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Conserved domains on  [gi|15901564|ref|NP_346168|]
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serine/threonine protein kinase [Streptococcus pneumoniae TIGR4]

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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 ...
11-271 1.43e-121

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 [Multi-domain]  Cd Length: 260  Bit Score: 364.99  E-value: 1.43e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  11 RYRIVKQIGRGGMADVYLAKDLiLDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDT-LLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  91 EYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQKPLPSVIAENPSVPQALENVIIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 15901564 251 TAKKLTNRYRSVSEMYVDLSS 271
Cdd:cd14014 240 LAKDPEERPQSAAELLAALRA 260
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
372-432 6.19e-18

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: 79.11  E-value: 6.19e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15901564 372 IPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVS 432
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
584-649 4.47e-04

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: 39.05  E-value: 4.47e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15901564 584 MPSYIGSSLEFTKNNLiqivgiKEANIEVVEVTT-APAGSAEGMVVEQSPRAGEKVDLNkTRVKISI 649
Cdd:cd06577   2 VPDVVGMTLDEAKAAL------EAAGLKVGVVTEeYSDDVPKGTVISQSPAAGTKVKKG-STVTLTV 61
PASTA smart00740
PASTA domain;
506-577 2.33e-05

PASTA domain;


:

Pssm-ID: 197851  Cd Length: 67  Bit Score: 42.68  E-value: 2.33e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15901564    506 KATTIQLGNYIGRNSTEVISELKQKKVPenlIKIEEEESSESEPGTIMKQSPGAGTTydVSKPTQIVLTVAK 577
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLK---VEVVEEYSSDGEEGTVISQSPAAGTT--VKPGSKVTLTVSK 67
PASTA smart00740
PASTA domain;
434-505 8.64e-05

PASTA domain;


:

Pssm-ID: 197851  Cd Length: 67  Bit Score: 41.14  E-value: 8.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15901564    434 GKQSFQISNYVGRKSSDVIAELKEKKVPdnlIKIEEEESNESEAGTVLKQSLPEGTTYDlsKATQIVLTVAK 505
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLK---VEVVEEYSSDGEEGTVISQSPAAGTTVK--PGSKVTLTVSK 67
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-247 4.44e-75

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 243.21  E-value: 4.44e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564     12 YRIVKQIGRGGMADVYLAKDlILDGEEVAVKVLRTNYQTDPiaVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-KKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564     92 YVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLtqTNS 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15901564    172 MLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQKPLPSVIAENPSVPQALENVI 247
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLI 231
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
345-659 2.67e-71

Uncharacterized protein conserved in bacteria [Function unknown]


:

Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 235.00  E-value: 2.67e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 345 YLILLASLVLVAASLIWILSRTPATIAIPDVAGQTVAEAKATLKKANFEIgEEKTEASEKVEEGRIIRTDPGAGTGRKEG 424
Cdd:COG2815   1 LLSLLVSLVVAGVLLATFFPVSPDKVKVPNVAGLDEEDAKAELQKAGLEV-GVRERESDKVPEGKVIRTDPKAGTVVKQG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 425 TKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIeEEESNESEAGTVLKQSLPEGTTYDLSKatQIVLTVA 504
Cdd:COG2815  80 SKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKITQ-EEVSDEVPAGTVISQSPSAGTEVKPGE--TVKLTVS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 505 KKATTIQLGNYIGRNSTEVISELKQKKVPENlikIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTvakKVTSVAM 584
Cdd:COG2815 157 KGPETITVPDLVGMTYDEASSNLKAAGLTVN---SKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVS---KGAFVAP 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15901564 585 PSYIGSSLEFTKNNLIQIVGIKEAnIEVVEVTTAPAGSAEgmVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP 659
Cdd:COG2815 231 DLSGMFTVEAEPHPREEGDTSQEV-IRDKDADVTASGTDS--SVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVI 302
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-271 1.43e-121

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 [Multi-domain]  Cd Length: 260  Bit Score: 364.99  E-value: 1.43e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  11 RYRIVKQIGRGGMADVYLAKDLiLDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDT-LLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  91 EYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQKPLPSVIAENPSVPQALENVIIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 15901564 251 TAKKLTNRYRSVSEMYVDLSS 271
Cdd:cd14014 240 LAKDPEERPQSAAELLAALRA 260
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
372-432 6.19e-18

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: 79.11  E-value: 6.19e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15901564 372 IPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVS 432
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
584-649 4.47e-04

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: 39.05  E-value: 4.47e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15901564 584 MPSYIGSSLEFTKNNLiqivgiKEANIEVVEVTT-APAGSAEGMVVEQSPRAGEKVDLNkTRVKISI 649
Cdd:cd06577   2 VPDVVGMTLDEAKAAL------EAAGLKVGVVTEeYSDDVPKGTVISQSPAAGTKVKKG-STVTLTV 61
PASTA smart00740
PASTA domain;
366-433 3.46e-14

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 68.49  E-value: 3.46e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15901564    366 TPATIAIPDVAGQTVAEAKATLKKANFEIgEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSS 433
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKV-EVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
370-433 1.25e-12

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: 252166  Cd Length: 63  Bit Score: 63.79  E-value: 1.25e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15901564   370 IAIPDVAGQTVAEAKATLKKANFEIGEeKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSS 433
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGT-VEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
578-648 6.04e-08

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 50.38  E-value: 6.04e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15901564    578 KVTSVAMPSYIGSSLEFTKNNLiqivgiKEANIEVVEVTTAPAGSAEGMVVEQSPRAGEKVDLNKT-RVKIS 648
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLL------KALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKvTLTVS 66
PASTA smart00740
PASTA domain;
506-577 2.33e-05

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 42.68  E-value: 2.33e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15901564    506 KATTIQLGNYIGRNSTEVISELKQKKVPenlIKIEEEESSESEPGTIMKQSPGAGTTydVSKPTQIVLTVAK 577
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLK---VEVVEEYSSDGEEGTVISQSPAAGTT--VKPGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
582-651 2.84e-05

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: 252166  Cd Length: 63  Bit Score: 42.60  E-value: 2.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   582 VAMPSYIGSSLEFTKNNLiqivgiKEANIEVVEVTTAPAGSAEGMVVEQSPRAGEKVDlNKTRVKISIYK 651
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLL------EALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVK-KGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
434-505 8.64e-05

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 41.14  E-value: 8.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15901564    434 GKQSFQISNYVGRKSSDVIAELKEKKVPdnlIKIEEEESNESEAGTVLKQSLPEGTTYDlsKATQIVLTVAK 505
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLK---VEVVEEYSSDGEEGTVISQSPAAGTTVK--PGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
510-577 6.83e-04

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: 252166  Cd Length: 63  Bit Score: 38.37  E-value: 6.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15901564   510 IQLGNYIGRNSTEVISELKQKKVpenLIKIEEEESSESEPGTIMKQSPGAGTTydVSKPTQIVLTVAK 577
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGL---KVGTVEEYSDDVGEGTVISQSPPAGTK--VKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
438-505 8.98e-04

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: 252166  Cd Length: 63  Bit Score: 37.98  E-value: 8.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15901564   438 FQISNYVGRKSSDVIAELKEKKVpdnLIKIEEEESNESEAGTVLKQSLPEGTTydLSKATQIVLTVAK 505
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGL---KVGTVEEYSDDVGEGTVISQSPPAGTK--VKKGSKVTLTVSK 63
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-247 4.44e-75

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 243.21  E-value: 4.44e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564     12 YRIVKQIGRGGMADVYLAKDlILDGEEVAVKVLRTNYQTDPiaVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-KKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564     92 YVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLtqTNS 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15901564    172 MLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQKPLPSVIAENPSVPQALENVI 247
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLI 231
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
345-659 2.67e-71

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 235.00  E-value: 2.67e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 345 YLILLASLVLVAASLIWILSRTPATIAIPDVAGQTVAEAKATLKKANFEIgEEKTEASEKVEEGRIIRTDPGAGTGRKEG 424
Cdd:COG2815   1 LLSLLVSLVVAGVLLATFFPVSPDKVKVPNVAGLDEEDAKAELQKAGLEV-GVRERESDKVPEGKVIRTDPKAGTVVKQG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 425 TKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIeEEESNESEAGTVLKQSLPEGTTYDLSKatQIVLTVA 504
Cdd:COG2815  80 SKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKITQ-EEVSDEVPAGTVISQSPSAGTEVKPGE--TVKLTVS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 505 KKATTIQLGNYIGRNSTEVISELKQKKVPENlikIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTvakKVTSVAM 584
Cdd:COG2815 157 KGPETITVPDLVGMTYDEASSNLKAAGLTVN---SKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVS---KGAFVAP 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15901564 585 PSYIGSSLEFTKNNLIQIVGIKEAnIEVVEVTTAPAGSAEgmVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP 659
Cdd:COG2815 231 DLSGMFTVEAEPHPREEGDTSQEV-IRDKDADVTASGTDS--SVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVI 302
Pkinase pfam00069
Protein kinase domain;
12-249 4.07e-63

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 211.72  E-value: 4.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564    12 YRIVKQIGRGGMADVYLAKDlILDGEEVAVKVLRTnYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAME 91
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKH-KGTGKIVAVKILKK-RSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564    92 YVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFaETSLTQTNS 171
Cdd:pfam00069  79 YCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKL-TKSSSSLTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   172 MLGSVHYLSPEQARGSK-ATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTiALQHFQK----PLPSVIAENPSVPQALENV 246
Cdd:pfam00069 158 FVGTPEYMAPEVLLGGNgYGPKVDVWSLGVILYELLTGKPPFSGESILD-QLQLIRRilgpPLEFDEPKSDSGSEEAKDL 236

                  ...
gi 15901564   247 IIK 249
Cdd:pfam00069 237 IKK 239
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
12-308 1.10e-60

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


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 209.21  E-value: 1.10e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  12 YRIVKQIGRGGMADVYLAKDLildgEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHP-HIVRITDIGEEDGQQYLAM 90
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR----KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  91 EYVAGLDLKRYIKEHY---PLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGT-AKVTDFGIAVAFAETSL 166
Cdd:COG0515  78 EYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 167 TQ-----TNSMLGSVHYLSPEQARGS---KATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQK---------PL 229
Cdd:COG0515 158 TSsipalPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIilelptpslAS 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15901564 230 PSVIAENPSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSIP 308
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLN 316
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-307 1.88e-51

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 192.37  E-value: 1.88e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564     36 GEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGE-EDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAV 114
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564    115 RIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGT---AKVTDFGIAV------AFAETSLTQTNSMLGSVHYLSPEQAR 185
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTllpgvrDADVATLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564    186 GSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQK---PLPSVIAENPsVPQALENVIIK------ATAKKLT 256
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPvdvSLPPWIAGHP-LGQVLRKALNKdprqraASAPALA 241
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15901564    257 NRYRSVSemYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSI 307
Cdd:TIGR03903  242 ERFRALE--LCALVGILRMGEGAGREAIAAPLVASGTLDGETGERRQLTAL 290
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-273 1.28e-46

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 176.50  E-value: 1.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   10 GRYRIVKQIGRGGMADVYLAKDLILdGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLA 89
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVC-SRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   90 MEYVAGLDLKRYIKEHY-------PLSNEEAV----RIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIA 158
Cdd:PRK13184  81 MPYIEGYTLKSLLKSVWqkeslskELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  159 VA-------FAETSLTQTNSM----------LGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIA 221
Cdd:PRK13184 161 IFkkleeedLLDIDVDERNICyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKIS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15901564  222 LQHfQKPLPSVIAENPSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSL 273
Cdd:PRK13184 241 YRD-VILSPIEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHL 291
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
12-280 8.29e-29

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 118.97  E-value: 8.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   12 YRIVKQIGRGGMADVYLAKDLILDGEEVAVKVLRTNyqtDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAME 91
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVATRGSDPKEKVVAKFVMLN---DERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIME 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   92 YVAGLDL----KRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAET-SL 166
Cdd:PTZ00267 146 YGSGGDLnkqiKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSvSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  167 TQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHF---QKPLPSVIAENPSV---P 240
Cdd:PTZ00267 226 DVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLygkYDPFPCPVSSGMKAlldP 305
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15901564  241 QALENVIIKATAKKL--TNRYRSVSEMYVDL---SSSLSYNRRNE 280
Cdd:PTZ00267 306 LLSKNPALRPTTQQLlhTEFLKYVANLFQDIvrhSETISPHDREE 350
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
11-218 3.83e-22

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 96.81  E-value: 3.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   11 RYRIVKQIGRGGMADVYLAKDLILDgEEVAVKVLRTNyQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAM 90
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTN-ETIALKKIRLE-QEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   91 EYVaGLDLKRYIKEHYPLSNEEAV--RIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTA-KVTDFGIAVAFAETSLT 167
Cdd:PLN00009  81 EYL-DLDLKKHMDSSPDFAKNPRLikTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNAlKLADFGLARAFGIPVRT 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15901564  168 QTNSMLgSVHYLSPEQARGSKA-TVQSDIYAMGIIFYEMLTGHIPYDGDSAV 218
Cdd:PLN00009 160 FTHEVV-TLWYRAPEILLGSRHySTPVDIWSVGCIFAEMVNQKPLFPGDSEI 210
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
69-230 3.29e-16

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 77.97  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564   69 DHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLT-PD 147
Cdd:PHA03390  67 DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  148 GTAKVTDFGIAVAfaetslTQTNSML-GSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSA----VTIAL 222
Cdd:PHA03390 147 DRIYLCDYGLCKI------IGTPSCYdGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDeeldLESLL 220

                 ....*...
gi 15901564  223 QHFQKPLP 230
Cdd:PHA03390 221 KRQQKKLP 228
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-271 1.43e-121

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 [Multi-domain]  Cd Length: 260  Bit Score: 364.99  E-value: 1.43e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  11 RYRIVKQIGRGGMADVYLAKDLiLDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDT-LLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  91 EYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQKPLPSVIAENPSVPQALENVIIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 15901564 251 TAKKLTNRYRSVSEMYVDLSS 271
Cdd:cd14014 240 LAKDPEERPQSAAELLAALRA 260
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
372-432 6.19e-18

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: 79.11  E-value: 6.19e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15901564 372 IPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVS 432
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
584-649 4.47e-04

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: 39.05  E-value: 4.47e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15901564 584 MPSYIGSSLEFTKNNLiqivgiKEANIEVVEVTT-APAGSAEGMVVEQSPRAGEKVDLNkTRVKISI 649
Cdd:cd06577   2 VPDVVGMTLDEAKAAL------EAAGLKVGVVTEeYSDDVPKGTVISQSPAAGTKVKKG-STVTLTV 61
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
11-216 3.28e-56

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 [Multi-domain]  Cd Length: 252  Bit Score: 192.35  E-value: 3.28e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  11 RYRIVKQIGRGGMADVYLAKDlILDGEEVAVKVLRtNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAM 90
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARH-KLTGEKVAIKIID-KSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  91 EYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTn 170
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKT- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15901564 171 sMLGSVHYLSPEQARGSK-ATVQSDIYAMGIIFYEMLTGHIPYDGDS 216
Cdd:cd14003 158 -FCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDN 203
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-205 3.49e-55

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 [Multi-domain]  Cd Length: 215  Bit Score: 188.25  E-value: 3.49e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  18 IGRGGMADVYLAKDLIlDGEEVAVKVLRTNYQTDPIAvaRFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLD 97
Cdd:cd00180   1 LGKGSFGKVYKARDKE-TGKKVAVKVIPKEKLKKLLE--ELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15901564  98 LKRYIKEH-YPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAE-TSLTQTNSMLGS 175
Cdd:cd00180  78 LKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSdDSLLKTTGGTTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 15901564 176 VHYLSPEQARGSKATVQSDIYAMGIIFYEM 205
Cdd:cd00180 158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-220 1.93e-51

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 [Multi-domain]  Cd Length: 258  Bit Score: 179.21  E-value: 1.93e-51