-11

serine/threonine-protein kinase; Reviewed


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

                 ....*...
gi 14532736  354 ADFGLATF 361
Cdd:PRK13184 155 LDWGAAIF 162
 
Description PssmId Multi-dom E-value
STKc_CDK9_like[cd07840], Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, ...
143345 yes 1.35e-142

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing.


Cd Length: 287  Bit Score: 422.72  E-value: 1.35e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSSLYLVFE 292
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLRHPNIVRLKEIVTSKGKGSIYMVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 293 YMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSVSLTS 372
Cdd:cd07840  81 YMDHDLTGLLDSPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKRNSADYTN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 373 HVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSAGFKT 451
Cdd:cd07840 161 RVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFLGKPIFQGSTELEQLEKIFELCGSPTDENWPGvSKLPWFENLKP 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14532736 452 AIPYRRKVSEMFKDF-PASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07840 241 KKPYKRRLREFFKHLiDPSALDLLDKLLTLDPKKRISADQALQHEYF 287
STKc_CDK_like[cd07829], Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase (CDK)-like subfamily, ...
173733 yes 2.15e-115

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase (CDK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Cd Length: 282  Bit Score: 352.17  E-value: 2.15e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPvsSSLYLVF 291
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKARDKKTGEIVALKKIRLD-NEEEGIPSTAlREISLLKELKHPNIVKLLDVIHTE--RKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 292 EYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSvSLT 371
Cdd:cd07829  78 EYCDMDLKKYLDKRPGPLSPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNILINRDGVLKLADFGLARAFGIPLR-TYT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 372 SHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPssaGFK 450
Cdd:cd07829 157 HEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAEMITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGvTKLP---DYK 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 14532736 451 TAIPYRRK--VSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07829 234 PTFPKFPPkdLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDK7[cd07841], Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 7 (CDK7) subfamily, ...
143346 yes 2.61e-109

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 7 (CDK7) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Cd Length: 298  Bit Score: 336.86  E-value: 2.61e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDL--NDMESVKFMA-REIIVMRRLDHPNVLKLEGLITApvSSSLYL 289
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGErkEAKDGINFTAlREIKLLQELKHPNIIGLLDVFGH--KSNINL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 290 VFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF-DPakSV 368
Cdd:cd07841  80 VFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFgSP--NR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 369 SLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSA 447
Cdd:cd07841 158 KMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPGvTSLPDYV 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14532736 448 GFK--TAIPYRrkvsEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLP 510
Cdd:cd07841 238 EFKpfPPTPLK----QIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYFSNDPAPTPPSQLP 298
STKc_BUR1[cd07866], Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Bypass UAS Requirement 1 and similar proteins; Serine/Threonine Kinases (STKs), Bypass UAS Requirement 1 (BUR1) subfamily, catalytic (c) ...
143371 yes 1.95e-102

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


Cd Length: 311  Bit Score: 319.65  E-value: 1.95e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVrFDLNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVSS------ 285
Cdd:cd07866  10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKI-LMHNEKDGFPITAlREIKILKKLKHPNVVPLIDMAVERPDKskrkrg 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 286 SLYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFD-- 363
Cdd:cd07866  89 SVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDgp 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 364 --------PAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTE 435
Cdd:cd07866 169 ppnpkgggGGGTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPTE 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14532736 436 NYWRK-QKLPSSAGFKTAIPYRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07866 249 ETWPGwRSLPGCEGVHSFTNYPRTLEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_CDK10[cd07845], Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; Serine/Threonine Kinases (STKs), Cyclin-dependent protein Kinase 10 (CDK10) subfamily, ...
173742 yes 9.47e-101

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


Cd Length: 309  Bit Score: 315.07  E-value: 9.47e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 208 RRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVSSS 286
Cdd:cd07845   4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMD-NERDGIPISSlREITLLLNLRHPNIVELKEVVVGKHLDS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 287 LYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLA-TFFDPA 365
Cdd:cd07845  83 IFLVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLArTYGLPA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 366 KSvsLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLP 444
Cdd:cd07845 163 KP--MTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIWPGfSDLP 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14532736 445 SSAGFK-TAIPY---RRKvsemFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLPKYP 513
Cdd:cd07845 241 LVGKFTlPKQPYnnlKHK----FPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEKPLPCEPEMMPTFP 309
STKc_CDC2L1[cd07843], Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; Serine/Threonine Kinases (STKs), Cell Division Cycle 2-like 1 (CDC2L1) subfamily, ...
173741 yes 2.05e-97

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; Serine/Threonine Kinases (STKs), Cell Division Cycle 2-like 1 (CDC2L1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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).


Cd Length: 293  Bit Score: 305.69  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 208 RRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVSSS 286
Cdd:cd07843   2 RSVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKME-KEKEGFPITSlREINILLKLQHPNIVTVKEVVVGSNLDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 287 LYLVFEYMDHDLLGL-SSLPGvKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFF-DP 364
Cdd:cd07843  81 IYMVMEYVEHDLKSLmETMKQ-PFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYgSP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 365 AKSvsLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKL 443
Cdd:cd07843 160 LKP--YTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKIWPGfSEL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14532736 444 PSSAGFKTAIPyrrKVSEMFKDFPASVLS-----LLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07843 238 PGAKKKTFTKY---PYNQLRKKFPALSLSdngfdLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_CDK12[cd07864], Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 12 (CDK12) subfamily, ...
173753 yes 3.88e-95

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


Cd Length: 302  Bit Score: 300.15  E-value: 3.88e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 205 WAPRRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPV 283
Cdd:cd07864   1 WGKRCVDKFDIIGQIGEGTYGQVYKARDKDTGELVALKKVRLD-NEKEGFPITAiREIKILRQLNHRNIVNLKEIVTDKQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 284 SS--------SLYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIAD 355
Cdd:cd07864  80 DAldfkkdkgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLAD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 356 FGLATFFDPAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTE 435
Cdd:cd07864 160 FGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCP 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14532736 436 NYWRK-QKLPSSAGFKTAIPYRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEY 496
Cdd:cd07864 240 AVWPDvIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEEALNSPW 301
STKc_CDK1_like[cd07835], Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 1 (CDK1)-like subfamily, ...
173738 yes 1.87e-94

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 1 (CDK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. This subfamily is composed of CDK1 from higher eukaryotes, plants, and yeasts, as well as 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.


Cd Length: 283  Bit Score: 297.69  E-value: 1.87e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDmESVKFMA-REIIVMRRLDHPNVLKLEGLITApvSSSLYLVF 291
Cdd:cd07835   1 YQKVEKIGEGTYGVVYKARDKLTGEIVALKKIRLETED-EGVPSTAiREISLLKELNHPNIVRLLDVVHS--ENKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 292 EYMDHDLLG-LSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFD-PAKSvs 369
Cdd:cd07835  78 EFLDLDLKKyMDSSPLTGLDPPLIKSYLYQLLQGIAYCHSHRVLHRDLKPQNLLIDREGALKLADFGLARAFGvPVRT-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 370 LTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSsag 448
Cdd:cd07835 156 YTHEVVTLWYRAPEILLGSRQYSTPVDIWSIGCIFAEMVNRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGvTSLPD--- 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14532736 449 FKTAIP--YRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07835 233 YKPTFPkwARQDLSKVVPNLDEDGLDLLSKMLVYDPAKRISAKAALQHPYF 283
STKc_CMGC[cd05118], Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), CMGC family, catalytic (c) domain. STKs catalyze the ...
143333 yes 3.25e-93

Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), CMGC family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and similar proteins. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation.


Cd Length: 283  Bit Score: 294.24  E-value: 3.25e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDmESVKFMA-REIIVMRRLDHPNVLKLEGLITAPvsSSLYLVF 291
Cdd:cd05118   1 YQKLGKIGEGTYGVVYKARDKLTGEIVAIKKIKLRFES-EGIPKTAlREIKLLKELNHPNIIKLLDVFRHK--GDLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 292 EYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPaKSVSLT 371
Cdd:cd05118  78 EFMDTDLYKLIKDRQRGLPESLIKSYLYQLLQGLAFCHSHGILHRDLKPENLLINTEGVLKLADFGLARSFGS-PVRPYT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 372 SHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRK-QKLPSSAGFK 450
Cdd:cd05118 157 HYVVTRWYRAPELLLGDKGYSTPVDIWSVGCIFAELLSRRPLFPGKSEIDQLFKIFRTLGTPDPEVWPKfTSLARNYKFS 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14532736 451 TAIPYRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd05118 237 FPKKAGMPLPKLFPNASPQALDLLSQMLHYDPHKRITAEQALAHPYF 283
STKc_CDK9[cd07865], Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9) subfamily, ...
173754 yes 9.61e-89

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. CDK9 together with a cyclin partner (cyclin T1, T2a, T2b, or K) is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors.


Cd Length: 310  Bit Score: 283.50  E-value: 9.61e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 211 NTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDlNDMESVKFMA-REIIVMRRLDHPNVLKLEGLITAPVS----- 284
Cdd:cd07865  12 SKYEKLAKIGQGTFGEVFKARHKKTKQIVALKKVLME-NEKEGFPITAlREIKILQLLKHENVVNLIEICRTKATpynry 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 285 -SSLYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFD 363
Cdd:cd07865  91 kGSFYLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGILKLADFGLARAFS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 364 PAKSVS---LTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPT------ 434
Cdd:cd07865 171 LSKNSKpnrYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITpevwpg 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14532736 435 -ENY--WRKQKLPSSagfktaipYRRKVSEMFKDFPASV--LSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07865 251 vDKLelFKKMELPQG--------QKRKVKERLKPYVKDPhaLDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_CCRK[cd07832], Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine Kinases (STKs), Cell Cycle-Related Kinase (CCRK) p42 subfamily, ...
173736 yes 4.37e-88

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine Kinases (STKs), Cell Cycle-Related Kinase (CCRK) p42 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed, this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure.


Cd Length: 286  Bit Score: 280.71  E-value: 4.37e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 212 TFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLegLITAPVSSSLYLVF 291
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRRLEGGIPNQALREIKALQACQHPYVVKL--LDVFPHGSGFVLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 292 EYMDHDL---LGLSSLPgvkFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSV 368
Cdd:cd07832  79 EYMPSDLsevLRDEERP---LPEAQVKSYMRMLLKGVAYMHANGIMHRDLKPANLLISADGVLKIADFGLARLFSEEEPR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 369 SLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRKQKLPSSAG 448
Cdd:cd07832 156 LYSHQVATRWYRAPELLYGARKYDPGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVFRTLGTPNEETWPGLTSLPDYN 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14532736 449 fKTAIPYRRKV--SEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07832 236 -KITFPESKPIplEEIFPDASPEALDLLKGLLVYDPSKRLSAAEALRHPYF 285
STKc_CDK4_6_like[cd07838], Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-dependent protein kinase 4 (CDK4) and CDK6-like ...
173739 yes 4.27e-87

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


Cd Length: 287  Bit Score: 278.37  E-value: 4.27e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLD---HPNVLKLEGLITAPVSS---S 286
Cdd:cd07838   1 YEELAEIGEGAYGTVYKARDLNTGRFVALKKVRVPLSEEGIPLSTLREIALLKQLEsfeHPNIVRLLDVCHGPRTDrelK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 287 LYLVFEYMDHDLLG-LSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDpa 365
Cdd:cd07838  81 LTLVFEHVDQDLATyLSKCPKPGLPPETIKDLMRQLLRGVDFLHSHRIVHRDLKPQNILVTSDGQVKIADFGLARIYS-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 366 KSVSLTSHVVTLWYRPPELLLGAShYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRKQKL-- 443
Cdd:cd07838 159 FEMALTSVVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFRRRPLFRGTSEADQLDKIFDVIGLPSEEEWPRNVSlp 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 14532736 444 PSSAGFKTAIPYRRKVSEMFKDfpasVLSLLETLLSIDPDHRSSADRALESEYF 497
Cdd:cd07838 238 RSSFPSYTPRSFKSFVPEICEE----GLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_MAPK[cd07834], Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), Mitogen-Activated Protein Kinase (MAPK) subfamily, ...
173737 yes 2.43e-80

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), Mitogen-Activated Protein Kinase (MAPK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three main typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7.


Cd Length: 330  Bit Score: 261.70  E-value: 2.43e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVR--FDlnDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSS---L 287
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAVDKRTGRKVAIKKISnvFD--DLIDAKRILREIKLLRHLRHENIIGLLDILRPPSPEDfndV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 288 YLVFEYMDHDLLG-LSSlpGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDP-- 364
Cdd:cd07834  80 YIVTELMETDLHKvIKS--PQPLTDDHIQYFLYQILRGLKYLHSANVIHRDLKPSNILVNSNCDLKICDFGLARGVDPde 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 365 AKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRKQKLP 444
Cdd:cd07834 158 DEKGFLTEYVVTRWYRAPELLLSSSRYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLKFITSE 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14532736 445 SSAGFKTAIPYRRKV--SEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFK 498
Cdd:cd07834 238 KARNYLKSLPKKPKKplSKLFPGASPEAIDLLEKMLVFDPKKRITADEALAHPYLA 293
STKc_Pho85[cd07836], Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; Serine/Threonine Kinases (STKs), Pho85 subfamily, catalytic (c) domain. STKs catalyze the ...
143341 yes 7.05e-79

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; Serine/Threonine Kinases (STKs), Pho85 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Pho85 is a multifunctional Cyclin-Dependent protein Kinase (CDK) in yeast. 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. Pho85 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.


Cd Length: 284  Bit Score: 256.25  E-value: 7.05e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14532736 213 FEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNdmESVKFMA-REIIVMRRLDHPNVLKLEGLITapVSSSLYLVF 291
Cdd:cd07836