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Conserved domains on  [gi|75910912|ref|YP_325208|]
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serine/threonine protein kinase and signal transduction histidine kinase [Anabaena variabilis ATCC 29413]

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-285 8.17e-66

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: 225.93  E-value: 8.17e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   11 GYRILELAHSGANTNIYRATKVDGNTPTILKVLIDNYFSLEAIV-RFKHEYSISANLDHPNIVKVISLETHHKRLVIVFE 89
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFReRFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   90 DFGGISLKHYLYNHQP-SLQLTLQVAIAITRALVYIHDNKIIHKDIKPGNIIIKNLGtrlqqtpevlsnlIIKLTDFSIA 168
Cdd:cd14014   81 YVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG-------------RVKLTDFGIA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  169 SRLKKETPQLINPNQleGTLAYMSPEQtgRMNRNLDYRSDFYSLGITLYEMLTGQLPFNSSEPLELVHAHIAKEPTPIQQ 248
Cdd:cd14014  148 RALGDSGLTQTGSVL--GTPAYMAPEQ--ARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSP 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 75910912  249 LAANVPNAVVGIVHKLMAKNAEDRYYSAQGLLVDLEQ 285
Cdd:cd14014  224 LNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
1688-1803 4.30e-22

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


:

Pssm-ID: 238030  Cd Length: 103  Bit Score: 94.25  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1688 INQVFLHLLTNSIDAllerknkcksyhgqeiSFSPTIWIS-SIVDDTKQAVIRVTDNGIGIDGNIISKIFDPF--FTTKP 1764
Cdd:cd00075    1 LQQVLLNLLSNAIKH----------------TPEGGGRITiSVERDGDHLEIRVEDNGPGIPEEDLERIFERFsdGSRSR 64
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 75910912 1765 VGKGTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKL 1803
Cdd:cd00075   65 KGGGTGLGLSIVKKLVELHGGRIEVESEPGGGTTFTITL 103
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
315-503 9.28e-38

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


:

Pssm-ID: 257559  Cd Length: 156  Bit Score: 141.45  E-value: 9.28e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    315 KLYGRETQVEQLLLSFARVSRGNSELILVSGYSGIGKTSVINEVNKPITQVKGYFISGKFDQFkrdiPYLSLVQAFSSLM 394
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKCDEL----PYAALRQLLRELL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    395 RQLLTESterlemwrsnilqavgsngkviidvIPEVELIigkqPEVSQLSPHESQNRFNQIFQSFIQVFCCCGHPLVIFL 474
Cdd:pfam13191   77 RQLLDEL-------------------------LPELELL----PPVPGLPPDDLRNRLEDLLRRLLRRLAARERPLVLVL 127
                          170       180
                   ....*....|....*....|....*....
gi 75910912    475 DDLQWADSATLNLMESLICDQTIKYLLII 503
Cdd:pfam13191  128 DDLQWADEASLALLLALARLLERLPLLLV 156
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
1344-1510 7.71e-19

FOG: GAF domain [Signal transduction mechanisms]


:

Pssm-ID: 225113  Cd Length: 175  Bit Score: 86.95  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1344 VVKASQALSSEIVLEKLLEKLMFLAKENAGAQkVFFIAKKDEKLVIEGSLMEEGIIKTLQAI--PITNSQALPASVINYV 1421
Cdd:COG2203    6 LNELAAKIAQDLDLEEILQAALELLAELLGAD-RGLIYLLDEDGLLDGALVAEAAEAGLEQLidELFGLVILPACLIGIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1422 KRTQAPLVLDDVTHAEDFNKDPYIINYRP-KSILVSPIISQGKLTGILYLENNLTSHAFTEDRLEVLQVLSAQAAISLEN 1500
Cdd:COG2203   85 LREGRPVVVEDILQDPRFRDNPLVLLEPPiRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIER 164
                        170
                 ....*....|
gi 75910912 1501 TRLYLTLETR 1510
Cdd:COG2203  165 ARLYEELQEA 174
COG3899 COG3899
Predicted ATPase [General function prediction only]
316-1179 0e+00

Predicted ATPase [General function prediction only]


:

Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 867.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  316 LYGRETQVEQLLLSFARVSRGNSELILVSGYSGIGKTSVINEVNKPITQVKGYFISGKFDQFKRDIPYLSLVQAFSSLMR 395
Cdd:COG3899    2 LYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLMG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  396 QLLTESTERLEMWRSNILQAVGSNGKVIIDVIPEVELIIGKQPEVSQLSPHESQNRFNQIFQSFIQVFCCCGHPLVIFLD 475
Cdd:COG3899   82 QLLSESDTRILSWRARLLAALGENGQVIIDVIPELELIIGKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEHPLVIVLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  476 DLQWADSATLNLMESLICDQTIkylliiGAYRDNEVSKLHPLISTIEEIKKSGIIINNIELQPLDLANVVHFVQDTLHDN 555
Cdd:COG3899  162 DLHWADSASLKLLQLLMDRIAI------GAYRDNEVLLLHPLRPTLGEILKSATNITTITLAPLSRADTNQLVAATLGCT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  556 TTRCYPLATLVFNKTAGNPFFINQLLKALHQESLLVFDFNIQQWQWEIEKIITVGLSDkSVVELVCSRIQLLPEKTQKIL 635
Cdd:COG3899  236 KLLPAPLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTD-AVVEFLAARLQKLPGTTREVL 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  636 QLAACIGDNFNLYVLSLVNEKSVFDTAHELDDALQCGLILPLSETYRIPLLFDAQDdilfdskqilYKFLHDRVQQAAYS 715
Cdd:COG3899  315 KAAACIGNRFDLDTLAALAEDSPALEAAALLDALQEGLILPLSETYRFGSNVDIAT----------YKFLHDRVQQAAYN 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  716 LIPENQKKYTHLKIGRLLLNNIQEKDIENHVFDIVNQLNKSVDLVIDDSEKNRLIELNFIAGHKSQQATAYEPALSYFMM 795
Cdd:COG3899  385 LIPESQRQYLHLRIGQLLEQNIPEAGQEEEIFDIVNQLNAGVGLITLEEAVDELAELNLLAGRKAKLRSAYSAAISYLER 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  796 AIKLIGESSWLTNYKTILNLYQEATEAAYLCGQFDKMQGLANVVINNAHNLQEKTKVYNLKILTAIAQKQLQEALSLGLN 875
Cdd:COG3899  465 GLSLLLADAWQNQYLLALMLHRLAAENAYLRGQFELSESLIEVVLICAASNLDGAKVYELVIQAYTAQKQRLEAIALGQN 544
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  876 LLNQLGINFPEEPTDDFVNQVLLETNSLIPRNNIQSLLHLPEMTDVNSLAAMDILDTISTAAYSASPKLMLLINLSRVKL 955
Cdd:COG3899  545 ALQLLGIAFPEKPCLAELNQAGEEINQLLGDRAIEELLNLPAMTDPDKLAALRILLNLILALFLTAPNLFPLIILTIVTL 624
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  956 SLTYGNSASSPIAYAAYALILCGVINDSELGYELGKVALDLTADLSP-FIKGKILFYVSNFIFHWKTHLRETLHFSKMGA 1034
Cdd:COG3899  625 SLKYGNSSESAAAYVRYGDILNSFLGDFEKAYEFGKLALQLLEKFNAkELKSKWYLEAGVFILHWNDHLKETISLFKEGL 704
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1035 KYSLEGGDLEYTAWFYQFGCCSLYWQGEELSNLKQKIENANCAIRQTKQEQPLSHQYMLYQVVVNLMDNSQDACCLIGEN 1114
Cdd:COG3899  705 VAGLEFGDLEFASYLAAFYLAEAYKQGELLDDLRQENENYSEALAPFNQVISMVYSVLLIQLIFNLELKSEAEYELIEKI 784
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75910912 1115 YNEQESLTQYEIVNDYLGIYYFHLYKTILNYLFGQHEQARIHAGIAAQNISGATAQFVVPIFYFY 1179
Cdd:COG3899  785 LLESYILPYLLAAKNLNGIGDLYLSKELLLYLFIDAEQAVKLAELAEQYLNDAAGNLAVPIFYFY 849
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-280 1.83e-41

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 155.38  E-value: 1.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912      12 YRILELAHSGANTNIYRATKVDGNTPTILKVlIDNYFSLEAIVRFKHEYSISANLDHPNIVKVISLETHHKRLVIVFEDF 91
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV-IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912      92 GGISLKHYLYNHQP-SLQLTLQVAIAITRALVYIHDNKIIHKDIKPGNIIIKNLGTrlqqtpevlsnliIKLTDFSIASR 170
Cdd:smart00220   80 EGGDLFDLLKKRGRlSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-------------VKLADFGLARQ 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912     171 LKKETPQlinpNQLEGTLAYMSPEQTgrMNRNLDYRSDFYSLGITLYEMLTGQLPFNSSEPLELVHAHIAKEPTPIQQLA 250
Cdd:smart00220  147 LDPGEKL----TTFVGTPEYMAPEVL--LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPE 220
                           250       260       270
                    ....*....|....*....|....*....|
gi 75910912     251 ANVPNAVVGIVHKLMAKNAEDRyYSAQGLL 280
Cdd:smart00220  221 WDISPEAKDLIRKLLVKDPEKR-LTAEEAL 249
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-285 8.17e-66

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: 225.93  E-value: 8.17e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   11 GYRILELAHSGANTNIYRATKVDGNTPTILKVLIDNYFSLEAIV-RFKHEYSISANLDHPNIVKVISLETHHKRLVIVFE 89
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFReRFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   90 DFGGISLKHYLYNHQP-SLQLTLQVAIAITRALVYIHDNKIIHKDIKPGNIIIKNLGtrlqqtpevlsnlIIKLTDFSIA 168
Cdd:cd14014   81 YVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG-------------RVKLTDFGIA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  169 SRLKKETPQLINPNQleGTLAYMSPEQtgRMNRNLDYRSDFYSLGITLYEMLTGQLPFNSSEPLELVHAHIAKEPTPIQQ 248
Cdd:cd14014  148 RALGDSGLTQTGSVL--GTPAYMAPEQ--ARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSP 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 75910912  249 LAANVPNAVVGIVHKLMAKNAEDRYYSAQGLLVDLEQ 285
Cdd:cd14014  224 LNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
1688-1803 4.30e-22

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 94.25  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1688 INQVFLHLLTNSIDAllerknkcksyhgqeiSFSPTIWIS-SIVDDTKQAVIRVTDNGIGIDGNIISKIFDPF--FTTKP 1764
Cdd:cd00075    1 LQQVLLNLLSNAIKH----------------TPEGGGRITiSVERDGDHLEIRVEDNGPGIPEEDLERIFERFsdGSRSR 64
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 75910912 1765 VGKGTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKL 1803
Cdd:cd00075   65 KGGGTGLGLSIVKKLVELHGGRIEVESEPGGGTTFTITL 103
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
315-503 9.28e-38

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 257559  Cd Length: 156  Bit Score: 141.45  E-value: 9.28e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    315 KLYGRETQVEQLLLSFARVSRGNSELILVSGYSGIGKTSVINEVNKPITQVKGYFISGKFDQFkrdiPYLSLVQAFSSLM 394
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKCDEL----PYAALRQLLRELL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    395 RQLLTESterlemwrsnilqavgsngkviidvIPEVELIigkqPEVSQLSPHESQNRFNQIFQSFIQVFCCCGHPLVIFL 474
Cdd:pfam13191   77 RQLLDEL-------------------------LPELELL----PPVPGLPPDDLRNRLEDLLRRLLRRLAARERPLVLVL 127
                          170       180
                   ....*....|....*....|....*....
gi 75910912    475 DDLQWADSATLNLMESLICDQTIKYLLII 503
Cdd:pfam13191  128 DDLQWADEASLALLLALARLLERLPLLLV 156
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1684-1806 1.12e-25

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643  Cd Length: 111  Bit Score: 105.04  E-value: 1.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    1684 DASQINQVFLHLLTNSIDALLErknkcksyhgqeisfSPTIWISsIVDDTKQAVIRVTDNGIGIDGNIISKIFDPFFTTK 1763
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPE---------------GGRITVT-LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 75910912    1764 P---VGKGTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKLPIS 1806
Cdd:smart00387   66 KrsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1684-1805 7.60e-25

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 251347  Cd Length: 111  Bit Score: 102.40  E-value: 7.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   1684 DASQINQVFLHLLTNSIDallerknkcksyHGQEisfSPTIWISsIVDDTKQAVIRVTDNGIGIDGNIISKIFDPFFTTK 1763
Cdd:pfam02518    2 DEDRLRQVLSNLLDNAIK------------HAPA---GGEIEVT-LERDGGRLRITVEDNGIGIPPEDLPKIFEPFFRTD 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 75910912   1764 PV---GKGTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKLPI 1805
Cdd:pfam02518   66 GSrskVGGTGLGLSIVRKLVELHGGTITVESEPGGGTTFTLTLPL 110
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
1344-1510 7.71e-19

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 86.95  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1344 VVKASQALSSEIVLEKLLEKLMFLAKENAGAQkVFFIAKKDEKLVIEGSLMEEGIIKTLQAI--PITNSQALPASVINYV 1421
Cdd:COG2203    6 LNELAAKIAQDLDLEEILQAALELLAELLGAD-RGLIYLLDEDGLLDGALVAEAAEAGLEQLidELFGLVILPACLIGIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1422 KRTQAPLVLDDVTHAEDFNKDPYIINYRP-KSILVSPIISQGKLTGILYLENNLTSHAFTEDRLEVLQVLSAQAAISLEN 1500
Cdd:COG2203   85 LREGRPVVVEDILQDPRFRDNPLVLLEPPiRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIER 164
                        170
                 ....*....|
gi 75910912 1501 TRLYLTLETR 1510
Cdd:COG2203  165 ARLYEELQEA 174
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1357-1504 1.98e-15

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 75.88  E-value: 1.98e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    1357 LEKLLEKLMFLAKENAGAQKVFfIAKKDEKLVIEGSLME-EGIIKTLQAIPItnsqALPASVINYVKRTQAPLVLDDVTH 1435
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVL-IYLVDENDRGELVLVAaDGLTLPTLGIRF----PLDEGLAGRVAETGRPLNIPDVEA 76
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75910912    1436 AEDFNKDPYIINYRPKSILVSPIISQGKLTGILYLENNLTSHAFTEDRLEVLQVLSAQAAISLENTRLY 1504
Cdd:smart00065   77 DPLFAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLY 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
1357-1498 3.22e-14

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54.


Pssm-ID: 250726  Cd Length: 146  Bit Score: 72.23  E-value: 3.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   1357 LEKLLEKLMFLAKENAGAQKVFFIAKKDEKLVIEGSLMEEGIIKTLQAIPITNSQALPASVInyvkRTQAPLVLDDVTHA 1436
Cdd:pfam01590    2 LEELLQTILEELRELLGADRVAIYLADADGLLLYLVAGDGLSDIPLAARGLPLGGGVVGEVI----AGGNPIVVPDVQDD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   1437 EDFNKDP--------YIINYRPKSILVSPIISQGKLTGILYLENNlTSHAFTEDRLEVLQVLSAQAAISL 1498
Cdd:pfam01590   78 PRFRDLTalasdlphFLRGLGIRSCLAVPLKGGGELIGVLVLHST-SPRAFTEEELELLQALADQVAIAL 146
COG3899 COG3899
Predicted ATPase [General function prediction only]
316-1179 0e+00

Predicted ATPase [General function prediction only]


Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 867.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  316 LYGRETQVEQLLLSFARVSRGNSELILVSGYSGIGKTSVINEVNKPITQVKGYFISGKFDQFKRDIPYLSLVQAFSSLMR 395
Cdd:COG3899    2 LYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLMG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  396 QLLTESTERLEMWRSNILQAVGSNGKVIIDVIPEVELIIGKQPEVSQLSPHESQNRFNQIFQSFIQVFCCCGHPLVIFLD 475
Cdd:COG3899   82 QLLSESDTRILSWRARLLAALGENGQVIIDVIPELELIIGKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEHPLVIVLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  476 DLQWADSATLNLMESLICDQTIkylliiGAYRDNEVSKLHPLISTIEEIKKSGIIINNIELQPLDLANVVHFVQDTLHDN 555
Cdd:COG3899  162 DLHWADSASLKLLQLLMDRIAI------GAYRDNEVLLLHPLRPTLGEILKSATNITTITLAPLSRADTNQLVAATLGCT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  556 TTRCYPLATLVFNKTAGNPFFINQLLKALHQESLLVFDFNIQQWQWEIEKIITVGLSDkSVVELVCSRIQLLPEKTQKIL 635
Cdd:COG3899  236 KLLPAPLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTD-AVVEFLAARLQKLPGTTREVL 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  636 QLAACIGDNFNLYVLSLVNEKSVFDTAHELDDALQCGLILPLSETYRIPLLFDAQDdilfdskqilYKFLHDRVQQAAYS 715
Cdd:COG3899  315 KAAACIGNRFDLDTLAALAEDSPALEAAALLDALQEGLILPLSETYRFGSNVDIAT----------YKFLHDRVQQAAYN 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  716 LIPENQKKYTHLKIGRLLLNNIQEKDIENHVFDIVNQLNKSVDLVIDDSEKNRLIELNFIAGHKSQQATAYEPALSYFMM 795
Cdd:COG3899  385 LIPESQRQYLHLRIGQLLEQNIPEAGQEEEIFDIVNQLNAGVGLITLEEAVDELAELNLLAGRKAKLRSAYSAAISYLER 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  796 AIKLIGESSWLTNYKTILNLYQEATEAAYLCGQFDKMQGLANVVINNAHNLQEKTKVYNLKILTAIAQKQLQEALSLGLN 875
Cdd:COG3899  465 GLSLLLADAWQNQYLLALMLHRLAAENAYLRGQFELSESLIEVVLICAASNLDGAKVYELVIQAYTAQKQRLEAIALGQN 544
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  876 LLNQLGINFPEEPTDDFVNQVLLETNSLIPRNNIQSLLHLPEMTDVNSLAAMDILDTISTAAYSASPKLMLLINLSRVKL 955
Cdd:COG3899  545 ALQLLGIAFPEKPCLAELNQAGEEINQLLGDRAIEELLNLPAMTDPDKLAALRILLNLILALFLTAPNLFPLIILTIVTL 624
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  956 SLTYGNSASSPIAYAAYALILCGVINDSELGYELGKVALDLTADLSP-FIKGKILFYVSNFIFHWKTHLRETLHFSKMGA 1034
Cdd:COG3899  625 SLKYGNSSESAAAYVRYGDILNSFLGDFEKAYEFGKLALQLLEKFNAkELKSKWYLEAGVFILHWNDHLKETISLFKEGL 704
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1035 KYSLEGGDLEYTAWFYQFGCCSLYWQGEELSNLKQKIENANCAIRQTKQEQPLSHQYMLYQVVVNLMDNSQDACCLIGEN 1114
Cdd:COG3899  705 VAGLEFGDLEFASYLAAFYLAEAYKQGELLDDLRQENENYSEALAPFNQVISMVYSVLLIQLIFNLELKSEAEYELIEKI 784
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75910912 1115 YNEQESLTQYEIVNDYLGIYYFHLYKTILNYLFGQHEQARIHAGIAAQNISGATAQFVVPIFYFY 1179
Cdd:COG3899  785 LLESYILPYLLAAKNLNGIGDLYLSKELLLYLFIDAEQAVKLAELAEQYLNDAAGNLAVPIFYFY 849
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-280 1.83e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 155.38  E-value: 1.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912      12 YRILELAHSGANTNIYRATKVDGNTPTILKVlIDNYFSLEAIVRFKHEYSISANLDHPNIVKVISLETHHKRLVIVFEDF 91
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV-IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912      92 GGISLKHYLYNHQP-SLQLTLQVAIAITRALVYIHDNKIIHKDIKPGNIIIKNLGTrlqqtpevlsnliIKLTDFSIASR 170
Cdd:smart00220   80 EGGDLFDLLKKRGRlSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-------------VKLADFGLARQ 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912     171 LKKETPQlinpNQLEGTLAYMSPEQTgrMNRNLDYRSDFYSLGITLYEMLTGQLPFNSSEPLELVHAHIAKEPTPIQQLA 250
Cdd:smart00220  147 LDPGEKL----TTFVGTPEYMAPEVL--LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPE 220
                           250       260       270
                    ....*....|....*....|....*....|
gi 75910912     251 ANVPNAVVGIVHKLMAKNAEDRyYSAQGLL 280
Cdd:smart00220  221 WDISPEAKDLIRKLLVKDPEKR-LTAEEAL 249
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
1420-1804 8.98e-44

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms]


Pssm-ID: 226654 [Multi-domain]  Cd Length: 603  Bit Score: 169.80  E-value: 8.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1420 YVKRTQAPLVLDDVThaedfnkdpyiINY-RPKSILVSPIISQGKLTGILYLEN-NLTSHAFTEDRLEVLQVLSAQAais 1497
Cdd:COG4191  265 YLSQSRVPLPETGWT-----------LSVlSPTAVLLRSAVRTARLAAILTLALlALLLALWLRRRRRARLRLAELQ--- 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1498 lentRLYLTLETRVQQRTQELEDKNHQLQTIL-------GELQRTQAQLIHNEKMSSLGQLVAGVAHEINNPinfiygnV 1570
Cdd:COG4191  331 ----EARAELERRVEERTADLTRANARLQAEIaereqaeAALRRAQDELVQAGKLAALGQMSAGIAHELNQP-------L 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1571 THIKDYSkslldiidfyqaeypDSQETILEIAdeyDIDFIKDDMpKLLTSMkngAERIRDIVISLRNFSRLDESAIKEVD 1650
Cdd:COG4191  400 AAIRTYA---------------DNARLLLERG---RTEEARENL-ERISAL---TERMAAITAHLKSFARKSRDAAGPVS 457
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912 1651 IHEGIDNTLMILQQRLP--DIQIIKEYGD-LPKITCDASQINQVFLHLLTNSIDALlerknkcksyHGQEisfSPTIWIs 1727
Cdd:COG4191  458 LREAIEGALELLRGRLRaaGVELELDLPDaPLWVMANEIRLEQVLVNLLQNALDAM----------AGQE---DRRLSI- 523
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75910912 1728 SIVDDTKQAVIRVTDNGIGIDGNIISKIFDPFFTTKPVGKGTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKLP 1804
Cdd:COG4191  524 RAQREGGQVVLTVRDNGPGIAPEALPHLFEPFFTTKPVGKGLGLGLAISQNIARDLGGSLEVANHPEGGASFTIELR 600
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
11-291 2.73e-39

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: 152.59  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   11 GYRILELAHSGANTNIYRATKvdgNTPTILKVLIDNYFS-LEAIVRFKHEYSISANLDHP-NIVKVISLETHHKRLVIVF 88
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESkSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   89 EDFGGISLKHYLYNHQPSLQLTLQVAIAITR----ALVYIHDNKIIHKDIKPGNIIIKNLGTrlqqtpevlsnlIIKLTD 164
Cdd:COG0515   78 EYVDGGSLEDLLKKIGRKGPLSESEALFILAqilsALEYLHSKGIIHRDIKPENILLDRDGR------------VVKLID 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  165 FSIASRLKKETPQLINPNQ---LEGTLAYMSPEQ-TGRMNRNLDYRSDFYSLGITLYEMLTGQLPF---NSSEPLELVHA 237
Cdd:COG0515  146 FGLAKLLPDPGSTSSIPALpstSVGTPGYMAPEVlLGLSLAYASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLK 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  238 HIAKEPTP------IQQLAANVPNAVVGIVHKLMAKNAEDRYYSAQGLLVDLEQCLEQLN 291
Cdd:COG0515  226 IILELPTPslasplSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKE 285
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
1531-1805 2.19e-38

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 152.81  E-value: 2.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  1531 ELQRTQAQLIHNEKMSSLGQLVAGVAHEINNPINFIYGNVTHIKDYSKSlldiidfyqaeyPDSQETILEIADEYDidfi 1610
Cdd:PRK11360  373 ERKRLQRRVARQERLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSD------------PPSQEYLSVVLREVD---- 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  1611 kddmpklltsmkngaeRIRDIVISLRNFSRLDESAIKEVDIHEGIDNTLMILQQRL--PDIQIIKEY-GDLPKITCDASQ 1687
Cdd:PRK11360  437 ----------------RLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGvqARVDFETELdNELPPIWADPEL 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912  1688 INQVFLHLLTNSIdallerknkcksyhgQEISFSPTIWISSIVDDTKQAVIRVTDNGIGIDGNIISKIFDPFFTTKPvgK 1767
Cdd:PRK11360  501 LKQVLLNILINAV---------------QAISARGKIRIRTWQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKA--K 563
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 75910912  1768 GTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKLPI 1805
Cdd:PRK11360  564 GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
Pkinase pfam00069
Protein kinase domain;
12-279 3.36e-37

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 143.16  E-value: 3.36e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912     12 YRILELAHSGANTNIYRATKVDGNTPTILKVL-IDNYFSLEAIVRFKhEYSISANLDHPNIVKVISLETHHKRLVIVFED 90
Cdd:pfam00069    1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILkKRSEKSKKDQTARR-EIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912     91 FGGISLKHYLYNHQPslqLTLQVAIAIT----RALVYIHDNKIIHKDIKPGNIIIKNlgtrlqqtpevlsNLIIKLTDFS 166
Cdd:pfam00069   80 CEGGDLFDYLSRGGP---LSEDEAKKIAlqilRGLEYLHSNGIIHRDLKPENILLDE-------------NGVVKIADFG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    167 IASRLKKETPqliNPNQLEGTLAYMSPEQTgRMNRNLDYRSDFYSLGITLYEMLTGQLPFNSSEPLEL--VHAHIAKEPT 244
Cdd:pfam00069  144 LAKKLTKSSS---SLTTFVGTPEYMAPEVL-LGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQlqLIRRILGPPL 219
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 75910912    245 PIQ-QLAANVPNAVVGIVHKLMAKNAEDRYYSAQGL 279
Cdd:pfam00069  220 EFDePKSDSGSEEAKDLIKKCLNKDPSKRPTAEEIL 255
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
20-226 2.12e-20

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 94.12  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    20 SGANTNIYRATKVDGNTPTILKVLIDNYfslEAIVRFK--HEYSISANLDHPNIVKVISLETHHKRLVIVFEDFGGISLK 97
Cdd:PLN00034   84 SGAGGTVYKVIHRPTGRLYALKVIYGNH---EDTVRRQicREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    98 HYLYNHQPSLQltlQVAIAITRALVYIHDNKIIHKDIKPGNIIIkNLGTRlqqtpevlsnliIKLTDFSIaSRLKKETpq 177
Cdd:PLN00034  161 GTHIADEQFLA---DVARQILSGIAYLHRRHIVHRDIKPSNLLI-NSAKN------------VKIADFGV-SRILAQT-- 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 75910912   178 lINP-NQLEGTLAYMSPEqtgRMNRNLD------YRSDFYSLGITLYEMLTGQLPF 226
Cdd:PLN00034  222 -MDPcNSSVGTIAYMSPE---RINTDLNhgaydgYAGDIWSLGVSILEFYLGRFPF 273
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
55-279 1.63e-17

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: 87.98  E-value: 1.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912     55 RFKHEYSISANLDHPNIVKVI-SLETHHKRLVIVFEDFGGISLKHYLYNHQP-----SLQLTLQVAIAITRAlvyiHDNK 128
Cdd:TIGR03903   24 RFRRETALCARLYHPNIVALLdSGEAPPGLLFAVFEYVPGRTLREVLAADGAlpageTGRLMLQVLDALACA----HNQG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    129 IIHKDIKPGNIIIKNLGTRLQQtpevlsnliiKLTDFSIASRL----KKETPQLINPNQLEGTLAYMSPEQTgrMNRNLD 204
Cdd:TIGR03903  100 IVHRDLKPQNIMVSQTGVRPHA----------KVLDFGIGTLLpgvrDADVATLTRTTEVLGTPTYCAPEQL--RGEPVT 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75910912    205 YRSDFYSLGITLYEMLTGQLPFNSSEPLELVHAHIAKEPTPIQQLAANVPNAVVgiVHKLMAKNAEDRYYSAQGL 279
Cdd:TIGR03903  168 PNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLPPWIAGHPLGQV--LRKALNKDPRQRAASAPAL 240
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
1503-1805 2.79e-16

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions].


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 82.64  E-value: 2.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   1503 LYLTLETRVQQRTQELEDKNHQLQTILGElqrtqaqlihNEKMSSLGQLVAGVAHEINNPINFIYGnvthikdySKSLLD 1582
Cdd:TIGR02938  241 LLLTIADISNLREEQERARLSALQALMAE----------EERLEAIRETLSAAIHRLQGPMNLISA--------AISVLQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   1583 iidfyqaeypdsqetilEIADEYDIDFIKDDMPKLLTSMKNGAERIRDiVISLRnfsrlDESAIKEVDIHEGIDNTLMIL 1662
Cdd:TIGR02938  303 -----------------RRGDDAGNPASAAMLQQALSAGREHMEALRQ-VIPQS-----PQEIVVPVNLNQILRDVITLS 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   1663 QQRLPDIQIIKEY---GDLPKITCDASQINQVFLHLLTNSIDALLErknkcKSYHGQEISfsptiwISSIVDDtKQAVIR 1739
Cdd:TIGR02938  360 TPRLLAAGIVVDWqpaATLPAILGRELQLRSLFKALVDNAIEAMNI-----KGWKRRELS------ITTALNG-DLIVVS 427
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75910912   1740 VTDNGIGIDGNIISKIFDPFFTTKP-VGKGTGLGLSISYQIVEKHQGSLECLPSLTDGTTFIVKLPI 1805
Cdd:TIGR02938  428 ILDSGPGIPQDLRYKVFEPFFTTKGgSRKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFRV 494
pknD PRK13184
serine/threonine-protein kinase; Reviewed
55-288 2.98e-16

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 83.67  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    55 RFKHEYSISANLDHPNIVKVISLETHHKRLVIVFEDFGGISLKHYLYN------------HQPSLQLTLQVAIAITRALV 122
Cdd:PRK13184   48 RFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTLKSLLKSvwqkeslskelaEKTSVGAFLSIFHKICATIE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   123 YIHDNKIIHKDIKPGNIIIKNLGTRL----------QQTPEVLSNLIIKLTDfSIASRLKKetpqlinPNQLEGTLAYMS 192
Cdd:PRK13184  128 YVHSKGVLHRDLKPDNILLGLFGEVVildwgaaifkKLEEEDLLDIDVDERN-ICYSSMTI-------PGKIVGTPDYMA 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   193 PEQTgrMNRNLDYRSDFYSLGITLYEMLTGQLPFNSSEPLELVHAHIAKEPtpiQQLAA--NVPNAVVGIVHKLMAKNAE 270
Cdd:PRK13184  200 PERL--LGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISYRDVILSP---IEVAPyrEIPPFLSQIAMKALAVDPA 274
                         250
                  ....*....|....*...
gi 75910912   271 DRYYSAQGLLVDLEQCLE 288
Cdd:PRK13184  275 ERYSSVQELKQDLEPHLQ 292
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
53-232 5.93e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 67.54  E-value: 5.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    53 IVRFKH------EYSISANLDHPNIVKVISLETHHKRLVIVFEDFGGISLKHYLynhQPSLQLTLQVA----IAITRALV 122
Cdd:PTZ00263   56 ILKMKQvqhvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGELFTHL---RKAGRFPNDVAkfyhAELVLAFE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   123 YIHDNKIIHKDIKPGNIIIKNLGTrlqqtpevlsnliIKLTDFSIASRLKKETPQLInpnqleGTLAYMSPE--QTGRMN 200
Cdd:PTZ00263  133 YLHSKDIIYRDLKPENLLLDNKGH-------------VKVTDFGFAKKVPDRTFTLC------GTPEYLAPEviQSKGHG 193
                         170       180       190
                  ....*....|....*....|....*....|..
gi 75910912   201 RNLDYrsdfYSLGITLYEMLTGQLPFNSSEPL 232
Cdd:PTZ00263  194 KAVDW----WTMGVLLYEFIAGYPPFFDDTPF 221
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
59-223 7.12e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 61.93  E-value: 7.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912    59 EYSISANLDHPNIVKVISLETHHKRLVIVFEDFGgISLKHYLYNHQpSLQLTLQVAI--AITRALVYIHDNKIIHKDIKP 136
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYK-TDLYCYLAAKR-NIAICDILAIerSVLRAIQYLHENRIIHRDIKA 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   137 GNIIIKNLGTrlqqtpevlsnliIKLTDFSIASrlkkeTPQLINPNQL---EGTLAYMSPEQTGRmnRNLDYRSDFYSLG 213
Cdd:PHA03212  211 ENIFINHPGD-------------VCLGDFGAAC-----FPVDINANKYygwAGTIATNAPELLAR--DPYGPAVDIWSAG 270
                         170
                  ....*....|
gi 75910912   214 ITLYEMLTGQ 223
Cdd:PHA03212  271 IVLFEMATCH 280
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-285 8.17e-66

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: 225.93  E-value: 8.17e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75910912   11 GYRILELAHSGANTNIYRATKVDGN