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Conserved domains on  [gi|15608881|ref|NP_216259|]
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serine/threonine-protein kinase PknE [Mycobacterium tuberculosis H37Rv]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
15-267 1.03e-103

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


:

Pssm-ID: 270916  Cd Length: 260  Bit Score: 316.84  E-value: 1.03e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  15 PYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMR 94
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  95 LINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQLGN 174
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 175 TVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGD-QLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGM 253
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDsPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250
                ....*....|....
gi 15608881 254 AKNPEDRYVTCGDL 267
Cdd:cd14014 241 AKDPEERPQSAAEL 254
DsbG COG1651
Protein-disulfide isomerase [Posttranslational modification, protein turnover, chaperones];
383-566 2.94e-25

Protein-disulfide isomerase [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 224565  Cd Length: 244  Bit Score: 105.33  E-value: 2.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 383 LRVLNDG--VFVGSSVAPTTIDIFNEPICPPCgsfIRSYASDIDTAVADKQLAVRYHLLNFLDDQSHsknYSTRAVAASY 460
Cdd:COG1651  68 LYLTPDGkdVVLGNPYAPVTVVEFFDYTCPYC---KEAFPELKKKYIDDGKVRLVLREFPFLDPACP---YCRRAAQAAR 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 461 CVAGQNDPKlYASFYSALFGSDFQPQENAASDRTDAELAHLAQTVGAEPTAISCIKSGADLGTAQTKATNasetlagFNA 540
Cdd:COG1651 142 CAADQGIVR-YWAFHDALFGSQAEAWAASILCAKDLAKADLAALDEGKKAKLNQKACDALIAKNYKLAQQ-------LGV 213
                       170       180
                ....*....|....*....|....*..
gi 15608881 541 SGTP-FVWDGSMVVNYQDPSWLARLIG 566
Cdd:COG1651 214 NGTPtFIVNGKLVPGLPDLDELKAIID 240
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
15-267 1.03e-103

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


Pssm-ID: 270916  Cd Length: 260  Bit Score: 316.84  E-value: 1.03e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  15 PYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMR 94
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  95 LINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQLGN 174
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 175 TVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGD-QLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGM 253
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDsPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250
                ....*....|....
gi 15608881 254 AKNPEDRYVTCGDL 267
Cdd:cd14014 241 AKDPEERPQSAAEL 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
16-261 6.72e-53

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 183.11  E-value: 6.72e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881     16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSetLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881     96 INGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQlgNT 175
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT--TF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    176 VGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGD-QLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGMA 254
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236

                   ....*..
gi 15608881    255 KNPEDRY 261
Cdd:smart00220 237 KDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
16-261 1.56e-46

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 169.54  E-value: 1.56e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTvreRIVALKLMSETLSSDPVFRTRMQREARTAGRLQ-EPHVVPIHDFGEIDGQLYVDMR 94
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNhPPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  95 LINGVDLAAMLR---RQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDF-AYLVDFGIASATTDEKLT 170
Cdd:COG0515  79 YVDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 171 QLGNT-----VGTLYYMAPERF---SESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQAI----------P 232
Cdd:COG0515 159 SSIPAlpstsVGTPGYMAPEVLlglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIIlelptpslasP 238
                       250       260
                ....*....|....*....|....*....
gi 15608881 233 RPSTVRPGIPVAFDAVIARGMAKNPEDRY 261
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRL 267
Pkinase pfam00069
Protein kinase domain;
16-260 1.35e-37

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 140.43  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMsETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKI-KKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    96 INGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQlgNT 175
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSSLT--SF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   176 VGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQG-DQLSVMGAHINQ--AIPRPSTvrpgIPVAFDAVIARG 252
Cdd:pfam00069 158 VGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGiNGNEIYEKIIDQdfDSPRPSS----ISEEAKDLLKKL 233

                  ....*...
gi 15608881   253 MAKNPEDR 260
Cdd:pfam00069 234 LKKDPSKR 241
pknD PRK13184
serine/threonine-protein kinase; Reviewed
14-267 3.37e-37

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 147.61  E-value: 3.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   14 GPYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFgEIDGQL-YVD 92
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSI-CSDGDPvYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   93 MRLINGVDLAAMLR--RQ-----GPLAPPRAVA----IVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIA 161
Cdd:PRK13184  81 MPYIEGYTLKSLLKsvWQkeslsKELAEKTSVGaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  162 SATTDEK-----------------LTQLGNTVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMg 224
Cdd:PRK13184 161 IFKKLEEedlldidvdernicyssMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI- 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15608881  225 aHINQAIPRPSTVRP--GIPVAFDAVIARGMAKNPEDRYVTCGDL 267
Cdd:PRK13184 240 -SYRDVILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQEL 283
DsbG COG1651
Protein-disulfide isomerase [Posttranslational modification, protein turnover, chaperones];
383-566 2.94e-25

Protein-disulfide isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224565  Cd Length: 244  Bit Score: 105.33  E-value: 2.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 383 LRVLNDG--VFVGSSVAPTTIDIFNEPICPPCgsfIRSYASDIDTAVADKQLAVRYHLLNFLDDQSHsknYSTRAVAASY 460
Cdd:COG1651  68 LYLTPDGkdVVLGNPYAPVTVVEFFDYTCPYC---KEAFPELKKKYIDDGKVRLVLREFPFLDPACP---YCRRAAQAAR 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 461 CVAGQNDPKlYASFYSALFGSDFQPQENAASDRTDAELAHLAQTVGAEPTAISCIKSGADLGTAQTKATNasetlagFNA 540
Cdd:COG1651 142 CAADQGIVR-YWAFHDALFGSQAEAWAASILCAKDLAKADLAALDEGKKAKLNQKACDALIAKNYKLAQQ-------LGV 213
                       170       180
                ....*....|....*....|....*..
gi 15608881 541 SGTP-FVWDGSMVVNYQDPSWLARLIG 566
Cdd:COG1651 214 NGTPtFIVNGKLVPGLPDLDELKAIID 240
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
42-260 3.34e-23

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


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 104.54  E-value: 3.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881     42 VALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEI-DGQLYVDMRLINGVDLAAMLRRQGPLAPPRAVAIV 120
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    121 RQIGSALDAAHAAGATHRDVKPENILVSADDF---AYLVDFGI------ASATTDEKLTQLGNTVGTLYYMAPERFSESH 191
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIgtllpgVRDADVATLTRTTEVLGTPTYCAPEQLRGEP 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608881    192 ATYRADIYALTCVLYECLTGSPPYQGDqlSVMGAHINQAIPRPSTVRPGI---PVAfdAVIARGMAKNPEDR 260
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTGQRVVQGA--SVAEILYQQLSPVDVSLPPWIaghPLG--QVLRKALNKDPRQR 233
Thioredoxin_4 pfam13462
Thioredoxin;
389-565 2.27e-04

Thioredoxin;


Pssm-ID: 316023  Cd Length: 165  Bit Score: 41.96  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   389 GVFVGSSVAPTTIDIFNEPICPPCGSFIRSYASDIDTAVADKQLAVRYHLLNFLDDqshskNYSTRAVAASYCvAGQNDP 468
Cdd:pfam13462   4 DIVIGNPDAPVTVIEYADLRCPHCAKFHEEVLKLLEEYIDTGKVRFIYRDFPLDKE-----GESLQAAMAAHC-AGDQSP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   469 KlYASFYSALFgsdFQPQENAAsdRTDAELAHLAqtVGAEPTAISCIKSGADLGTAQTKATNASEtlAGFNAsgTP-FVW 547
Cdd:pfam13462  78 E-YFLGIDDLL---YSQQEEWA--QDLDELAALA--GDKDEKFEACLEEEDLLALVMADVNEARA--AGINF--TPtFII 145
                         170
                  ....*....|....*...
gi 15608881   548 DGSMVVNYQDPSWLARLI 565
Cdd:pfam13462 146 NGEKVDGPLTYEELKKLI 163
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
15-267 1.03e-103

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


Pssm-ID: 270916  Cd Length: 260  Bit Score: 316.84  E-value: 1.03e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  15 PYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMR 94
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  95 LINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQLGN 174
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 175 TVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGD-QLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGM 253
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDsPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250
                ....*....|....
gi 15608881 254 AKNPEDRYVTCGDL 267
Cdd:cd14014 241 AKDPEERPQSAAEL 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
16-261 6.72e-53

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 183.11  E-value: 6.72e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881     16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSetLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881     96 INGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQlgNT 175
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT--TF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    176 VGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGD-QLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGMA 254
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236

                   ....*..
gi 15608881    255 KNPEDRY 261
Cdd:smart00220 237 KDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
16-261 1.56e-46

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 169.54  E-value: 1.56e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTvreRIVALKLMSETLSSDPVFRTRMQREARTAGRLQ-EPHVVPIHDFGEIDGQLYVDMR 94
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNhPPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  95 LINGVDLAAMLR---RQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDF-AYLVDFGIASATTDEKLT 170
Cdd:COG0515  79 YVDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 171 QLGNT-----VGTLYYMAPERF---SESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQAI----------P 232
Cdd:COG0515 159 SSIPAlpstsVGTPGYMAPEVLlglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIIlelptpslasP 238
                       250       260
                ....*....|....*....|....*....
gi 15608881 233 RPSTVRPGIPVAFDAVIARGMAKNPEDRY 261
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRL 267
Pkinase pfam00069
Protein kinase domain;
16-260 1.35e-37

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 140.43  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMsETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKI-KKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881    96 INGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQlgNT 175
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSSLT--SF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   176 VGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQG-DQLSVMGAHINQ--AIPRPSTvrpgIPVAFDAVIARG 252
Cdd:pfam00069 158 VGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGiNGNEIYEKIIDQdfDSPRPSS----ISEEAKDLLKKL 233

                  ....*...
gi 15608881   253 MAKNPEDR 260
Cdd:pfam00069 234 LKKDPSKR 241
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
23-208 2.98e-37

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622  Cd Length: 215  Bit Score: 138.17  E-value: 2.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  23 GRGGMGDVYEAEDTVRERIVALKLMSETLSSDPvfRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRLINGVDLA 102
Cdd:cd00180   2 GKGSFGKVYKARDKETGKKVAVKVIPKEKLKKL--LEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 103 AMLRRQ-GPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIA-SATTDEKLTQLGNTVGTLY 180
Cdd:cd00180  80 DLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAkDLDSDDSLLKTTGGTTPPY 159
                       170       180
                ....*....|....*....|....*...
gi 15608881 181 YMAPERFSESHATYRADIYALTCVLYEC 208
Cdd:cd00180 160 YAPPELLGGRYYGPKVDIWSLGVILYEL 187
pknD PRK13184
serine/threonine-protein kinase; Reviewed
14-267 3.37e-37

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 147.61  E-value: 3.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   14 GPYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFgEIDGQL-YVD 92
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSI-CSDGDPvYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881   93 MRLINGVDLAAMLR--RQ-----GPLAPPRAVA----IVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIA 161
Cdd:PRK13184  81 MPYIEGYTLKSLLKsvWQkeslsKELAEKTSVGaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  162 SATTDEK-----------------LTQLGNTVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMg 224
Cdd:PRK13184 161 IFKKLEEedlldidvdernicyssMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI- 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15608881  225 aHINQAIPRPSTVRP--GIPVAFDAVIARGMAKNPEDRYVTCGDL 267
Cdd:PRK13184 240 -SYRDVILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQEL 283
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
16-267 1.49e-31

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK 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: 270783  Cd Length: 258  Bit Score: 123.40  E-value: 1.49e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRtRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:cd06606   2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELE-ALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  96 INGVDLAAMLRRQGPLAPPRAVAIVRQI----------GsaldaahaagATHRDVKPENILVSADDFAYLVDFGiASATT 165
Cdd:cd06606  81 VPGGSLASLLKKFGKLPEPVVRKYTRQIlegleylhsnG----------IVHRDIKGANILVDSDGVVKLADFG-CAKRL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 166 DEKLTQLGNT--VGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPY--QGDQLSVMGaHINQaiprpSTVRPGI 241
Cdd:cd06606 150 AEIATGEGTKslRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWseLGNPVAALF-KIGS-----SGEPPPI 223
                       250       260       270
                ....*....|....*....|....*....|
gi 15608881 242 PVAFDAV----IARGMAKNPEDRYvTCGDL 267
Cdd:cd06606 224 PEHLSEEakdfLRKCLQRDPKKRP-TADEL 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
16-218 2.23e-30

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK 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.


Pssm-ID: 270687  Cd Length: 258  Bit Score: 120.27  E-value: 2.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDpVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKS-EDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  96 INGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAY---LVDFGIAS-ATTDEKLTQ 171
Cdd:cd05117  81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSpikIIDFGLAKiFEEGEKLKT 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15608881 172 LgntVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGD 218
Cdd:cd05117 161 V---CGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGE 204
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
15-261 1.26e-29

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-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: 270905  Cd Length: 252  Bit Score: 118.00  E-value: 1.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  15 PYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMS-ETLSSDPvfRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDM 93
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDkSKLKEEI--EEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  94 RLINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLtqLG 173
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSL--LK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 174 NTVGTLYYMAPERFS-ESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQA-IPRPSTVRPGipvaFDAVIAR 251
Cdd:cd14003 157 TFCGTPAYAAPEVLLgRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGkYPIPSHLSPD----ARDLIRR 232
                       250
                ....*....|
gi 15608881 252 GMAKNPEDRY 261
Cdd:cd14003 233 MLVVDPSKRI 242
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
16-260 1.30e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855  Cd Length: 258  Bit Score: 115.25  E-value: 1.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSeTLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEID-LSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  96 INGVDLAAMLRRQ----GPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEklTQ 171
Cdd:cd08215  81 ADGGDLAQKIKKQkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLEST--TD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 172 LGNT-VGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQAIPRPstvrpgIPVAFDA--- 247
Cdd:cd08215 159 LAKTvVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPP------IPSQYSSelr 232
                       250
                ....*....|....
gi 15608881 248 -VIARGMAKNPEDR 260
Cdd:cd08215 233 dLVNSMLQKDPEKR 246
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
16-215 1.69e-27

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-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: 270797  Cd Length: 254  Bit Score: 111.93  E-value: 1.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMS-ETLSSDPVFRTRMqrEARTAGRLQEPHVVPIHDFGEIDGQLYVDMR 94
Cdd:cd06627   2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISlEKIPKSDLKSVMG--EIDLLKKLNHPNIVKYIGSVKTKDSLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  95 LINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKlTQLGN 174
Cdd:cd06627  80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVE-KDENS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15608881 175 TVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPY 215
Cdd:cd06627 159 VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY 199
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
16-260 7.18e-27

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001  Cd Length: 258  Bit Score: 110.34  E-value: 7.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  16 YRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRL 95
Cdd:cd14099   3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881  96 INGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASattdeKLTQLGN- 174
Cdd:cd14099  83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAA-----RLEYDGEr 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608881 175 --TV-GTLYYMAPE-RFSESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQA---IPRpstvRPGIPVAFDA 247
Cdd:cd14099 158 kkTLcGTPNYIAPEvLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNeysFPS----HLSISDEAKD 233
                       250
                ....*....|...
gi 15608881 248 VIARGMAKNPEDR 260
Cdd:cd14099 234 L