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Conserved domains on  [gi|47778234|ref|YP_020640|]
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serine/threonine protein kinase [Bacillus anthracis str. 'Ames Ancestor']

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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 1.09e-119

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: 359.98  E-value: 1.09e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVME 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  90 YVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIATATSATTITHTNS 169
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 170 VLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKAT 249
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250       260
                ....*....|....*....|
gi 47778234 250 AKDPFHRYQSANAMKRDIET 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 ...
370-431 1.30e-15

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: 72.56  E-value: 1.30e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47778234 370 KVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVETGDVIKTDPVAGRVVKENSKITIYQS 431
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
508-565 1.13e-11

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: 61.01  E-value: 1.13e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47778234 508 DFSRWTENSVTGYLNERKLTP-DIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIIS 565
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKVgVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
438-498 1.79e-03

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: 37.12  E-value: 1.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47778234 438 KMIDFTGKDLESIRTELEE---KYKQVTVYYiEDDRPKGAIVEQIPTSDQMvVEAEQELKIWVS 498
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAaglKVGVVTEEY-SDDVPKGTVISQSPAAGTK-VKKGSTVTLTVS 62
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-264 7.96e-71

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 232.04  E-value: 7.96e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234     11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234     91 VPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGiaTATSATTITHTNSV 170
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFG--LARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    171 LGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKATA 250
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 47778234    251 KDPFHRYQSANAMK 264
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
341-647 1.24e-44

Uncharacterized protein conserved in bacteria [Function unknown]


:

Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 161.43  E-value: 1.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 341 ILITTFLLLAIGITLAlTVIPgfFIPKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNIvYTDDVETGDVIKTDPVAGRVV 420
Cdd:COG2815   1 LLSLLVSLVVAGVLLA-TFFP--VSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRER-ESDKVPEGKVIRTDPKAGTVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 421 KENSKITIYQSGGKKKSKMIDFTGKDLESIRTELEEKYK---QVTVYYIEDDRPKGAIVEQIPTSDQMVVEAEQeLKIWV 497
Cdd:COG2815  77 KQGSKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLnlsKITQEEVSDEVPAGTVISQSPSAGTEVKPGET-VKLTV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 498 SKGPYQIRPGDFSRWTENSVTGYLNERKLTPDIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIISEGPKPKVTKTVK 577
Cdd:COG2815 156 SKGPETITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGM 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 578 VdNISIPYESSIIGEKKPQTIEIykEDMQQKMDRPIETRTISESATISLEFVIQEDTKGRYKIVRDGVTI 647
Cdd:COG2815 236 F-TVEAEPHPREEGDTSQEVIRD--KDADVTASGTDSSVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVI 302
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
10-269 1.09e-119

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: 359.98  E-value: 1.09e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVME 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  90 YVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIATATSATTITHTNS 169
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 170 VLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKAT 249
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250       260
                ....*....|....*....|
gi 47778234 250 AKDPFHRYQSANAMKRDIET 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 ...
370-431 1.30e-15

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: 72.56  E-value: 1.30e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47778234 370 KVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVETGDVIKTDPVAGRVVKENSKITIYQS 431
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
508-565 1.13e-11

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: 61.01  E-value: 1.13e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47778234 508 DFSRWTENSVTGYLNERKLTP-DIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIIS 565
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKVgVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
438-498 1.79e-03

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: 37.12  E-value: 1.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47778234 438 KMIDFTGKDLESIRTELEE---KYKQVTVYYiEDDRPKGAIVEQIPTSDQMvVEAEQELKIWVS 498
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAaglKVGVVTEEY-SDDVPKGTVISQSPAAGTK-VKKGSTVTLTVS 62
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
508-566 4.20e-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: 65.33  E-value: 4.20e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 47778234   508 DFSRWTENSVTGYLNERKLTPDIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIISE 566
Cdd:pfam03793   5 DVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
369-432 1.59e-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: 1.59e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47778234   369 VKVPDVAGMKYTTAVNTLVEKGFEVTEPNiVYTDDVETGDVIKTDPVAGRVVKENSKITIYQSG 432
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVE-EYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
366-429 2.88e-11

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 60.01  E-value: 2.88e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47778234    366 PKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNiVYTDDVETGDVIKTDPVAGRVVKENSKITIY 429
Cdd:smart00740   2 PEKVEVPDVIGKSKEEAKKLLKALGLKVEVVE-EYSSDGEEGTVISQSPAAGTTVKPGSKVTLT 64
PASTA smart00740
PASTA domain;
508-565 2.63e-10

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 57.32  E-value: 2.63e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 47778234    508 DFSRWTENSVTGYLNERKLTPDIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIIS 565
Cdd:smart00740   9 DVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVS 66
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
438-499 1.79e-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: 42.99  E-value: 1.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47778234   438 KMIDFTGKDLESIRTELEEK-YKQVTVYYIEDDRPKGAIVEQIPTSDQMvVEAEQELKIWVSK 499
Cdd:pfam03793   2 TVPDVVGLSLEEAKKLLEALgLKVGTVEEYSDDVGEGTVISQSPPAGTK-VKKGSKVTLTVSK 63
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-264 7.96e-71

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 232.04  E-value: 7.96e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234     11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234     91 VPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGiaTATSATTITHTNSV 170
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFG--LARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    171 LGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKATA 250
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 47778234    251 KDPFHRYQSANAMK 264
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
341-647 1.24e-44

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 161.43  E-value: 1.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 341 ILITTFLLLAIGITLAlTVIPgfFIPKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNIvYTDDVETGDVIKTDPVAGRVV 420
Cdd:COG2815   1 LLSLLVSLVVAGVLLA-TFFP--VSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRER-ESDKVPEGKVIRTDPKAGTVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 421 KENSKITIYQSGGKKKSKMIDFTGKDLESIRTELEEKYK---QVTVYYIEDDRPKGAIVEQIPTSDQMVVEAEQeLKIWV 497
Cdd:COG2815  77 KQGSKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLnlsKITQEEVSDEVPAGTVISQSPSAGTEVKPGET-VKLTV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 498 SKGPYQIRPGDFSRWTENSVTGYLNERKLTPDIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIISEGPKPKVTKTVK 577
Cdd:COG2815 156 SKGPETITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGM 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 578 VdNISIPYESSIIGEKKPQTIEIykEDMQQKMDRPIETRTISESATISLEFVIQEDTKGRYKIVRDGVTI 647
Cdd:COG2815 236 F-TVEAEPHPREEGDTSQEVIRD--KDADVTASGTDSSVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVI 302
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
11-353 1.84e-57

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: 200.35  E-value: 1.84e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  11 YKLLKMIGGGGMANVYLAHDDilgRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHP-NIVNMYDVGEEDGIYYLVME 89
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  90 YVPGQTLKQYI---IERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADG-VIKVTDFG-----IATATS 160
Cdd:COG0515  79 YVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGlakllPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 161 ATTITHTNSVLGSVHYLSPEQARGGI---ANKQSDIYSLGIVMFELLTGRQPFSGES---AVAIALKHLQSE------IP 228
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKnssATSQTLKIILELptpslaSP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 229 SPKRWNENIPQSVENIILKATAKDPFHRYQSANAMKRDIETALYPERINEQPFYIPEDMEATKAIPIIQQEQLFENVTDE 308
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNSL 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 47778234 309 TIVLKGSKVDEQIRKEETDLSKKKKRSNKWLKILITTFLLLAIGI 353
Cdd:COG0515 319 AISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSL 363
Pkinase pfam00069
Protein kinase domain;
11-264 2.05e-57

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 195.93  E-value: 2.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDySNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    91 VPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGiATATSATTITHTNSV 170
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFG-LAKKLTKSSSSLTTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   171 LGSVHYLSPEQARGGI-ANKQSDIYSLGIVMFELLTGRQPFSGESAV---AIALKHLQSEIPSPKRWNENIPQSVENIIL 246
Cdd:pfam00069 159 VGTPEYMAPEVLLGGNgYGPKVDVWSLGVILYELLTGKPPFSGESILdqlQLIRRILGPPLEFDEPKSDSGSEEAKDLIK 238
                         250
                  ....*....|....*...
gi 47778234   247 KATAKDPFHRYQSANAMK 264
Cdd:pfam00069 239 KCLNKDPSKRPTAEEILQ 256
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-271 1.61e-45

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 173.03  E-value: 1.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDV-GEEDGIYYlVM 88
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSIcSDGDPVYY-TM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   89 EYVPGQTLKQY---IIERGMLP--------IGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIAT 157
Cdd:PRK13184  82 PYIEGYTLKSLlksVWQKESLSkelaektsVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  158 ATSATTITHTNS-----------------VLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIAL 220
Cdd:PRK13184 162 FKKLEEEDLLDIdvdernicyssmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISY 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 47778234  221 KHlqsEIPSPKRW--NENIPQSVENIILKATAKDPFHRYQSANAMKRDIETAL 271
Cdd:PRK13184 242 RD---VILSPIEVapYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHL 291
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
34-263 1.22e-42

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 165.02  E-value: 1.22e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234     34 GRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGE-EDGIYYLVMEYVPGQTLKQYIIERGMLPIGEAL 112
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    113 DIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGV---IKVTDFGI------ATATSATTITHTNSVLGSVHYLSPEQAR 183
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIgtllpgVRDADVATLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    184 GGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLqseipSPKrwNENIPQSVE-----NIILKATAKDPFHRYQ 258
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQL-----SPV--DVSLPPWIAghplgQVLRKALNKDPRQRAA 235

                   ....*
gi 47778234    259 SANAM 263
Cdd:TIGR03903  236 SAPAL 240
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
6-235 6.85e-25

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 105.28  E-value: 6.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234    6 RLNDrYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRldysnNEEFIK-----RFHREAQSVTTLSHPNIVNMYDVGEE 80
Cdd:PTZ00263  16 KLSD-FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK-----KREILKmkqvqHVAQEKSILMELSHPFIVNMMCSFQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   81 DGIYYLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIATATS 160
Cdd:PTZ00263  90 ENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47778234  161 ATTIthtnSVLGSVHYLSPE--QARGgiANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPkRWNE 235
Cdd:PTZ00263 170 DRTF----TLCGTPEYLAPEviQSKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP-NWFD 239
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
17-210 3.00e-23

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 100.67  E-value: 3.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   17 IGGGGMANVYLAHDDILGRDVAVKILrldYSNNEEFIKR-FHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQT 95
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVI---YGNHEDTVRRqICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   96 LK-QYIIERGMLPigealDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGiATATSATTITHTNSVLGSV 174
Cdd:PLN00034 159 LEgTHIADEQFLA-----DVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFG-VSRILAQTMDPCNSSVGTI 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 47778234  175 HYLSPEQA-----RGGIANKQSDIYSLGIVMFELLTGRQPF 210
Cdd:PLN00034 233 AYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPF 273
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
68-236 4.92e-14

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 71.43  E-value: 4.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234   68 HPNIVNMYDVGEEDGIYYLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMA--HAHHfeIVHRDIKPHNILI-RA 144
Cdd:PHA03390  68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNdlHKHN--IIHNDIKLENVLYdRA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  145 DGVIKVTDFGIATATSATtithtnSVL-GSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESA----VAIA 219
Cdd:PHA03390 146 KDRIYLCDYGLCKIIGTP------SCYdGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDeeldLESL 219
                        170
                 ....*....|....*..
gi 47778234  220 LKHLQSEIPSPKRWNEN 236
Cdd:PHA03390 220 LKRQQKKLPFIKNVSKN 236
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
10-269 1.09e-119

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: 359.98  E-value: 1.09e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVME 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  90 YVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIATATSATTITHTNS 169
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 170 VLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKAT 249
Cdd:cd14014 161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRAL 240
                       250       260
                ....*....|....*....|
gi 47778234 250 AKDPFHRYQSANAMKRDIET 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 ...
370-431 1.30e-15

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: 72.56  E-value: 1.30e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47778234 370 KVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVETGDVIKTDPVAGRVVKENSKITIYQS 431
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
508-565 1.13e-11

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: 61.01  E-value: 1.13e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47778234 508 DFSRWTENSVTGYLNERKLTP-DIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIIS 565
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKVgVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
438-498 1.79e-03

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: 37.12  E-value: 1.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47778234 438 KMIDFTGKDLESIRTELEE---KYKQVTVYYiEDDRPKGAIVEQIPTSDQMvVEAEQELKIWVS 498
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAaglKVGVVTEEY-SDDVPKGTVISQSPAAGTK-VKKGSTVTLTVS 62
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
17-203 1.37e-52

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: 180.93  E-value: 1.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  17 IGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEfiKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQTL 96
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLL--EELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  97 KQYIIER-GMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGI-ATATSATTITHTNSVLGSV 174
Cdd:cd00180  79 KDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLaKDLDSDDSLLKTTGGTTPP 158
                       170       180
                ....*....|....*....|....*....
gi 47778234 175 HYLSPEQARGGIANKQSDIYSLGIVMFEL 203
Cdd:cd00180 159 YYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
10-264 7.72e-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: 177.67  E-value: 7.72e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDySNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVME 89
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKK-KLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  90 YVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILI---RADGVIKVTDFGiaTATSATTITH 166
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFG--LAKIFEEGEK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 167 TNSVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIIL 246
Cdd:cd05117 158 LKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIK 237
                       250
                ....*....|....*...
gi 47778234 247 KATAKDPFHRYQSANAMK 264
Cdd:cd05117 238 RLLVVDPKKRLTAAEALN 255
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
10-257 1.44e-50

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: 176.55  E-value: 1.44e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFiKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVME 89
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIE-EKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234  90 YVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGiaTATSATTITHTNS 169
Cdd:cd14003  80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG--LSNEFRGGSLLKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47778234 170 VLGSVHYLSPEQ-ARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRwnenIPQSVENIILKA 248
Cdd:cd14003 158 FCGTPAYAAPEVlLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSH----LSPDARDLIRRM 233

                ....*....
gi 47778234 249 TAKDPFHRY 257
Cdd:cd14003 234 LVVDPSKRI 242
STKc_MAP3K-like