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Conserved domains on  [gi|16803860|ref|NP_465345.1|]
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serine/threonine protein kinase [Listeria monocytogenes EGD-e]

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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 ...
10-269 1.22e-127

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: 380.39  E-value: 1.22e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  10 RYKILHAIGGGGMANVYLAHDIILDRDVAVKILRIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVME 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  90 HVDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETSITQTNS 169
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 170 LLGSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKHLQADIPSAREQNPEIPQSLENIIIKAT 249
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250       260
                ....*....|....*....|
gi 16803860 250 AKDPFLRYQNAEEMEKDLQT 269
Cdd:cd14014 241 AKDPEERPQSAAELLAALRA 260
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
369-429 9.33e-19

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: 81.42  E-value: 9.33e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16803860 369 VPDVSGKTEDQAVALLQKEGFVIGKTAEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVS 429
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
436-498 2.63e-13

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: 66.01  E-value: 2.63e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16803860 436 TMDDYTGRSYTDTKALLEEQGFKNISSEEAYSSEIEKGLIISQTPTQGTEVVAKSTdVKFVVS 498
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGST-VTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
505-565 1.29e-12

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: 63.70  E-value: 1.29e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16803860 505 TLKDLRGYTKTAVEDYASPLGLKVSS-KEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVIS 565
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVvTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
362-647 7.19e-89

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


:

Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 281.61  E-value: 7.19e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 362 KSPDEVAVPDVSGKTEDQAVALLQKEGFVIGkTAEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVSIGSKKITMDDYT 441
Cdd:COG2815  21 VSPDKVKVPNVAGLDEEDAKAELQKAGLEVG-VRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQYITVPDVV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 442 GRSYTDTKALLEEQGFKNISSE-EAYSSEIEKGLIISQTPTQGTEVVAKSTdVKFVVSKGAEPITLKDLRGYTKTAVEDY 520
Cdd:COG2815 100 GLTIEEAVAKLKAYGLNLSKITqEEVSDEVPAGTVISQSPSAGTEVKPGET-VKLTVSKGPETITVPDLVGMTYDEASSN 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 521 ASPLGLKVSSKEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVISAGPKEKQVKEVTKTFNIPYTPsDEENPQPQKiQIY 600
Cdd:COG2815 179 LKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGMFTVEAEPHP-REEGDTSQE-VIR 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 16803860 601 IQDKDHSMTSAYREMSITQNTSVEITFQIEEGSSAGYKIISDDKVID 647
Cdd:COG2815 257 DKDADVTASGTDSSVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVIS 303
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-264 6.84e-79

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 253.22  E-value: 6.84e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860     11 YKILHAIGGGGMANVYLAHDIILDRDVAVKIlrIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVMEH 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV--IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860     91 VDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETsiTQTNSL 170
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG--EKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    171 LGSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKHLQADIPSAREQNPEIPQSLENIIIKATA 250
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 16803860    251 KDPFLRYQNAEEME 264
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
10-269 1.22e-127

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: 380.39  E-value: 1.22e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  10 RYKILHAIGGGGMANVYLAHDIILDRDVAVKILRIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVME 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  90 HVDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETSITQTNS 169
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 170 LLGSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKHLQADIPSAREQNPEIPQSLENIIIKAT 249
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250       260
                ....*....|....*....|
gi 16803860 250 AKDPFLRYQNAEEMEKDLQT 269
Cdd:cd14014 241 AKDPEERPQSAAELLAALRA 260
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
369-429 9.33e-19

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: 81.42  E-value: 9.33e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16803860 369 VPDVSGKTEDQAVALLQKEGFVIGKTAEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVS 429
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
436-498 2.63e-13

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: 66.01  E-value: 2.63e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16803860 436 TMDDYTGRSYTDTKALLEEQGFKNISSEEAYSSEIEKGLIISQTPTQGTEVVAKSTdVKFVVS 498
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGST-VTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
505-565 1.29e-12

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: 63.70  E-value: 1.29e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16803860 505 TLKDLRGYTKTAVEDYASPLGLKVSS-KEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVIS 565
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVvTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
367-429 1.80e-13

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: 66.49  E-value: 1.80e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16803860   367 VAVPDVSGKTEDQAVALLQKEGFVIgKTAEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVS 429
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKV-GTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVS 62
PASTA smart00740
PASTA domain;
363-429 3.79e-13

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 65.40  E-value: 3.79e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16803860    363 SPDEVAVPDVSGKTEDQAVALLQKEGFVIGKTaEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVS 429
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVV-EEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVS 66
PASTA smart00740
PASTA domain;
500-565 1.39e-12

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 63.86  E-value: 1.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16803860    500 GAEPITLKDLRGYTKTAVEDYASPLGLKVSSKEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVIS 565
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVS 66
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
504-565 3.41e-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: 62.63  E-value: 3.41e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16803860   504 ITLKDLRGYTKTAVEDYASPLGLKVSSKEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVIS 565
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVS 62
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
17-165 1.59e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 63.00  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   17 IGGGGMANVYLAHdiILDRDVAVKI-----LRIDLADESNLIRRFQREAQ--SATSLVHPNIVSVYDVGEENDLhyIVME 89
Cdd:PRK14879   4 IKRGAEAEIYLGD--FLGIKAVIKWripkrYRHPELDERIRRERTRREARimSRARKAGVNVPAVYFVDPENFI--IVME 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16803860   90 HVDGMDLKQYIHENHPISYEKAVDIMLQivsaVAIAHQHHIIHRDLKPQNILIDHDGVVKItDFGiamaLSETSIT 165
Cdd:PRK14879  80 YIEGEPLKDLINSNGMEELELSREIGRL----VGKLHSAGIIHGDLTTSNMILSGGKIYLI-DFG----LAEFSKD 146
PASTA smart00740
PASTA domain;
431-499 1.27e-10

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 58.09  E-value: 1.27e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16803860    431 GSKKITMDDYTGRSYTDTKALLEEQGFKnISSEEAYSSEIEKGLIISQTPTQGTEvVAKSTDVKFVVSK 499
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLK-VEVVEEYSSDGEEGTVISQSPAAGTT-VKPGSKVTLTVSK 67
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
14-156 1.88e-10

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168  Cd Length: 204  Bit Score: 59.60  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  14 LHAIGGGGMANVYLAHdiILDRDVAVKI-----LRIDLADESNLIRRFQREAQsATSLVHPNIVS---VYDVGEENDLhy 85
Cdd:COG3642   1 MDLIKQGAEAIIYLTD--FLGLPAVVKEripkrYRHPELDEKLRRERTRREAR-ILAKAREAGVPvpiVYDVDPDNGL-- 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16803860  86 IVMEHVDGMDLKQYIHENHPisyekavDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKItDFGIA 156
Cdd:COG3642  76 IVMEYIEGELLKDALEEARP-------DLLREVGRLVGKLHKAGIVHGDLTTSNIILSGGRIYFI-DFGLG 138
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
17-156 3.86e-10

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749  Cd Length: 199  Bit Score: 58.76  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    17 IGGGGMANVYLahDIILDRDVAVKI-----LRIDLADESNLIRRFQREAQsATSLVHPNIVS---VYDVGEENDLhyIVM 88
Cdd:TIGR03724   2 IAKGAEAIIYL--GDFLGRKAVIKErvpksYRHPELDERLRKERTRREAR-LLSRARKAGVNtpvIYDVDPDNKT--IVM 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16803860    89 EHVDGMDLKQYIHENHPisyekavDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKItDFGIA 156
Cdd:TIGR03724  77 EYIEGKPLKDVIEENGD-------ELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYLI-DFGLG 136
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
435-499 7.15e-10

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: 56.08  E-value: 7.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16803860   435 ITMDDYTGRSYTDTKALLEEQGFKnISSEEAYSSEIEKGLIISQTPTQGTEvVAKSTDVKFVVSK 499
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLK-VGTVEEYSDDVGEGTVISQSPPAGTK-VKKGSKVTLTVSK 63
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
362-647 7.19e-89

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


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 281.61  E-value: 7.19e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 362 KSPDEVAVPDVSGKTEDQAVALLQKEGFVIGkTAEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVSIGSKKITMDDYT 441
Cdd:COG2815  21 VSPDKVKVPNVAGLDEEDAKAELQKAGLEVG-VRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQYITVPDVV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 442 GRSYTDTKALLEEQGFKNISSE-EAYSSEIEKGLIISQTPTQGTEVVAKSTdVKFVVSKGAEPITLKDLRGYTKTAVEDY 520
Cdd:COG2815 100 GLTIEEAVAKLKAYGLNLSKITqEEVSDEVPAGTVISQSPSAGTEVKPGET-VKLTVSKGPETITVPDLVGMTYDEASSN 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 521 ASPLGLKVSSKEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVISAGPKEKQVKEVTKTFNIPYTPsDEENPQPQKiQIY 600
Cdd:COG2815 179 LKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGMFTVEAEPHP-REEGDTSQE-VIR 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 16803860 601 IQDKDHSMTSAYREMSITQNTSVEITFQIEEGSSAGYKIISDDKVID 647
Cdd:COG2815 257 DKDADVTASGTDSSVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVIS 303
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-264 6.84e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 253.22  E-value: 6.84e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860     11 YKILHAIGGGGMANVYLAHDIILDRDVAVKIlrIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVMEH 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV--IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860     91 VDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETsiTQTNSL 170
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG--EKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    171 LGSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKHLQADIPSAREQNPEIPQSLENIIIKATA 250
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 16803860    251 KDPFLRYQNAEEME 264
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
11-262 2.00e-70

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 230.98  E-value: 2.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    11 YKILHAIGGGGMANVYLAHDIILDRDVAVKILRIDLADESNLIRRFqREAQSATSLVHPNIVSVYDVGEENDLHYIVMEH 90
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTAR-REIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    91 VDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAmALSETSITQTNSL 170
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLA-KKLTKSSSSLTTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   171 LGSVHYLSPEQARGG-MATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKH---LQADIPSAREQNPEIPQSLENIII 246
Cdd:pfam00069 159 VGTPEYMAPEVLLGGnGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIrriLGPPLEFDEPKSDSGSEEAKDLIK 238
                         250
                  ....*....|....*.
gi 16803860   247 KATAKDPFLRYqNAEE 262
Cdd:pfam00069 239 KCLNKDPSKRP-TAEE 253
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-291 6.81e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 212.29  E-value: 6.81e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  11 YKILHAIGGGGMANVYLAHDIildRDVAVKILRIDLADESNLIRRFQREAQSATSLVHP-NIVSVYDVGEENDLHYIVME 89
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  90 HVDGMDLKQYIHENH---PISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDG-VVKITDFGIAMALSETSIT 165
Cdd:COG0515  79 YVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 166 Q-----TNSLLGSVHYLSPEQARG---GMATQKSDIYSLGIVLYELLTGKVPFDGESAVSI---AIKHLQADIPSAREQN 234
Cdd:COG0515 159 SsipalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSAtsqTLKIILELPTPSLASP 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16803860 235 ------PEIPQSLENIIIKATAKDPFLRYQNAEEMEKDLQTCLNKDRLNEPKYVFPTDDGDTK 291
Cdd:COG0515 239 lspsnpELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLR 301
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-287 2.22e-53

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 196.53  E-value: 2.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   10 RYKILHAIGGGGMANVYLAHDIILDRDVAVKILRIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVME 89
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   90 HVDGMDLKQYIH---ENHPISYEKA--------VDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMA 158
Cdd:PRK13184  83 YIEGYTLKSLLKsvwQKESLSKELAektsvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  159 -------LSETSITQTNSL----------LGSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIK 221
Cdd:PRK13184 163 kkleeedLLDIDVDERNICyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISYR 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16803860  222 HlqaDIPSAREQNP--EIPQSLENIIIKATAKDPFLRYQNAEEMEKDLQTCLNKDRLNEPKYVFPTDD 287
Cdd:PRK13184 243 D---VILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSPEWTVKATLMTKK 307
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-263 1.57e-44

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 170.80  E-value: 1.57e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860     37 VAVKILRIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGE-ENDLHYIVMEHVDGMDLKQYIHENHPISYEKAVDIM 115
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    116 LQIVSAVAIAHQHHIIHRDLKPQNILIDHDGV---VKITDFGIAMALS------ETSITQTNSLLGSVHYLSPEQARGGM 186
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLPgvrdadVATLTRTTEVLGTPTYCAPEQLRGEP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    187 ATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKHLQAD---IPSAREQNPeipqsLENIIIKATAKDPFLRYQNAEEM 263
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVdvsLPPWIAGHP-----LGQVLRKALNKDPRQRAASAPAL 240
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2-216 1.07e-26

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 111.01  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860    2 MIGKRLSDRYKILHA-IGGGGMANVYLAHDIILDRDVAVKILR-IDLADESNLIRRF----------QREAQSATSLVHP 69
Cdd:PTZ00024   1 NMSFSISERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKiIEISNDVTKDRQLvgmcgihfttLRELKIMNEIKHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   70 NIVSVYDVGEENDLHYIVMEHVDGmDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVK 149
Cdd:PTZ00024  81 NIMGLVDVYVEGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  150 ITDFGIA------MALSETSITQTNSL-------LGSVHYLSPEQARGGMA-TQKSDIYSLGIVLYELLTGKVPFDGESA 215
Cdd:PTZ00024 160 IADFGLArrygypPYSDTLSKDETMQRreemtskVVTLWYRAPELLMGAEKyHFAVDMWSVGCIFAELLTGKPLFPGENE 239

                 .
gi 16803860  216 V 216
Cdd:PTZ00024 240 I 240
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
17-210 5.16e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 109.14  E-value: 5.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   17 IGGGGMANVYLAHDIILDRDVAVKILRIDlaDESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVMEHVDGMDL 96
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIYGN--HEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   97 kqyihENHPISYEKAV-DIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETsITQTNSLLGSVH 175
Cdd:PLN00034 160 -----EGTHIADEQFLaDVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQT-MDPCNSSVGTIA 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16803860  176 YLSPEQ--------ARGGMAtqkSDIYSLGIVLYELLTGKVPF 210
Cdd:PLN00034 234 YMSPERintdlnhgAYDGYA---GDIWSLGVSILEFYLGRFPF 273
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
68-211 1.21e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 91.84  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860   68 HPNIVSVYDVGEENDLHYIVMEHVDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILID-HDG 146
Cdd:PHA03390  68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKD 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16803860  147 VVKITDFGIAmalsetSITQTNSLL-GSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFD 211
Cdd:PHA03390 148 RIYLCDYGLC------KIIGTPSCYdGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK 207
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
10-269 1.22e-127

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: 380.39  E-value: 1.22e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  10 RYKILHAIGGGGMANVYLAHDIILDRDVAVKILRIDLADESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVME 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  90 HVDGMDLKQYIHENHPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETSITQTNS 169
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 170 LLGSVHYLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGESAVSIAIKHLQADIPSAREQNPEIPQSLENIIIKAT 249
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250       260
                ....*....|....*....|
gi 16803860 250 AKDPFLRYQNAEEMEKDLQT 269
Cdd:cd14014 241 AKDPEERPQSAAELLAALRA 260
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
369-429 9.33e-19

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: 81.42  E-value: 9.33e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16803860 369 VPDVSGKTEDQAVALLQKEGFVIGKTAEKNSDEVDEGKVINTDPEAGEMKEKGTKINLFVS 429
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
436-498 2.63e-13

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: 66.01  E-value: 2.63e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16803860 436 TMDDYTGRSYTDTKALLEEQGFKNISSEEAYSSEIEKGLIISQTPTQGTEVVAKSTdVKFVVS 498
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGST-VTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
505-565 1.29e-12

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: 63.70  E-value: 1.29e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16803860 505 TLKDLRGYTKTAVEDYASPLGLKVSS-KEENSSTVEKGQVISQSPSAGTAMNSGDTIEIVIS 565
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVvTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
17-253 2.73e-61

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 [Multi-domain]  Cd Length: 245  Bit Score: 206.23  E-value: 2.73e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  17 IGGGGMANVYLAhdIILDRDVAVKILRIDLaDESNLIRRFQREAQSATSLVHPNIVSVYDVGEENDLHYIVMEHVDGMDL 96
Cdd:cd13999   1 IGSGSFGEVYKG--KWRGTDVAIKKLKVED-DNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860  97 KQYIHEN-HPISYEKAVDIMLQIVSAVAIAHQHHIIHRDLKPQNILIDHDGVVKITDFGIAMALSETSITQTnSLLGSVH 175
Cdd:cd13999  78 YDLLHKKkIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMT-GVVGTPR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16803860 176 YLSPEQARGGMATQKSDIYSLGIVLYELLTGKVPFDGES----AVSIAIKHLQADIPsareqnPEIPQSLENIIIKATAK 251
Cdd:cd13999 157 WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSpiqiAAAVVQKGLRPPIP------PDCPPELSKLIKRCWNE 230