NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|120401051|ref|YP_950880|]
View 

protein kinase [Mycobacterium vanbaalenii PYR-1]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
360-420 4.67e-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: 64.86  E-value: 4.67e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051 360 QVPDVRGQASADAIATLQNRGFSIRTQ-QKPDSEVPPDHVIDTDPGANTEVGAGDEITLNVS 420
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVtEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
495-555 1.47e-10

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: 57.92  E-value: 1.47e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051 495 VVPECVGQTVEVCQQILSASGFT-KSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVS 555
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
427-487 3.56e-09

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: 53.69  E-value: 3.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120401051 427 EVPDVSGLSYTEAVRRLTEAGFEKFRQTASTSLPEQKDRVLSTVPPANQTSAITNEITIVV 487
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTV 61
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
561-621 4.70e-07

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: 47.52  E-value: 4.70e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120401051 561 VMPDLRGQFWADAEPRLRALGWTGVLDKgaDVPNSGQRTNAVVTQSPSPGSGVNYGSRITL 621
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVT--EEYSDDVPKGTVISQSPAAGTKVKKGSTVTL 59
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-262 6.00e-55

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


:

Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 188.86  E-value: 6.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  10 RYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLraDLAR-DPSFYLRFRREAQNAAALNHPAIVAVYDTGEaetpTGPLP 88
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEI--DLSNmSEKEREDALNEVKILKKLNHPNIIKYYESFE----EKGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  89 YIVMEYVDGVTLRDIVHN----DGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALA 164
Cdd:cd08215   75 CIVMEYADGGDLSQKIKKqkkeGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 165 DAGnPVTQTaaVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPVP-PSQrhagI 243
Cdd:cd08215  155 STV-DLAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPiPSQ----Y 227
                        250
                 ....*....|....*....
gi 120401051 244 SPELDAVVLKALAKNPDNR 262
Cdd:cd08215  228 SSELRNLVSSLLQKDPEER 246
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-268 9.27e-79

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 252.45  E-value: 9.27e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051    11 YEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRadLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPtgplPYI 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK----LYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051    91 VMEYVDGVTLRDIVHNDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALADagNPV 170
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   171 TQTaaVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPVPPSQRHAGISPELDAV 250
Cdd:smart00220 153 LTT--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....*...
gi 120401051   251 VLKALAKNPDNRYqTAAE 268
Cdd:smart00220 231 IRKLLVKDPEKRL-TAEE 247
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
335-621 4.19e-65

Uncharacterized protein conserved in bacteria [Function unknown]


:

Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 217.67  E-value: 4.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 335 VAILAVLTVVVTIGINMFGGGTRDVQVPDVRGQASADAIATLQNRGFSIRTQQKPDSEVPPDHVIDTDPGANTEVGAGDE 414
Cdd:COG2815    2 LSLLVSLVVAGVLLATFFPVSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRERESDKVPEGKVIRTDPKAGTVVKQGSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 415 ITLNVSTGPEQREVPDVSGLSYTEAVRRLTEAGFEKFRQTASTSLPE-QKDRVLSTVPPANQTSAITNEITIVVGKGPAT 493
Cdd:COG2815   82 VTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKITQEEVSDEvPAGTVISQSPSAGTEVKPGETVKLTVSKGPET 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 494 AVVPECVGQTVEVCQQILSASGFTKSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVSRGnQFVMPDLRGQFWADA 573
Cdd:COG2815  162 ITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKG-AFVAPDLSGMFTVEA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 120401051 574 EPRLRALGWTG---VLDKGADVPNSGQRTNaVVTQSPSPGSGVNYGSRITL 621
Cdd:COG2815  241 EPHPREEGDTSqevIRDKDADVTASGTDSS-VNIQPPPGGTIVLKGSEITS 290
 
Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
360-420 4.67e-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: 64.86  E-value: 4.67e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051 360 QVPDVRGQASADAIATLQNRGFSIRTQ-QKPDSEVPPDHVIDTDPGANTEVGAGDEITLNVS 420
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVtEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
495-555 1.47e-10

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: 57.92  E-value: 1.47e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051 495 VVPECVGQTVEVCQQILSASGFT-KSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVS 555
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
427-487 3.56e-09

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: 53.69  E-value: 3.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120401051 427 EVPDVSGLSYTEAVRRLTEAGFEKFRQTASTSLPEQKDRVLSTVPPANQTSAITNEITIVV 487
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTV 61
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
561-621 4.70e-07

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: 47.52  E-value: 4.70e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120401051 561 VMPDLRGQFWADAEPRLRALGWTGVLDKgaDVPNSGQRTNAVVTQSPSPGSGVNYGSRITL 621
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVT--EEYSDDVPKGTVISQSPAAGTKVKKGSTVTL 59
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-262 6.00e-55

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


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 188.86  E-value: 6.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  10 RYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLraDLAR-DPSFYLRFRREAQNAAALNHPAIVAVYDTGEaetpTGPLP 88
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEI--DLSNmSEKEREDALNEVKILKKLNHPNIIKYYESFE----EKGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  89 YIVMEYVDGVTLRDIVHN----DGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALA 164
Cdd:cd08215   75 CIVMEYADGGDLSQKIKKqkkeGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 165 DAGnPVTQTaaVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPVP-PSQrhagI 243
Cdd:cd08215  155 STV-DLAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPiPSQ----Y 227
                        250
                 ....*....|....*....
gi 120401051 244 SPELDAVVLKALAKNPDNR 262
Cdd:cd08215  228 SSELRNLVSSLLQKDPEER 246
PASTA smart00740
PASTA domain;
355-421 1.31e-13

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 66.56  E-value: 1.31e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 120401051   355 GTRDVQVPDVRGQASADAIATLQNRGFSIRTQQKPDSEVPPDHVIDTDPGANTEVGAGDEITLNVST 421
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
359-421 5.24e-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: 64.94  E-value: 5.24e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 120401051  359 VQVPDVRGQASADAIATLQNRGFSIRTQQKPDSEVPPDHVIDTDPGANTEVGAGDEITLNVST 421
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
14-161 5.53e-13

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 67.62  E-value: 5.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  14 GEILGFGGMSEVHLARDLRLHrdVAIKVLRADLARDPSF-----YLRFRREAQN-----AAALNHPAIVAVyDTGEAEtp 83
Cdd:PRK14879   1 MKLIKRGAEAEIYLGDFLGIK--AVIKWRIPKRYRHPELderirRERTRREARImsrarKAGVNVPAVYFV-DPENFI-- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 120401051  84 tgplpyIVMEYVDGVTLRDIVhNDGPMapqRAIEVIADACQALNFSHQHGIIHRDVKPANIMISkTGAVKVMDFGIAR 161
Cdd:PRK14879  76 ------IVMEYIEGEPLKDLI-NSNGM---EELELSREIGRLVGKLHSAGIIHGDLTTSNMILS-GGKIYLIDFGLAE 142
PASTA smart00740
PASTA domain;
422-489 6.67e-11

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 58.86  E-value: 6.67e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 120401051   422 GPEQREVPDVSGLSYTEAVRRLTEAGFeKFRQTASTSLPEQKDRVLSTVPPANQTSAITNEITIVVGK 489
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGL-KVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
16-161 2.22e-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: 234331  Cd Length: 199  Bit Score: 59.54  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   16 ILGFGGMSEVHLARdlRLHRDVAIKVLRADLARDPSF-----YLRFRREAQNaaalnhpaIVAVYDTGeaeTPTgPLPY- 89
Cdd:TIGR03724   1 LIAKGAEAIIYLGD--FLGLKAVIKERVPKSYRHPELderirRERTRNEARL--------LSRARKAG---VNT-PVVYd 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120401051   90 -------IVMEYVDGVTLRDIVhNDGPMapqraiEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVkVMDFGIAR 161
Cdd:TIGR03724  67 vdpdnktIVMEYIEGKPLKDVI-EEGND------ELLREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKLY-LIDFGLGK 137
PASTA smart00740
PASTA domain;
557-621 3.91e-09

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 53.85  E-value: 3.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120401051   557 GNQFVMPDLRGQFWADAEPRLRALGWTGVLDkgaDVPNSGQRTNAVVTQSPSPGSGVNYGSRITL 621
Cdd:smart00740   2 PEKVEVPDVIGKSKEEAKKLLKALGLKVEVV---EEYSSDGEEGTVISQSPAAGTTVKPGSKVTL 63
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
25-165 3.06e-08

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 55.01  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  25 VHLARdLRLHRDVAIKVLR--------ADLA-----------RDP-SFYLR-----------------FRREAQNAAAL- 66
Cdd:COG0661  141 VHRAV-LKSGEEVAVKVQRpgirerieADLKllrrlarlikrLPPgGRRLDlvevvdefekrlreeldYRREAANAERFr 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  67 ----NHPAIV--AVYDtgEAETPTgplpYIVMEYVDGVTLRDI-VHNDGPMAPQRAIEVIADAC--QALNfshqHGIIHR 137
Cdd:COG0661  220 enfkDDPDVYvpKVYW--EYTTRR----VLTMEWIDGIKISDIaALKSAGIDRKELAELLVRAFlrQLLR----DGFFHA 289
                        170       180
                 ....*....|....*....|....*...
gi 120401051 138 DVKPANIMISKTGAVKVMDFGIARALAD 165
Cdd:COG0661  290 DPHPGNILVRSDGRIVLLDFGIVGRLDP 317
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
560-625 7.29e-08

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: 49.92  E-value: 7.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120401051  560 FVMPDLRGQFWADAEPRLRALGWTGVLDKgadVPNSGQRTNAVVTQSPSPGSGVNYGSRITLNFAS 625
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVE---EYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
427-489 7.43e-08

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: 49.92  E-value: 7.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 120401051  427 EVPDVSGLSYTEAVRRLTEAGFeKFRQTASTSLPEQKDRVLSTVPPANQTSAITNEITIVVGK 489
Cdd:pfam03793   2 TVPDVVGLSLEEAKKLLEALGL-KVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
495-556 1.12e-07

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: 49.54  E-value: 1.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051  495 VVPECVGQTVEVCQQILSASGFTKSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVSR 556
Cdd:pfam03793   2 TVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
118-206 1.54e-07

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 52.26  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 118 VIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALADAGNPV----TQTAAVIGTAQYLSPEQARGVKV 193
Cdd:PHA02882 131 IMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIIDYGIASHFIIHGKHIeyskEQKDLHRGTLYYAGLDAHNGACV 210
                         90
                 ....*....|....
gi 120401051 194 DARSDVYSLG-CVL 206
Cdd:PHA02882 211 TRRGDLESLGyCML 224
PASTA smart00740
PASTA domain;
490-555 4.33e-07

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 47.69  E-value: 4.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120401051   490 GPATAVVPECVGQTVEVCQQILSASGFTKSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVS 555
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVS 66
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
98-215 2.37e-05

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 43.93  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051    98 VTLRDIV-HNDGPMAPQRAIEVIADACQALNFSHqhgiihRDVKPANIMISKTGAVKVmdfgiaraladAGNPVTQTAAV 176
Cdd:smart00750   1 VSLADILeVRGRPLNEEEIWAVCLQCLGALRELH------RQAKSGNILLTWDGLLKL-----------DGSVAFKTPEQ 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 120401051   177 -IGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPP 215
Cdd:smart00750  64 sRPDPYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELP 103
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-268 9.27e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 252.45  E-value: 9.27e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051    11 YEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRadLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPtgplPYI 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK----LYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051    91 VMEYVDGVTLRDIVHNDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALADagNPV 170
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   171 TQTaaVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPVPPSQRHAGISPELDAV 250
Cdd:smart00220 153 LTT--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....*...
gi 120401051   251 VLKALAKNPDNRYqTAAE 268
Cdd:smart00220 231 IRKLLVKDPEKRL-TAEE 247
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
335-621 4.19e-65

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 217.67  E-value: 4.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 335 VAILAVLTVVVTIGINMFGGGTRDVQVPDVRGQASADAIATLQNRGFSIRTQQKPDSEVPPDHVIDTDPGANTEVGAGDE 414
Cdd:COG2815    2 LSLLVSLVVAGVLLATFFPVSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRERESDKVPEGKVIRTDPKAGTVVKQGSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 415 ITLNVSTGPEQREVPDVSGLSYTEAVRRLTEAGFEKFRQTASTSLPE-QKDRVLSTVPPANQTSAITNEITIVVGKGPAT 493
Cdd:COG2815   82 VTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKITQEEVSDEvPAGTVISQSPSAGTEVKPGETVKLTVSKGPET 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 494 AVVPECVGQTVEVCQQILSASGFTKSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVSRGnQFVMPDLRGQFWADA 573
Cdd:COG2815  162 ITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKG-AFVAPDLSGMFTVEA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 120401051 574 EPRLRALGWTG---VLDKGADVPNSGQRTNaVVTQSPSPGSGVNYGSRITL 621
Cdd:COG2815  241 EPHPREEGDTSqevIRDKDADVTASGTDSS-VNIQPPPGGTIVLKGSEITS 290
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
11-275 5.71e-59

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: 203.82  E-value: 5.71e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  11 YEVGEILGFGGMSEVHLARDlrlHRDVAIKVLRADLARDPSFYLRFRREAQNAAALNHP-AIVAVYDTGEaetpTGPLPY 89
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQ----DEGSLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  90 IVMEYVDGVTLRDIVHNDG---PMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTG-AVKVMDFGIARALAD 165
Cdd:COG0515   75 LVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 166 AGNPVTQ---TAAVIGTAQYLSPEQARG---VKVDARSDVYSLGCVLYEVLTGEPPF---VGDSPVAVAYQHVREDPVPP 236
Cdd:COG0515  155 PGSTSSIpalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILELPTPS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 120401051 237 SQRH------AGISPELDAVVLKALAKNPDNRYQTAAEMRTDLVR 275
Cdd:COG0515  235 LASPlspsnpELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA 279
Pkinase pfam00069
Protein kinase domain;
11-268 4.06e-58

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 197.47  E-value: 4.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   11 YEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRADLaRDPSFYLRFRREAQNAAALNHPAIVAVYDTGEaetpTGPLPYI 90
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRS-EKSKKDQTARREIRILRRLSHPNIVRLIDAFE----DKDHLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   91 VMEYVDGVTLRDIVHNDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALaDAGNPV 170
Cdd:pfam00069  76 VMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKL-TKSSSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  171 TQTaaVIGTAQYLSPEQARGVK-VDARSDVYSLGCVLYEVLTGEPPFVGDSPVA--VAYQHVREDPVP-PSQRHAGISPE 246
Cdd:pfam00069 155 LTT--FVGTPEYMAPEVLLGGNgYGPKVDVWSLGVILYELLTGKPPFSGESILDqlQLIRRILGPPLEfDEPKSDSGSEE 232
                         250       260
                  ....*....|....*....|..
gi 120401051  247 LDAVVLKALAKNPDNRYqTAAE 268
Cdd:pfam00069 233 AKDLIKKCLNKDPSKRP-TAEE 253
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-273 2.40e-46

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 175.34  E-value: 2.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  10 RYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYdTGEAEtptGPLPY 89
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVY-SICSD---GDPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  90 IVMEYVDGVTLRDIVHN-------DGPMAPQRAI----EVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFG 158
Cdd:PRK13184  79 YTMPYIEGYTLKSLLKSvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 159 IARALA---------DAGNP------VTQTAAVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVA 223
Cdd:PRK13184 159 AAIFKKleeedlldiDVDERnicyssMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRK 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 120401051 224 VAYQHVREDP--VPPsqrHAGISPELDAVVLKALAKNPDNRYQTAAEMRTDL 273
Cdd:PRK13184 239 ISYRDVILSPieVAP---YREIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-277 8.97e-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: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 168.10  E-value: 8.97e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051    37 VAIKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPtgpLPYIVMEYVDGVTLRDIVHNDGPMAPQRAI 116
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPG---LLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   117 EVIADACQALNFSHQHGIIHRDVKPANIMISKTGA---VKVMDFGIARALADAGNP----VTQTAAVIGTAQYLSPEQAR 189
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLPGVRDAdvatLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   190 GVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPV--PPS-QRHagispELDAVVLKALAKNPDNRYQTA 266
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVslPPWiAGH-----PLGQVLRKALNKDPRQRAASA 237
                          250
                   ....*....|.
gi 120401051   267 AEMRTDLVRVH 277
Cdd:TIGR03903  238 PALAERFRALE 248
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
7-221 3.17e-23

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 100.28  E-value: 3.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   7 LSDrYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRADLArdpsfyLRFRR------EAQNAAALNHPAIVAVYDTGEA 80
Cdd:PTZ00263  17 LSD-FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREI------LKMKQvqhvaqEKSILMELSHPFIVNMMCSFQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  81 ETPTgplpYIVMEYVDGVTLRDIVHNDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIA 160
Cdd:PTZ00263  90 ENRV----YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 120401051 161 RALADagnpvtQTAAVIGTAQYLSPE--QARGvkVDARSDVYSLGCVLYEVLTGEPPFVGDSP 221
Cdd:PTZ00263 166 KKVPD------RTFTLCGTPEYLAPEviQSKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDTP 220
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
9-258 1.13e-17

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 82.94  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051   9 DRYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRADLARD--PSFYLRfrrEAQNAAALNHPAIVAVYDTGEAETPTgp 86
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEgvPSTAIR---EISLLKEMQHGNIVRLQDVVHSEKRL-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  87 lpYIVMEYVDgVTLRDIVHNDGPMAP-QRAIEV-IADACQALNFSHQHGIIHRDVKPANIMISK-TGAVKVMDFGIARAL 163
Cdd:PLN00009  77 --YLVFEYLD-LDLKKHMDSSPDFAKnPRLIKTyLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 164 adaGNPV-TQTAAVIgTAQYLSPEQARGVK-VDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPVPPSQRHA 241
Cdd:PLN00009 154 ---GIPVrTFTHEVV-TLWYRAPEILLGSRhYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWP 229
                        250
                 ....*....|....*....
gi 120401051 242 GIS--PELDAVVLKALAKN 258
Cdd:PLN00009 230 GVTslPDYKSAFPKWPPKD 248
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
89-219 1.16e-15

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 76.43  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  89 YIVMEYVDGVTLRDIVHNDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMIS-KTGAVKVMDFGIARAladAG 167
Cdd:PHA03390  85 VLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKI---IG 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 120401051 168 NPVTQTaaviGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGD 219
Cdd:PHA03390 162 TPSCYD----GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKED 209
spoVD_pbp TIGR02214
stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the ...
561-625 2.33e-03

stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the cell division protein FtsI, a penicillin binding protein. This subfamily is restricted to Bacillus subtilis and related Gram-positive species with known or suspected endospore formation capability. In these species, the functional equivalent of FtsI is desginated PBP-2B, a paralog of spoVD [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination].


Pssm-ID: 131269 [Multi-domain]  Cd Length: 636  Bit Score: 39.41  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120401051  561 VMPDLRGQFWADAEPRLRALGWtgvldkGADVPNSGQRtnaVVTQSPSPGSGVNYGSRITLNFAS 625
Cdd:TIGR02214 581 AVPNLRGMKVDDAEKTLLHLGL------DVATEGFGTR---VVNQTPIPGEKVKEGTKVVLYLGE 636
 
Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
360-420 4.67e-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: 64.86  E-value: 4.67e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051 360 QVPDVRGQASADAIATLQNRGFSIRTQ-QKPDSEVPPDHVIDTDPGANTEVGAGDEITLNVS 420
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVtEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
495-555 1.47e-10

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: 57.92  E-value: 1.47e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120401051 495 VVPECVGQTVEVCQQILSASGFT-KSVPVEVDSTVAAGQVVGLEPAAGQTVPQDTVIQIQVS 555
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
427-487 3.56e-09

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: 53.69  E-value: 3.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120401051 427 EVPDVSGLSYTEAVRRLTEAGFEKFRQTASTSLPEQKDRVLSTVPPANQTSAITNEITIVV 487
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTV 61
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
561-621 4.70e-07

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: 47.52  E-value: 4.70e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120401051 561 VMPDLRGQFWADAEPRLRALGWTGVLDKgaDVPNSGQRTNAVVTQSPSPGSGVNYGSRITL 621
Cdd:cd06577    1 TVPDVVGMTLDEAKAALEAAGLKVGVVT--EEYSDDVPKGTVISQSPAAGTKVKKGSTVTL 59
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-262 6.00e-55

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


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 188.86  E-value: 6.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  10 RYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLraDLAR-DPSFYLRFRREAQNAAALNHPAIVAVYDTGEaetpTGPLP 88
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEI--DLSNmSEKEREDALNEVKILKKLNHPNIIKYYESFE----EKGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  89 YIVMEYVDGVTLRDIVHN----DGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALA 164
Cdd:cd08215   75 CIVMEYADGGDLSQKIKKqkkeGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 165 DAGnPVTQTaaVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVGDSPVAVAYQHVREDPVP-PSQrhagI 243
Cdd:cd08215  155 STV-DLAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPiPSQ----Y 227
                        250
                 ....*....|....*....
gi 120401051 244 SPELDAVVLKALAKNPDNR 262
Cdd:cd08215  228 SSELRNLVSSLLQKDPEER 246
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
17-208 1.01e-49

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 172.81  E-value: 1.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  17 LGFGGMSEVHLARDLRLHRDVAIKVLRADLarDPSFYLRFRREAQNAAALNHPAIVAVYDTGEaetpTGPLPYIVMEYVD 96
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIKKED--SSSLLEELLREIEILKKLNHPNIVKLYGVFE----DENHLYLVMEYCE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  97 GVTLRDIVH-NDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISK-TGAVKVMDFGIARALADAGNPVTQta 174
Cdd:cd00180   75 GGSLKDLLKeNEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSdNGKVKLADFGLSKLLTSDKSLLKT-- 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 120401051 175 aVIGTAQYLSPEQARG-VKVDARSDVYSLGCVLYE 208
Cdd:cd00180  153 -IVGTPAYMAPEVLLGkGYYSEKSDIWSLGVILYE 186
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
10-268 1.77e-47

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK 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. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 168.12  E-value: 1.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  10 RYEVGEILGFGGMSEVHLARDLRLHRDVAIKVLRadLARDPSFYLR-FRREAQNAAALNHPAIVAVYDTGEAETPTGPlp 88
Cdd:cd06606    1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSVE--LSGDSEEELEaLEREIRILSSLQHPNIVRYYGSERDEEKNTL-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051  89 YIVMEYVDGVTLRDIVHNDGPMAPQRAIEVIADACQALNFSHQHGIIHRDVKPANIMISKTGAVKVMDFGIARALADAGN 168
Cdd:cd06606   77 NIFLEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLGDIET 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120401051 169 PvTQTAAVIGTAQYLSPEQARGVKVDARSDVYSLGCVLYEVLTGEPPFVG-DSPVAVAYQHVREDPVPPSqrHAGISPEL 247
Cdd:cd06606  157 G-EGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSElGNPMAALYKIGSSGEPPEI--PE