|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
263-496 |
1.15e-40 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 153.25 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 263 IDTNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAM--------------N 328
Cdd:COG0840 265 VASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGevveeavegieeirE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 329 EAENADRAAARLTEVAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREID 408
Cdd:COG0840 345 SVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 409 GMQSVSHDVVSSLGTIRSAMNNLREFVVMS-------AGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVG 481
Cdd:COG0840 425 EIQSETEEAVEAMEEGSEEVEEGVELVEEAgealeeiVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENA 504
|
250
....*....|....*
gi 933519334 482 SAIAETKDAARVLAR 496
Cdd:COG0840 505 ASVEEVAAAAEELAE 519
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
285-474 |
4.35e-37 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 135.44 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 285 AVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAMNEAENADRAAARLTEVAKAMGGIVELIRSIAGQINML 364
Cdd:cd11386 4 SASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 365 ALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREIDGMQSVSHDVVSSLGTIRSAMNNLREFVVMS------ 438
Cdd:cd11386 84 ALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETgrafee 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 933519334 439 -AGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIA 474
Cdd:cd11386 164 iVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
263-496 |
1.38e-36 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 135.88 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 263 IDTNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAMNEAENADRAAARLTE 342
Cdd:smart00283 9 IAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 343 VAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREIDGMQSVSHDVV---- 418
Cdd:smart00283 89 SSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVaame 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 419 -------SSLGTIRSAMNNLREFVvmsaGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVGSAIAETKDAA 491
Cdd:smart00283 169 essseveEGVELVEETGDALEEIV----DSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAA 244
|
....*
gi 933519334 492 RVLAR 496
Cdd:smart00283 245 EELSG 249
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
23-259 |
1.92e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 132.84 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 23 NHSQAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDQaEQNSTAYREFWDRLKRGEFQRALYKRIGKNGREVW 102
Cdd:COG2202 19 SSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP-EDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 103 VEATYNPILDSGGRPCKVIKIATDVTERQKINADLRGKVEAL-----SRSQAVIEFNPDGTVITANENFLKVLGYSLDEV 177
Cdd:COG2202 98 VELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLrllveNAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 178 RGRHHSMFVDPgeRDGAAYREFWRTLNKGQFEA--AQYRRIGKGGRVAWIQASYNPVFDDAGRLcKIVKFATDITEQVRL 255
Cdd:COG2202 178 LGKSLLDLLHP--EDRERLLELLRRLLEGGRESyeLELRLKDGDGRWVWVEASAVPLRDGGEVI-GVLGIVRDITERKRA 254
|
....
gi 933519334 256 LERL 259
Cdd:COG2202 255 EEAL 258
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
319-482 |
1.23e-23 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 97.50 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 319 SQQAADIAMNEAENADRAAARLTEVAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSAN 398
Cdd:pfam00015 7 ASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 399 ATAQISREIDGMQSVSHDVVSSLGTIRSAMNNLREFVVMSAGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFA 478
Cdd:pfam00015 87 AAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVA 166
|
....
gi 933519334 479 QVGS 482
Cdd:pfam00015 167 RMDQ 170
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
265-464 |
1.60e-23 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 103.61 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 265 TNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANsmtRSQQAADIAMNEAENADRAAARLTEVA 344
Cdd:PRK09793 275 IGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASE---LAKNAATTAQAGGVQVSTMTHTMQEIA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 345 ---KAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQI--------------SREI 407
Cdd:PRK09793 352 tssQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIkglieesvnrvqqgSKLV 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933519334 408 DGMQSVSHDVVSS-------LGTIRSAMNNLREFVVMSAGAVEEQTTVTSSMSANMQEASTSVE 464
Cdd:PRK09793 432 NNAAATMTDIVSSvtrvndiMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATE 495
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
159-246 |
2.50e-18 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 79.69 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 159 VITANENFLKVLGYSLDEVRGR--HHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQASYNPVFDDA 236
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
90
....*....|
gi 933519334 237 GRLCKIVKFA 246
Cdd:pfam08447 80 GKPVRVIGVA 89
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
147-249 |
1.12e-14 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 69.97 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 147 SQAVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQ 226
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 933519334 227 ASYNPVFDDAGRLCKIVKFATDI 249
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
20-137 |
1.37e-12 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 64.62 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 20 SALNHSQ-AVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIdqAEQNSTAYREFWDRLKRGE--FQRALYKRIGK 96
Cdd:TIGR00229 7 AIFESSPdAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI--PEEDREEVRERIERRLEGEpePVSEERRVRRK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 933519334 97 NGREVWVEATYNPILDSGGRPcKVIKIATDVTERQKINADL 137
Cdd:TIGR00229 85 DGSEIWVEVSVSPIRTNGGEL-GVVGIVRDITERKEAEEAL 124
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
1-260 |
8.85e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 54.68 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 1 MIGFMRAIKGKGSDSKAILSALNHSQAVIEF---AIDGTILDANPNFL--------------TVMGYTLP--------EI 55
Cdd:PRK13560 310 LVGAITDISGRRAAERELLEKEDMLRAIIEAapiAAIGLDADGNICFVnnnaaermlgwsaaEVMGKPLPgmdpelneEF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 56 VGHHHRMFIDQAEQNSTAYREFWDRLKRGE-FQRALYKRIGKNGREVWVEATYNPILDSGGRPCKVIKIATDVTERQKIN 134
Cdd:PRK13560 390 WCGDFQEWYPDGRPMAFDACPMAKTIKGGKiFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 135 ADLRGKVEALSRSQAVI---EFNPDGTVITANENFLKvLGYSLDE-VRG-RHHSMFVDPGERDGAAyREFWRTLNKG--Q 207
Cdd:PRK13560 470 EQLLLANLIVENSPLVLfrwKAEEGWPVELVSKNITQ-FGYEPDEfISGkRMFAAIIHPADLEQVA-AEVAEFAAQGvdR 547
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 933519334 208 FEAaQYRRIGKGGRVAWIQASYNPVFDDAGRLCKIVKFATDITEQVRLLERLK 260
Cdd:PRK13560 548 FEQ-EYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIK 599
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
147-192 |
1.91e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 39.69 E-value: 1.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 933519334 147 SQAVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERD 192
Cdd:smart00091 11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRE 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
263-496 |
1.15e-40 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 153.25 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 263 IDTNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAM--------------N 328
Cdd:COG0840 265 VASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGevveeavegieeirE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 329 EAENADRAAARLTEVAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREID 408
Cdd:COG0840 345 SVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 409 GMQSVSHDVVSSLGTIRSAMNNLREFVVMS-------AGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVG 481
Cdd:COG0840 425 EIQSETEEAVEAMEEGSEEVEEGVELVEEAgealeeiVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENA 504
|
250
....*....|....*
gi 933519334 482 SAIAETKDAARVLAR 496
Cdd:COG0840 505 ASVEEVAAAAEELAE 519
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
285-474 |
4.35e-37 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 135.44 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 285 AVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAMNEAENADRAAARLTEVAKAMGGIVELIRSIAGQINML 364
Cdd:cd11386 4 SASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 365 ALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREIDGMQSVSHDVVSSLGTIRSAMNNLREFVVMS------ 438
Cdd:cd11386 84 ALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETgrafee 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 933519334 439 -AGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIA 474
Cdd:cd11386 164 iVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
263-496 |
1.38e-36 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 135.88 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 263 IDTNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAMNEAENADRAAARLTE 342
Cdd:smart00283 9 IAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 343 VAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREIDGMQSVSHDVV---- 418
Cdd:smart00283 89 SSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVaame 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 419 -------SSLGTIRSAMNNLREFVvmsaGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVGSAIAETKDAA 491
Cdd:smart00283 169 essseveEGVELVEETGDALEEIV----DSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAA 244
|
....*
gi 933519334 492 RVLAR 496
Cdd:smart00283 245 EELSG 249
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
23-259 |
1.92e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 132.84 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 23 NHSQAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDQaEQNSTAYREFWDRLKRGEFQRALYKRIGKNGREVW 102
Cdd:COG2202 19 SSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP-EDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 103 VEATYNPILDSGGRPCKVIKIATDVTERQKINADLRGKVEAL-----SRSQAVIEFNPDGTVITANENFLKVLGYSLDEV 177
Cdd:COG2202 98 VELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLrllveNAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 178 RGRHHSMFVDPgeRDGAAYREFWRTLNKGQFEA--AQYRRIGKGGRVAWIQASYNPVFDDAGRLcKIVKFATDITEQVRL 255
Cdd:COG2202 178 LGKSLLDLLHP--EDRERLLELLRRLLEGGRESyeLELRLKDGDGRWVWVEASAVPLRDGGEVI-GVLGIVRDITERKRA 254
|
....
gi 933519334 256 LERL 259
Cdd:COG2202 255 EEAL 258
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
23-317 |
2.10e-28 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 117.77 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 23 NHSQAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDqAEQNSTaYREFWDRLKRGE-FQRALYKRIGKNGREV 101
Cdd:COG5809 23 NAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLH-PDDEKE-LREILKLLKEGEsRDELEFELRHKNGKRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 102 WVEATYNPILDSGGRPCKVIKIATDVTERQKINADLRgKVEALSRS------QAVIEFNPDGTVITANENFLKVLGYSLD 175
Cdd:COG5809 101 EFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALR-ESEEKFRLifnhspDGIIVTDLDGRIIYANPAACKLLGISIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 176 EVRGRHHSMFVDPGERDGAAyREFWRTLNKGQFEAAQYRRIGKGGRVAWIQASYNPVFDDAGRLCKIVkFATDITEQVRL 255
Cdd:COG5809 180 ELIGKSILELIHSDDQENVA-AFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVI-IFRDITERKKL 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933519334 256 LERLkllidtnfgeiekamgsahQRADAAAVAStetratvqtiaagaeEMASS-AQEIANSMT 317
Cdd:COG5809 258 EELL-------------------RKSEKLSVVG---------------ELAAGiAHEIRNPLT 286
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
319-482 |
1.23e-23 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 97.50 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 319 SQQAADIAMNEAENADRAAARLTEVAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSAN 398
Cdd:pfam00015 7 ASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 399 ATAQISREIDGMQSVSHDVVSSLGTIRSAMNNLREFVVMSAGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFA 478
Cdd:pfam00015 87 AAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVA 166
|
....
gi 933519334 479 QVGS 482
Cdd:pfam00015 167 RMDQ 170
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
265-464 |
1.60e-23 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 103.61 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 265 TNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANsmtRSQQAADIAMNEAENADRAAARLTEVA 344
Cdd:PRK09793 275 IGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASE---LAKNAATTAQAGGVQVSTMTHTMQEIA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 345 ---KAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQI--------------SREI 407
Cdd:PRK09793 352 tssQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIkglieesvnrvqqgSKLV 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933519334 408 DGMQSVSHDVVSS-------LGTIRSAMNNLREFVVMSAGAVEEQTTVTSSMSANMQEASTSVE 464
Cdd:PRK09793 432 NNAAATMTDIVSSvtrvndiMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATE 495
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
268-494 |
7.11e-21 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 95.79 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 268 GEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTR-----------SQQAADIAMNEAENADRA 336
Cdd:PRK15041 261 GELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQltatvkqnaenARQASHLALSASETAQRG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 337 AARLTEVAKAM----------GGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISRE 406
Cdd:PRK15041 341 GKVVDNVVQTMrdistssqkiADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 407 IDgmQSVSH-DVVSSLgtIRSAMNNLREFVvmsaGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVGSAIA 485
Cdd:PRK15041 421 IE--DSVGKvDVGSTL--VESAGETMAEIV----SAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVE 492
|
....*....
gi 933519334 486 ETKDAARVL 494
Cdd:PRK15041 493 ESAAAAAAL 501
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
268-494 |
4.25e-20 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 93.15 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 268 GEIEKAMGSA--HQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANsmtRSQQAADIAMNEAENADRAAARLTEVA- 344
Cdd:PRK15048 278 GTREIAAGNTdlSSRTEQQASALEETAASMEQLTATVKQNADNARQASQ---LAQSASDTAQHGGKVVDGVVKTMHEIAd 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 345 --KAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSANATAQISREIDgmQSVSH-DVVSSL 421
Cdd:PRK15048 355 ssKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE--DSVSRvDTGSVL 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933519334 422 gtIRSAMNNLREFVvmsaGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVGSAIAETKDAARVL 494
Cdd:PRK15048 433 --VESAGETMNNIV----NAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAAL 499
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
147-260 |
7.80e-20 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 88.93 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 147 SQAVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVdPGERDGAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQ 226
Cdd:COG2202 21 PDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLL-PPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVE 99
|
90 100 110
....*....|....*....|....*....|....
gi 933519334 227 ASYNPVFDDAGRLCKIVKFATDITEQVRLLERLK 260
Cdd:COG2202 100 LSISPVRDEDGEITGFVGIARDITERKRAEEALR 133
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
159-246 |
2.50e-18 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 79.69 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 159 VITANENFLKVLGYSLDEVRGR--HHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQASYNPVFDDA 236
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
90
....*....|
gi 933519334 237 GRLCKIVKFA 246
Cdd:pfam08447 80 GKPVRVIGVA 89
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
263-425 |
2.09e-17 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 85.07 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 263 IDTNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAMNEAE----------- 331
Cdd:COG0840 258 VRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEeggevveeave 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 332 ----------NADRAAARLTEVAKAMGGIVELIRSIAGQINMLALNATIEAARAGEAGRGFAVVANEVKNLANQSAN--- 398
Cdd:COG0840 338 gieeiresveETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEatk 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 --------------------------------------------------------------------------------
Cdd:COG0840 418 eieelieeiqseteeaveameegseeveegvelveeagealeeiveaveevsdliqeiaaaseeqsagteevnqaieqia 497
|
250 260 270
....*....|....*....|....*....|....*
gi 933519334 399 --------ATAQISREIDGMQSVSHDVVSSLGTIR 425
Cdd:COG0840 498 aaaqenaaSVEEVAAAAEELAELAEELQELVSRFK 532
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
23-279 |
2.33e-17 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 84.40 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 23 NHSQAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDqAEQNSTAYREFwDRLKRGEFQRALYKRIGKNGREVW 102
Cdd:COG5805 42 NLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLE-KEYHYRVKTRI-ERLQKGYDVVMIEQIYCKDGELIY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 103 VEATYNPILDSGGRPckVIKIATDVTERQKINADLRgkvEALSRSQAVIE--------FNPDGTVITANENFLKVLGYSL 174
Cdd:COG5805 120 VEVKLFPIYNQNGQA--AILALRDITKKKKIEEILQ---EQEERLQTLIEnspdlicvIDTDGRILFINESIERLFGAPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 175 DEVRGRHHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQASYNPVFDDAGRLCKIVKFATDITEQVR 254
Cdd:COG5805 195 EELIGKNLLELLHPCDKE-EFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKE 273
|
250 260 270
....*....|....*....|....*....|.
gi 933519334 255 L------LERLKLLidtnfGEIekAMGSAHQ 279
Cdd:COG5805 274 AeelmarSEKLSIA-----GQL--AAGIAHE 297
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
37-124 |
4.15e-16 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 73.53 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 37 ILDANPNFLTVMGYTLPEIVG--HHHRMFI---DQAEqnstAYREFWDRLKRGEFQRALYKRIGKNGREVWVEATYNPIL 111
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVhpdDRER----VREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76
|
90
....*....|...
gi 933519334 112 DSGGRPCKVIKIA 124
Cdd:pfam08447 77 DENGKPVRVIGVA 89
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
34-129 |
6.26e-15 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 70.18 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 34 DGTILDANPNFLTVMGYTLPEIVGHHHRMFIDQAEQNSTaYREFWDRLKRGEFQRALYKRigKNGREVWVEATYNPILDS 113
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSER-LREALREGKAVREFEVVLYR--KDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 933519334 114 GGRPCKVIKIATDVTE 129
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
147-249 |
1.12e-14 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 69.97 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 147 SQAVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQ 226
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 933519334 227 ASYNPVFDDAGRLCKIVKFATDI 249
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
145-254 |
8.10e-13 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 64.74 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 145 SRSQAVIEFNPDGTVITANENFLKVLGYSLDEVRGRH-HSMFVDPgerDGAAYREFWRTLNKGQFEAAQYRRIGKGGRVA 223
Cdd:pfam08448 3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTlAELLPPE---DAARLERALRRALEGEEPIDFLEELLLNGEER 79
|
90 100 110
....*....|....*....|....*....|.
gi 933519334 224 WIQASYNPVFDDAGRLCKIVKFATDITEQVR 254
Cdd:pfam08448 80 HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
20-137 |
1.37e-12 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 64.62 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 20 SALNHSQ-AVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIdqAEQNSTAYREFWDRLKRGE--FQRALYKRIGK 96
Cdd:TIGR00229 7 AIFESSPdAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI--PEEDREEVRERIERRLEGEpePVSEERRVRRK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 933519334 97 NGREVWVEATYNPILDSGGRPcKVIKIATDVTERQKINADL 137
Cdd:TIGR00229 85 DGSEIWVEVSVSPIRTNGGEL-GVVGIVRDITERKEAEEAL 124
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
156-251 |
1.99e-12 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 63.25 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 156 DGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRigKGGRVAWIQASYNPVFDD 235
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDS-ERLREALREGKAVREFEVVLYR--KDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 933519334 236 AGRLCKIVKFATDITE 251
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
25-127 |
3.69e-12 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 62.65 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 25 SQAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDQAEQNsTAYREFWDRLKRGEFQRALYKRIGKNGREVWVE 104
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 933519334 105 ATYNPILDSGGRPCKVIKIATDV 127
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
22-130 |
1.45e-11 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 61.28 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 22 LNHS-QAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDQAEQnsTAYREFWDRLKRGEFQRALYKRIGKNGRE 100
Cdd:pfam08448 1 LDSLpDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDA--ARLERALRRALEGEEPIDFLEELLLNGEE 78
|
90 100 110
....*....|....*....|....*....|
gi 933519334 101 VWVEATYNPILDSGGRPCKVIKIATDVTER 130
Cdd:pfam08448 79 RHYELRLTPLRDPDGEVIGVLVISRDITER 108
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
149-259 |
1.30e-10 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 58.84 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 149 AVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDgAAYREFWRTLNKGQFEAAQYRRIG-KGGRVAWIQA 227
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE-EVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEV 93
|
90 100 110
....*....|....*....|....*....|..
gi 933519334 228 SYNPVFDDAGRLcKIVKFATDITEQVRLLERL 259
Cdd:TIGR00229 94 SVSPIRTNGGEL-GVVGIVRDITERKEAEEAL 124
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
16-152 |
6.13e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 57.55 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 16 KAILSALNHsqAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIdqaEQNSTAYREFWDRLKRGE-FQRALYKRI 94
Cdd:COG3852 10 RAILDSLPD--AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELF---PEDSPLRELLERALAEGQpVTEREVTLR 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 933519334 95 GKNGREVWVEATYNPILDSGGRPCKVIkIATDVTERQKINADLRgkveALSRSQAVIE 152
Cdd:COG3852 85 RKDGEERPVDVSVSPLRDAEGEGGVLL-VLRDITERKRLERELR----RAEKLAAVGE 137
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
149-262 |
3.60e-08 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 55.24 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 149 AVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDGAAyreFWRTLNKGQ-FEAAQYRRIGKGGRVAWIQA 227
Cdd:COG3852 19 AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLREL---LERALAEGQpVTEREVTLRRKDGEERPVDV 95
|
90 100 110
....*....|....*....|....*....|....*
gi 933519334 228 SYNPVFDDAGRLCkIVKFATDITEQVRLLERLKLL 262
Cdd:COG3852 96 SVSPLRDAEGEGG-VLLVLRDITERKRLERELRRA 129
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
1-260 |
8.85e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 54.68 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 1 MIGFMRAIKGKGSDSKAILSALNHSQAVIEF---AIDGTILDANPNFL--------------TVMGYTLP--------EI 55
Cdd:PRK13560 310 LVGAITDISGRRAAERELLEKEDMLRAIIEAapiAAIGLDADGNICFVnnnaaermlgwsaaEVMGKPLPgmdpelneEF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 56 VGHHHRMFIDQAEQNSTAYREFWDRLKRGE-FQRALYKRIGKNGREVWVEATYNPILDSGGRPCKVIKIATDVTERQKIN 134
Cdd:PRK13560 390 WCGDFQEWYPDGRPMAFDACPMAKTIKGGKiFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 135 ADLRGKVEALSRSQAVI---EFNPDGTVITANENFLKvLGYSLDE-VRG-RHHSMFVDPGERDGAAyREFWRTLNKG--Q 207
Cdd:PRK13560 470 EQLLLANLIVENSPLVLfrwKAEEGWPVELVSKNITQ-FGYEPDEfISGkRMFAAIIHPADLEQVA-AEVAEFAAQGvdR 547
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 933519334 208 FEAaQYRRIGKGGRVAWIQASYNPVFDDAGRLCKIVKFATDITEQVRLLERLK 260
Cdd:PRK13560 548 FEQ-EYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIK 599
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
155-303 |
2.24e-07 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 53.30 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 155 PDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGErDGAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQASYNPVFD 234
Cdd:PRK13558 169 PDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDT-NEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933519334 235 DAGRLCKIVKFATDITEQVRL---LERLKLLIDTNFGEIEKAMGSAHQRADAAAVASTETRATVQTIAAGAE 303
Cdd:PRK13558 248 EDGTVTHYVGFQTDVTERKEAelaLQRERRKLQRLLERVEGLVNDVTSALVRATDREEIEAAVCDRVGAGGE 319
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
148-258 |
3.28e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 52.85 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 148 QAVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDGAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQA 227
Cdd:PRK11359 147 RPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKA 226
|
90 100 110
....*....|....*....|....*....|...
gi 933519334 228 SYNPVFDDAGRLCKIVKFATDITE--QVRLLER 258
Cdd:PRK11359 227 SISPVYDVLAHLQNLVMTFSDITEerQIRQLEG 259
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
149-249 |
2.10e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 46.64 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 149 AVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERDGAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQAS 228
Cdd:pfam00989 13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVR 92
|
90 100
....*....|....*....|.
gi 933519334 229 YNPVFDDAGRLCKIVKFATDI 249
Cdd:pfam00989 93 ASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
19-127 |
4.52e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 45.49 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 19 LSALNHSQAVIEFAID--GTILDANPNFLTVMGYTLPEIVGhhhRMFIDQ--AEQNSTAYREFWDRLKRGEFQRALYKRI 94
Cdd:pfam00989 3 LRAILESLPDGIFVVDedGRILYVNAAAEELLGLSREEVIG---KSLLDLipEEDDAEVAELLRQALLQGEESRGFEVSF 79
|
90 100 110
....*....|....*....|....*....|....
gi 933519334 95 -GKNGREVWVEATYNPILDSGGRPCKVIKIATDV 127
Cdd:pfam00989 80 rVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
13-170 |
1.97e-05 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 47.07 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 13 SDSKAILSALNHSQAVIeFAID--GTILDANPNFLTVMGYTLPEIVGHHhrmfIDQAEQNSTAYRefwdRLKRGEFQRAL 90
Cdd:COG3829 8 ELEEELEAILDSLDDGI-IVVDadGRITYVNRAAERILGLPREEVIGKN----VTELIPNSPLLE----VLKTGKPVTGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 91 YKRIGKNGREVWVEATynPILDsGGRPCKVIKIATDVTERQKINADLRgKVEALSRSQAVIEFNpdgTVITANENFLKVL 170
Cdd:COG3829 79 IQKTGGKGKTVIVTAI--PIFE-DGEVIGAVETFRDITELKRLERKLR-EEELERGLSAKYTFD---DIIGKSPAMKELL 151
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
3-261 |
1.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 44.66 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 3 GFMRAIKGKGSDSKAILSALNHSQAVIE--------FAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFI------DQAE 68
Cdd:PRK13560 184 GFAEDITERKRAEERIDEALHFLQQLLDniadpafwKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFApaqpadDYQE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 69 QNSTAYREFWDRLKRGEFQRalykrigKNGREVWVEATYNPI--LDSGGRPCKVIKIATDVTERQKINADLRgkvEALSR 146
Cdd:PRK13560 264 ADAAKFDADGSQIIEAEFQN-------KDGRTRPVDVIFNHAefDDKENHCAGLVGAITDISGRRAAERELL---EKEDM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 147 SQAVIEFNP--------DGTVITANENFL-KVLGYSLDEVRGRHHSMfVDPGERD---GAAYREFWRTLNKGQFEAAQYR 214
Cdd:PRK13560 334 LRAIIEAAPiaaigldaDGNICFVNNNAAeRMLGWSAAEVMGKPLPG-MDPELNEefwCGDFQEWYPDGRPMAFDACPMA 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933519334 215 RIGKGGRV---------------AWIQASYNPVFDDAGRLCKIVKFATDITEQVRLLERLKL 261
Cdd:PRK13560 413 KTIKGGKIfdgqevliereddgpADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLL 474
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
155-380 |
1.48e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 44.04 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 155 PDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGErDGAAYREFWRTLNKGQF---EAAQYRrigKGGRVAWIQASYNP 231
Cdd:PRK13559 64 PDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAAT-DPIAVAKIRAAIAAEREivvELLNYR---KDGEPFWNALHLGP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 232 VFDDAGRLCKIVKFATDITE--QVRLLERlkllidtnfGEIEKAMGSAHQRADAAAVASTETRATvqTIAAGAEEMASSA 309
Cdd:PRK13559 140 VYGEDGRLLYFFGSQWDVTDirAVRALEA---------HERRLAREVDHRSKNVFAVVDSIVRLT--GRADDPSLYAAAI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 310 QEIANSMTRSQQA-------ADIAMNEAENADRA--AARLTEVAKAMGGI---VELIRSIAGQINMLALNATIEAARAGE 377
Cdd:PRK13559 209 QERVQALARAHETlldergwETVEVEELIRAQVApyAPRATRVAFEGPGIrlgAASVQPLGLVLHELAVNAIKHGALSAD 288
|
...
gi 933519334 378 AGR 380
Cdd:PRK13559 289 QGR 291
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
147-192 |
1.91e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 39.69 E-value: 1.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 933519334 147 SQAVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPGERD 192
Cdd:smart00091 11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRE 56
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
149-259 |
2.93e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 43.42 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 149 AVIEFNPDGTVITANENFLKVLGYSLDEVRGRHHSMFVDPgerDGAAYREFWRTLNKGQFEAAQYRRIGKGGRVAWIQAS 228
Cdd:PRK11360 274 GVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPP---NTPFASPLLDTLEHGTEHVDLEISFPGRDRTIELSVS 350
|
90 100 110
....*....|....*....|....*....|.
gi 933519334 229 YNPVFDDAGRLCKIVKFATDITEQVRLLERL 259
Cdd:PRK11360 351 TSLLHNTHGEMIGALVIFSDLTERKRLQRRV 381
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
26-152 |
3.25e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 43.29 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 26 QAVIEFAIDGTILDA----------NPNFLTVMGYTLPEIVGHHHRmFIDQAEQNSTAYREFWDRLKRGEFQRALYKRIG 95
Cdd:PRK13558 152 RALDEAPVGITIADAtlpdepliyiNDAFERITGYSPDEVLGRNCR-FLQGEDTNEERVAELREAIDEERPTSVELRNYR 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 933519334 96 KNGREVWVEATYNPILDSGGRPCKVIKIATDVTERQKINADLRGKVEALSRSQAVIE 152
Cdd:PRK13558 231 KDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKLQRLLERVE 287
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
18-143 |
4.25e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 42.83 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 18 ILSALNHS-QAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHHHRMFIDQAEQNSTAYREFWDRL-KRGEFQRALYKRIg 95
Cdd:PRK11359 138 LIIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLwKTARDQDEFLLLT- 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 933519334 96 KNGREVWVEATYNPILDSGGRPCKVIKIATDVTERQKINaDLRGKVEA 143
Cdd:PRK11359 217 RTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIR-QLEGNILA 263
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
212-252 |
4.54e-04 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 37.93 E-value: 4.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 933519334 212 QYRRIGKGGRVAWIQASYNPVFDDAGRLCKIVKFATDITEQ 252
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
91-130 |
1.54e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.39 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 933519334 91 YKRIGKNGREVWVEATYNPILDSGGRPCKVIKIATDVTER 130
Cdd:smart00086 4 YRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
270-492 |
1.64e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 40.77 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 270 IEKAMGSAHQRADAAAVASTETRATVQTIAAGAEEMASSAQEIANSMTRSQQAADIAMNEAENADRAAARLTEVAKAMGG 349
Cdd:COG0840 126 ALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933519334 350 IVELIRSIAGQINMLA---LNATIEAARAGEAGR----------GFAVVANEVKNLANQSANATAQISREIDGMQSVSHD 416
Cdd:COG0840 206 ITRPLRELLEVLERIAegdLTVRIDVDSKDEIGQladafnrmieNLRELVGQVRESAEQVASASEELAASAEELAAGAEE 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933519334 417 VVSSLGTIRSAMNNLREFVVMSAGAVEEQTTVTSSMSANMQEASTSVEVVDRNIGAIATAFAQVGSAIAETKDAAR 492
Cdd:COG0840 286 QAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQ 361
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
17-59 |
2.77e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 36.22 E-value: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 933519334 17 AILSALNhsQAVIEFAIDGTILDANPNFLTVMGYTLPEIVGHH 59
Cdd:smart00091 5 AILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
|
|
| |
