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Conserved domains on  [gi|118471844|ref|YP_884449|]
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serine-threonine protein kinase [Mycobacterium smegmatis str. MC2 155]

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 ...
10-275 3.44e-129

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: 384.25  E-value: 3.44e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETpngpLPY 89
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDG----RPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGns 169
Cdd:cd14014   77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSG-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 170 VTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDA 249
Cdd:cd14014  155 LTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                        250       260
                 ....*....|....*....|....*.
gi 118471844 250 VVLKALAKNPDNRYQTAAEMRADLIR 275
Cdd:cd14014  235 IILRALAKDPEERPQSAAELLAALRA 260
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
355-623 1.05e-57

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 225372  Cd Length: 303  Bit Score: 198.79  E-value: 1.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 355 NPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGL 434
Cdd:COG2815   22 SPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQYITVPDVVGL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 435 TPTQARQKLKDAGFEKFRESPSPSTPE-QKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAA 513
Cdd:COG2815  102 TIEEAVAKLKAYGLNLSKITQEEVSDEvPAGTVISQSPSAGTEVKPGETVKLTVSKGPETITVPDLVGMTYDEASSNLKA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 514 GGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGnQFVMPDLVGQFWSDAYPRLTALGWTG---VLDKGP 590
Cdd:COG2815  182 AGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKG-AFVAPDLSGMFTVEAEPHPREEGDTSqevIRDKDA 260
                        250       260       270
                 ....*....|....*....|....*....|...
gi 118471844 591 DVRDSGQRTNaVVTQSPSAGTPVNKDAKITLSF 623
Cdd:COG2815  261 DVTASGTDSS-VNIQPPPGGTIVLKGSEITSGI 292
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
10-275 3.44e-129

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: 384.25  E-value: 3.44e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETpngpLPY 89
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDG----RPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGns 169
Cdd:cd14014   77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSG-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 170 VTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDA 249
Cdd:cd14014  155 LTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                        250       260
                 ....*....|....*....|....*.
gi 118471844 250 VVLKALAKNPDNRYQTAAEMRADLIR 275
Cdd:cd14014  235 IILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-272 4.05e-79

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 254.38  E-value: 4.05e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844    11 YELGEILGFGGMSEVHLARDLRLHRDVAVKVLRadLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPngplPYI 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK----LYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844    91 VMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSV 170
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   171 TqtaaVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAV 250
Cdd:smart00220 155 T----FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250       260
                   ....*....|....*....|..
gi 118471844   251 VLKALAKNPDNRYqTAAEMRAD 272
Cdd:smart00220 231 IRKLLVKDPEKRL-TAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-331 2.63e-59

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 205.75  E-value: 2.63e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  11 YELGEILGFGGMSEVHLARDlrlHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHP-AIVAVYDTGEAETPNgplpY 89
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL----Y 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHTDG---PIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKN-NAVKVMDFGIARALAD 165
Cdd:COG0515   75 LVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 166 TGNSVTQ---TAAVIGTAQYLSPEQARG---ETVDARSDVYSLGCVLYEILTGEPPFIGDS---PVAVAYQHVREDPVP- 235
Cdd:COG0515  155 PGSTSSIpalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKnssATSQTLKIILELPTPs 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 236 -----PSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRvHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQ 310
Cdd:COG0515  235 lasplSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA-HLKLKESDLSDLLKPDDSAPLRLSLPPSLEALIS 313
                        330       340
                 ....*....|....*....|.
gi 118471844 311 DMPVPRPAGYSKQRSTSVARW 331
Cdd:COG0515  314 SLNSLAISGSDLKLDDSNFSK 334
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
355-623 1.05e-57

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225372  Cd Length: 303  Bit Score: 198.79  E-value: 1.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 355 NPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGL 434
Cdd:COG2815   22 SPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQYITVPDVVGL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 435 TPTQARQKLKDAGFEKFRESPSPSTPE-QKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAA 513
Cdd:COG2815  102 TIEEAVAKLKAYGLNLSKITQEEVSDEvPAGTVISQSPSAGTEVKPGETVKLTVSKGPETITVPDLVGMTYDEASSNLKA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 514 GGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGnQFVMPDLVGQFWSDAYPRLTALGWTG---VLDKGP 590
Cdd:COG2815  182 AGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKG-AFVAPDLSGMFTVEAEPHPREEGDTSqevIRDKDA 260
                        250       260       270
                 ....*....|....*....|....*....|...
gi 118471844 591 DVRDSGQRTNaVVTQSPSAGTPVNKDAKITLSF 623
Cdd:COG2815  261 DVTASGTDSS-VNIQPPPGGTIVLKGSEITSGI 292
Pkinase pfam00069
Protein kinase domain;
11-269 2.70e-54

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 187.81  E-value: 2.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   11 YELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLArDPSFYLRFRREAQNAAALNHPAIVAVYDtgeAETPNGPLpYI 90
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLNHPNIVRLYD---AFEDKDNL-YL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   91 VMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALadtGNSV 170
Cdd:pfam00069  76 VLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQL---NSGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  171 TQTAAViGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRhaDVTPELDAV 250
Cdd:pfam00069 153 SLTSFV-GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRPS--SISEEAKDL 229
                         250
                  ....*....|....*....
gi 118471844  251 VLKALAKNPDNRYqTAAEM 269
Cdd:pfam00069 230 LKKLLKKDPSKRL-TATEA 247
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-273 1.17e-45

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 174.19  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYdTGEAEtpnGPLPY 89
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVY-SICSD---GDPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHT-------DGPIAPRRAI----EIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFG 158
Cdd:PRK13184  79 YTMPYIEGYTLKSLLKSvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 159 IARA-------LADTG--------NSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVA 223
Cdd:PRK13184 159 AAIFkkleeedLLDIDvdernicySSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRK 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 118471844 224 VAYQHVREDP--VPPSRrhaDVTPELDAVVLKALAKNPDNRYQTAAEMRADL 273
Cdd:PRK13184 239 ISYRDVILSPieVAPYR---EIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-266 4.13e-42

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: 164.25  E-value: 4.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844    37 VAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPngpLPYIVMEYVDGVTLRDIVHTDGPIAPRRAI 116
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPG---LLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   117 EIIADACQALNFSHQHGIIHRDVKPANIMISKNNA---VKVMDFGIARALADTGN----SVTQTAAVIGTAQYLSPEQAR 189
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLPGVRDadvaTLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   190 GETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPV--PPS-RRHadvtpELDAVVLKALAKNPDNRYQTA 266
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVslPPWiAGH-----PLGQVLRKALNKDPRQRAASA 237
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
359-421 2.93e-14

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 309063  Cd Length: 63  Bit Score: 69.57  E-value: 2.93e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118471844  359 VQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVST 421
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
360-420 6.22e-14

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 68.71  E-value: 6.22e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118471844 360 QVPDVAEQSADDAQAALQNRGFK-TVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVS 420
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA smart00740
PASTA domain;
355-421 3.33e-12

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 63.86  E-value: 3.33e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118471844   355 NPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVST 421
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
10-275 3.44e-129

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: 384.25  E-value: 3.44e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETpngpLPY 89
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDG----RPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGns 169
Cdd:cd14014   77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSG-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 170 VTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDA 249
Cdd:cd14014  155 LTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                        250       260
                 ....*....|....*....|....*.
gi 118471844 250 VVLKALAKNPDNRYQTAAEMRADLIR 275
Cdd:cd14014  235 IILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-272 4.05e-79

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 254.38  E-value: 4.05e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844    11 YELGEILGFGGMSEVHLARDLRLHRDVAVKVLRadLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPngplPYI 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK----LYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844    91 VMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSV 170
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   171 TqtaaVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAV 250
Cdd:smart00220 155 T----FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250       260
                   ....*....|....*....|..
gi 118471844   251 VLKALAKNPDNRYqTAAEMRAD 272
Cdd:smart00220 231 IRKLLVKDPEKRL-TAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-331 2.63e-59

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 205.75  E-value: 2.63e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  11 YELGEILGFGGMSEVHLARDlrlHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHP-AIVAVYDTGEAETPNgplpY 89
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL----Y 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHTDG---PIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKN-NAVKVMDFGIARALAD 165
Cdd:COG0515   75 LVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 166 TGNSVTQ---TAAVIGTAQYLSPEQARG---ETVDARSDVYSLGCVLYEILTGEPPFIGDS---PVAVAYQHVREDPVP- 235
Cdd:COG0515  155 PGSTSSIpalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKnssATSQTLKIILELPTPs 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 236 -----PSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRvHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQ 310
Cdd:COG0515  235 lasplSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA-HLKLKESDLSDLLKPDDSAPLRLSLPPSLEALIS 313
                        330       340
                 ....*....|....*....|.
gi 118471844 311 DMPVPRPAGYSKQRSTSVARW 331
Cdd:COG0515  314 SLNSLAISGSDLKLDDSNFSK 334
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
355-623 1.05e-57

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225372  Cd Length: 303  Bit Score: 198.79  E-value: 1.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 355 NPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGL 434
Cdd:COG2815   22 SPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQYITVPDVVGL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 435 TPTQARQKLKDAGFEKFRESPSPSTPE-QKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAA 513
Cdd:COG2815  102 TIEEAVAKLKAYGLNLSKITQEEVSDEvPAGTVISQSPSAGTEVKPGETVKLTVSKGPETITVPDLVGMTYDEASSNLKA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 514 GGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGnQFVMPDLVGQFWSDAYPRLTALGWTG---VLDKGP 590
Cdd:COG2815  182 AGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKG-AFVAPDLSGMFTVEAEPHPREEGDTSqevIRDKDA 260
                        250       260       270
                 ....*....|....*....|....*....|...
gi 118471844 591 DVRDSGQRTNaVVTQSPSAGTPVNKDAKITLSF 623
Cdd:COG2815  261 DVTASGTDSS-VNIQPPPGGTIVLKGSEITSGI 292
Pkinase pfam00069
Protein kinase domain;
11-269 2.70e-54

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 187.81  E-value: 2.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   11 YELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLArDPSFYLRFRREAQNAAALNHPAIVAVYDtgeAETPNGPLpYI 90
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLNHPNIVRLYD---AFEDKDNL-YL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844   91 VMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALadtGNSV 170
Cdd:pfam00069  76 VLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQL---NSGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  171 TQTAAViGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRhaDVTPELDAV 250
Cdd:pfam00069 153 SLTSFV-GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRPS--SISEEAKDL 229
                         250
                  ....*....|....*....
gi 118471844  251 VLKALAKNPDNRYqTAAEM 269
Cdd:pfam00069 230 LKKLLKKDPSKRL-TATEA 247
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
10-269 8.98e-54

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: 186.51  E-value: 8.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLraDLARDPSfylRFRREAQNAA----ALNHPAIVAVYDTGEAetpNG 85
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEI--DLSNMSE---KEREEALNEVkllsKLKHPNIVKYYESFEE---NG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  86 PLpYIVMEYVDGVTLRDIV----HTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIAR 161
Cdd:cd08215   73 KL-CIVMEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 162 ALADTgNSVTQTaaVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRha 241
Cdd:cd08215  152 VLEST-TDLAKT--VVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQ-- 226
                        250       260
                 ....*....|....*....|....*...
gi 118471844 242 dVTPELDAVVLKALAKNPDNRYqTAAEM 269
Cdd:cd08215  227 -YSSELRDLVNSMLQKDPEKRP-SANEI 252
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
17-262 1.56e-51

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) 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. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901  Cd Length: 245  Bit Score: 180.04  E-value: 1.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  17 LGFGGMSEVHLARdlrlHR--DVAVKVLRADLARDpSFYLRFRREAQNAAALNHPAIVAVYdtGEAETPngPLPYIVMEY 94
Cdd:cd13999    1 IGSGSFGEVYKGK----WRgtDVAIKKLKVEDDND-ELLKEFRREVSILSKLRHPNIVQFI--GACLSP--PPLCIVTEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  95 VDGVTLRDIVHT-DGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTqt 173
Cdd:cd13999   72 MPGGSLYDLLHKkKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMT-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 174 aAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADvtPELDAVVLK 253
Cdd:cd13999  150 -GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCP--PELSKLIKR 226

                 ....*....
gi 118471844 254 ALAKNPDNR 262
Cdd:cd13999  227 CWNEDPEKR 235
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
17-273 2.15e-50

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: 175.92  E-value: 2.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  17 LGFGGMSEVHLARDLRLHRDVAVKVLraDLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNgplpYIVMEYVD 96
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVI--PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFL----YLVMEYCE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  97 GVTLRDIVHT-DGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAA 175
Cdd:cd00180   75 GGSLKDLLKEnKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 176 vIGTAQYLSPEQARGETVDARSDVYSLGCVLYEIltgeppfigdspvavayqhvredpvppsrrhadvtPELDAVVLKAL 255
Cdd:cd00180  155 -TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRML 198
                        250
                 ....*....|....*...
gi 118471844 256 AKNPDNRYqTAAEMRADL 273
Cdd:cd00180  199 QYDPKKRP-SAKELLEHL 215
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
10-272 1.46e-47

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: 168.85  E-value: 1.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFyLRFRREAQNAAALNHPAIVAVYDTgeAETPNgpLPY 89
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIE-EKIKREIEIMKLLNHPNIIKLYEV--IETEN--KIY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALadTGNS 169
Cdd:cd14003   76 LVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF--RGGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 170 VTQTaaVIGTAQYLSPEQARGETVDAR-SDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRrhadVTPELD 248
Cdd:cd14003  154 LLKT--FCGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSH----LSPDAR 227
                        250       260
                 ....*....|....*....|....
gi 118471844 249 AVVLKALAKNPDNRYqTAAEMRAD 272
Cdd:cd14003  228 DLIRRMLVVDPSKRI-TIEEILNH 250
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
11-262 1.79e-47

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE 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: 270692  Cd Length: 254  Bit Score: 168.92  E-value: 1.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  11 YELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRfrrEAQNAAALNHPAIVAVYDtgeAETPNGPLpYI 90
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILN---EIAILKKCKHPNIVKYYG---SYLKKDEL-WI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  91 VMEYVDGVTLRDIV-HTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNS 169
Cdd:cd05122   75 VMEFCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844 170 VTQtaavIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPvPPSRRHADVTPELDA 249
Cdd:cd05122  155 NTF----VGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGP-PGLRNPKKWSKEFKD 229
                        250
                 ....*....|...
gi 118471844 250 VVLKALAKNPDNR 262
Cdd:cd05122  230 FLKKCLQKDPEKR 242
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-273 1.17e-45

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 174.19  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  10 RYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYdTGEAEtpnGPLPY 89
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVY-SICSD---GDPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118471844  90 IVM