|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
253-431 |
2.49e-46 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 167.50 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 253 TERMSRN-RAVTEAAAIAHESAVSTVKTAVLGSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVSTISSIADQ 331
Cdd:COG0840 297 MEELSATvQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 332 TNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRELISEVSD 411
Cdd:COG0840 377 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGE 456
|
170 180
....*....|....*....|
gi 2569300571 412 VIKDIEAGAEKVSEIVSQLN 431
Cdd:COG0840 457 ALEEIVEAVEEVSDLIQEIA 476
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
249-431 |
8.54e-46 |
|
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: 158.99 E-value: 8.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 249 ASDITERMSRNRAVTEAAAIAHESAVSTVKTAVL----GSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVST 324
Cdd:smart00283 20 LEELAERMEELSASIEEVAANADEIAATAQSAAEaaeeGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 325 ISSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRE 404
Cdd:smart00283 100 IDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVE 179
|
170 180
....*....|....*....|....*..
gi 2569300571 405 LISEVSDVIKDIEAGAEKVSEIVSQLN 431
Cdd:smart00283 180 LVEETGDALEEIVDSVEEIADLVQEIA 206
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
262-432 |
1.84e-45 |
|
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: 156.24 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 262 VTEAAAIAHESAVSTVKTAVLGSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVSTISSIADQTNLLALNAAI 341
Cdd:cd11386 10 VAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 342 EAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRELISEVSDVIKDIEAGAE 421
Cdd:cd11386 90 EAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVE 169
|
170
....*....|.
gi 2569300571 422 KVSEIVSQLNV 432
Cdd:cd11386 170 EVADGIQEISA 180
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
298-430 |
3.76e-31 |
|
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: 117.53 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 298 VNQVLKSVELIknlNEQSAVIGSIVSTISSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATV 377
Cdd:pfam00015 18 VANVVGQMEQI---AQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEAL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2569300571 378 VKNNQELTNDISKQITSVSDSSVKGRELISEVSDVIKDIEAGAEKVSEIVSQL 430
Cdd:pfam00015 95 IIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
12-255 |
2.67e-25 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 103.95 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 12 EALELQVAQKESVLNAItkHVAYIEFTAEGIILDANLLFLNTVDYTKDDVVGHHHRMFCEKSYAESkEYTQFWKNLRDGK 91
Cdd:COG2202 4 EALEESERRLRALVESS--PDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 92 SVSGSFLRYNSQGEKIWLEATYFPV-EIDGVVVKVIKIASDITAnytQRKAQEAVAEALSKALATIEFTP--------QG 162
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVrDEDGEITGFVGIARDITE---RKRAEEALRESEERLRLLVENAPdgifvldlDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 163 EILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFWDELGKGQFKSGQ--FKRVKANGDIIWLEATYNPILDNkG 240
Cdd:COG2202 158 RILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYEleLRLKDGDGRWVWVEASAVPLRDG-G 236
|
250
....*....|....*
gi 2569300571 241 NVIKVIKFASDITER 255
Cdd:COG2202 237 EVIGVLGIVRDITER 251
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
250-431 |
3.34e-23 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 102.07 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 250 SDITERMSRNRAVTEAAAIAHESAVSTV----KTAVLGSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVSTI 325
Cdd:PRK09793 285 NDLSSRTEQQAASLAQTAASMEQLTATVgqnaDNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 326 SSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATV-------VKNNQELTNDISKQITSVSDS 398
Cdd:PRK09793 365 DGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLieesvnrVQQGSKLVNNAAATMTDIVSS 444
|
170 180 190
....*....|....*....|....*....|...
gi 2569300571 399 SVKGRELISEVSDVIKDIEAGAEKVSEIVSQLN 431
Cdd:PRK09793 445 VTRVNDIMGEIASASEEQRRGIEQVAQAVSQMD 477
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
164-249 |
1.78e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 65.82 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 164 ILTANNNFLSATGYKLNEIIG--EHHRMFCTDEfyDKNP---HFWDELGKGQFKSGQFKRVKANGDIIWLEATYNPILDN 238
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPD--DRERvreALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|.
gi 2569300571 239 KGNVIKVIKFA 249
Cdd:pfam08447 79 NGKPVRVIGVA 89
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
21-144 |
4.29e-08 |
|
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: 51.52 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 21 KESVLNAITKH--VAYIEFTAEGIILDANLLFLNTVDYTKDDVVGHHHRM-FCEKSYAESKEYtqFWKNLRDGKSVSGSF 97
Cdd:TIGR00229 1 SEERYRAIFESspDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLElIPEEDREEVRER--IERRLEGEPEPVSEE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2569300571 98 LRY-NSQGEKIWLEATYFPVEIDGVVVKVIKIASDItanyTQRK-AQEA 144
Cdd:TIGR00229 79 RRVrRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDI----TERKeAEEA 123
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
154-252 |
7.25e-07 |
|
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: 47.24 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 154 ATIEFTPQGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFW-DELGKGQFKSGQFKRVKANGDIIWLEATY 232
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLeNLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83
|
90 100
....*....|....*....|
gi 2569300571 233 NPILDNKGNVIKVIKFASDI 252
Cdd:cd00130 84 TPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
127-264 |
1.48e-06 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 50.61 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 127 KIASDITANYTQRKAQEAVAEA---LSKALATIEFTPqgeILTANNNFLSATGYKLNEIIGEHHRmFCTDEFYDKNP--H 201
Cdd:PRK13558 136 MPISDLTVESDRRLKERALDEApvgITIADATLPDEP---LIYINDAFERITGYSPDEVLGRNCR-FLQGEDTNEERvaE 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569300571 202 FWDELGKGQFKSGQFKRVKANGDIIWLEATYNPILDNKGNVIKVIKFASDITERMSRNRAVTE 264
Cdd:PRK13558 212 LREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQR 274
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
213-255 |
1.29e-05 |
|
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: 42.17 E-value: 1.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2569300571 213 SGQFKRVKANGDIIWLEATYNPILDNKGNVIKVIKFASDITER 255
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
253-431 |
2.49e-46 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 167.50 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 253 TERMSRN-RAVTEAAAIAHESAVSTVKTAVLGSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVSTISSIADQ 331
Cdd:COG0840 297 MEELSATvQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 332 TNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRELISEVSD 411
Cdd:COG0840 377 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGE 456
|
170 180
....*....|....*....|
gi 2569300571 412 VIKDIEAGAEKVSEIVSQLN 431
Cdd:COG0840 457 ALEEIVEAVEEVSDLIQEIA 476
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
249-431 |
8.54e-46 |
|
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: 158.99 E-value: 8.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 249 ASDITERMSRNRAVTEAAAIAHESAVSTVKTAVL----GSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVST 324
Cdd:smart00283 20 LEELAERMEELSASIEEVAANADEIAATAQSAAEaaeeGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 325 ISSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRE 404
Cdd:smart00283 100 IDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVE 179
|
170 180
....*....|....*....|....*..
gi 2569300571 405 LISEVSDVIKDIEAGAEKVSEIVSQLN 431
Cdd:smart00283 180 LVEETGDALEEIVDSVEEIADLVQEIA 206
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
262-432 |
1.84e-45 |
|
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: 156.24 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 262 VTEAAAIAHESAVSTVKTAVLGSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVSTISSIADQTNLLALNAAI 341
Cdd:cd11386 10 VAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 342 EAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRELISEVSDVIKDIEAGAE 421
Cdd:cd11386 90 EAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVE 169
|
170
....*....|.
gi 2569300571 422 KVSEIVSQLNV 432
Cdd:cd11386 170 EVADGIQEISA 180
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
298-430 |
3.76e-31 |
|
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: 117.53 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 298 VNQVLKSVELIknlNEQSAVIGSIVSTISSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATV 377
Cdd:pfam00015 18 VANVVGQMEQI---AQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEAL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2569300571 378 VKNNQELTNDISKQITSVSDSSVKGRELISEVSDVIKDIEAGAEKVSEIVSQL 430
Cdd:pfam00015 95 IIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
12-255 |
2.67e-25 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 103.95 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 12 EALELQVAQKESVLNAItkHVAYIEFTAEGIILDANLLFLNTVDYTKDDVVGHHHRMFCEKSYAESkEYTQFWKNLRDGK 91
Cdd:COG2202 4 EALEESERRLRALVESS--PDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 92 SVSGSFLRYNSQGEKIWLEATYFPV-EIDGVVVKVIKIASDITAnytQRKAQEAVAEALSKALATIEFTP--------QG 162
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVrDEDGEITGFVGIARDITE---RKRAEEALRESEERLRLLVENAPdgifvldlDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 163 EILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFWDELGKGQFKSGQ--FKRVKANGDIIWLEATYNPILDNkG 240
Cdd:COG2202 158 RILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYEleLRLKDGDGRWVWVEASAVPLRDG-G 236
|
250
....*....|....*
gi 2569300571 241 NVIKVIKFASDITER 255
Cdd:COG2202 237 EVIGVLGIVRDITER 251
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
250-431 |
3.34e-23 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 102.07 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 250 SDITERMSRNRAVTEAAAIAHESAVSTV----KTAVLGSGILSDSIANSDAIVNQVLKSVELIKNLNEQSAVIGSIVSTI 325
Cdd:PRK09793 285 NDLSSRTEQQAASLAQTAASMEQLTATVgqnaDNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 326 SSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATV-------VKNNQELTNDISKQITSVSDS 398
Cdd:PRK09793 365 DGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLieesvnrVQQGSKLVNNAAATMTDIVSS 444
|
170 180 190
....*....|....*....|....*....|...
gi 2569300571 399 SVKGRELISEVSDVIKDIEAGAEKVSEIVSQLN 431
Cdd:PRK09793 445 VTRVNDIMGEIASASEEQRRGIEQVAQAVSQMD 477
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
250-430 |
1.41e-21 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 97.00 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 250 SDITERMSRNRAVTEAAAIAHESAVSTVK----TAVLGSGIL---SDSIANSDAIVNQVLKSVELIKnlnEQSAVIGSIV 322
Cdd:PRK15048 287 TDLSSRTEQQASALEETAASMEQLTATVKqnadNARQASQLAqsaSDTAQHGGKVVDGVVKTMHEIA---DSSKKIADII 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 323 STISSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKG 402
Cdd:PRK15048 364 SVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNI 443
|
170 180
....*....|....*....|....*...
gi 2569300571 403 RELISEVSDVIKDIEAGAEKVSEIVSQL 430
Cdd:PRK15048 444 VNAVTRVTDIMGEIASASDEQSRGIDQV 471
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
250-430 |
3.68e-20 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 92.71 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 250 SDITERMSRNRAVTEAAAIAHESAVSTVK----TAVLGSGIL---SDSIANSDAIVNQVlksVELIKNLNEQSAVIGSIV 322
Cdd:PRK15041 289 NDLSSRTEQQAASLEETAASMEQLTATVKqnaeNARQASHLAlsaSETAQRGGKVVDNV---VQTMRDISTSSQKIADII 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 323 STISSIADQTNLLALNAAIEAARAGEYGRGFAVVADEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKG 402
Cdd:PRK15041 366 SVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEI 445
|
170 180
....*....|....*....|....*...
gi 2569300571 403 RELISEVSDVIKDIEAGAEKVSEIVSQL 430
Cdd:PRK15041 446 VSAVTRVTDIMGEIASASDEQSRGIDQV 473
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
137-255 |
3.64e-16 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 78.14 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 137 TQRKAQEAVAEALSKAL-----ATIEFTPQGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDK-NPHFWDELGKGQ 210
Cdd:COG2202 1 TAEEALEESERRLRALVesspdAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEfLELLRAALAGGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2569300571 211 FKSGQFKRVKANGDIIWLEATYNPILDNKGNVIKVIKFASDITER 255
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITER 125
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
164-249 |
1.78e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 65.82 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 164 ILTANNNFLSATGYKLNEIIG--EHHRMFCTDEfyDKNP---HFWDELGKGQFKSGQFKRVKANGDIIWLEATYNPILDN 238
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPD--DRERvreALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|.
gi 2569300571 239 KGNVIKVIKFA 249
Cdd:pfam08447 79 NGKPVRVIGVA 89
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
161-254 |
2.85e-10 |
|
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: 56.70 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 161 QGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPH-FWDElgKGQFKSGQFKRVKANGDIIWLEATYNPILDNK 239
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLReALRE--GKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
|
90
....*....|....*
gi 2569300571 240 GNVIKVIKFASDITE 254
Cdd:pfam13426 79 GELVGIIAILRDITE 93
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
21-144 |
4.29e-08 |
|
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: 51.52 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 21 KESVLNAITKH--VAYIEFTAEGIILDANLLFLNTVDYTKDDVVGHHHRM-FCEKSYAESKEYtqFWKNLRDGKSVSGSF 97
Cdd:TIGR00229 1 SEERYRAIFESspDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLElIPEEDREEVRER--IERRLEGEPEPVSEE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2569300571 98 LRY-NSQGEKIWLEATYFPVEIDGVVVKVIKIASDItanyTQRK-AQEA 144
Cdd:TIGR00229 79 RRVrRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDI----TERKeAEEA 123
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
40-134 |
4.82e-08 |
|
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: 50.54 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 40 EGIILDANLLFLNTVDYTKDDVVGHHHRMFCEKSYAESKEYtQFWKNLRDGKSVSGSFLRYNsqGEKIWLEATYFPVEID 119
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLR-EALREGKAVREFEVVLYRKD--GEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 2569300571 120 -GVVVKVIKIASDITA 134
Cdd:pfam13426 78 gGELVGIIAILRDITE 93
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
154-255 |
2.32e-07 |
|
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: 48.95 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 154 ATIEFTPQGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFWDELGKGQFKSGQFKRVKANGDIIWLEATYN 233
Cdd:pfam08448 7 ALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYELRLT 86
|
90 100
....*....|....*....|..
gi 2569300571 234 PILDNKGNVIKVIKFASDITER 255
Cdd:pfam08448 87 PLRDPDGEVIGVLVISRDITER 108
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
154-255 |
2.47e-07 |
|
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: 49.21 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 154 ATIEFTPQGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFWDEL--GKGQFKSGQFKRVKANGDIIWLEAT 231
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRleGEPEPVSEERRVRRKDGSEIWVEVS 94
|
90 100
....*....|....*....|....
gi 2569300571 232 YNPILDNkGNVIKVIKFASDITER 255
Cdd:TIGR00229 95 VSPIRTN-GGELGVVGIVRDITER 117
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
154-252 |
7.25e-07 |
|
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: 47.24 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 154 ATIEFTPQGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFW-DELGKGQFKSGQFKRVKANGDIIWLEATY 232
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLeNLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83
|
90 100
....*....|....*....|
gi 2569300571 233 NPILDNKGNVIKVIKFASDI 252
Cdd:cd00130 84 TPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
161-252 |
1.12e-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: 47.03 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 161 QGEILTANNNFLSATGYKLNEIIGEH--HRMFCTDEFYDKNPHFWDELGKGQFKSGQFKRVKANGDIIWLEATYNPILDN 238
Cdd:pfam00989 20 DGRILYVNAAAEELLGLSREEVIGKSllDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVRASPVRDA 99
|
90
....*....|....
gi 2569300571 239 KGNVIKVIKFASDI 252
Cdd:pfam00989 100 GGEILGFLGVLRDI 113
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
127-264 |
1.48e-06 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 50.61 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 127 KIASDITANYTQRKAQEAVAEA---LSKALATIEFTPqgeILTANNNFLSATGYKLNEIIGEHHRmFCTDEFYDKNP--H 201
Cdd:PRK13558 136 MPISDLTVESDRRLKERALDEApvgITIADATLPDEP---LIYINDAFERITGYSPDEVLGRNCR-FLQGEDTNEERvaE 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569300571 202 FWDELGKGQFKSGQFKRVKANGDIIWLEATYNPILDNKGNVIKVIKFASDITERMSRNRAVTE 264
Cdd:PRK13558 212 LREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQR 274
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
213-255 |
1.29e-05 |
|
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: 42.17 E-value: 1.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2569300571 213 SGQFKRVKANGDIIWLEATYNPILDNKGNVIKVIKFASDITER 255
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
142-271 |
1.51e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 46.76 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 142 QEAVAEALSKALATIEftPQGEILTANNNFLSATGYKLNEIIGEHhrmfCTDEFYDKNPH---FWDELGKGQ-FKSGQFK 217
Cdd:COG3852 9 LRAILDSLPDAVIVLD--ADGRITYVNPAAERLLGLSAEELLGRP----LAELFPEDSPLrelLERALAEGQpVTEREVT 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569300571 218 RVKANGDIIWLEATYNPILDNKGNvIKVIKFASDITE---------RMSRNRAVTEAAA-IAHE 271
Cdd:COG3852 83 LRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITErkrlerelrRAEKLAAVGELAAgLAHE 145
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
11-189 |
2.45e-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: 46.30 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 11 IEALELQVAQK--ESVLNAItkHVAYIEFTAEGIILDANLLFLNTVDYTKDDVVGHHhrmfCEKSYAESKeytqFWKNLR 88
Cdd:COG3829 1 AEELELKELEEelEAILDSL--DDGIIVVDADGRITYVNRAAERILGLPREEVIGKN----VTELIPNSP----LLEVLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 89 DGKSVSGSFLRYNsqGEKIWLEATYFPVEIDGVVVKVIKIASDITAnyTQRKAQEAVAEALSKALatieftpqgeiltan 168
Cdd:COG3829 71 TGKPVTGVIQKTG--GKGKTVIVTAIPIFEDGEVIGAVETFRDITE--LKRLERKLREEELERGL--------------- 131
|
170 180
....*....|....*....|.
gi 2569300571 169 nnflsATGYKLNEIIGEHHRM 189
Cdd:COG3829 132 -----SAKYTFDDIIGKSPAM 147
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
50-129 |
2.59e-05 |
|
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: 42.71 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 50 FLNTVDYTKDDVVG--HHHRMFCEKSYAEsKEYTQFWKNLRDGKSVSGSFLRYNSQGEKIWLEATYFPV-EIDGVVVKVI 126
Cdd:pfam08447 8 FEEILGYTPEELLGkgESWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIrDENGKPVRVI 86
|
...
gi 2569300571 127 KIA 129
Cdd:pfam08447 87 GVA 89
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
218-431 |
2.65e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 46.55 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 218 RVKANGDIIWLEATYNPILDNKGNVIKVIKFASDITERMSRNRAVTEAAAIAHESAVSTVKTAVLGSGILSDSIANSDAI 297
Cdd:COG0840 133 ALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 298 VNQVLKSV------------------ELIKNLNEQSAVIGSIVSTISSIADQTNLLA--LNAAIEAARAGeygrgfavvA 357
Cdd:COG0840 213 LLEVLERIaegdltvridvdskdeigQLADAFNRMIENLRELVGQVRESAEQVASASeeLAASAEELAAG---------A 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569300571 358 DEVRQLAARTSSSTNEIATVVKNNQELTNDISKQITSVSDSSVKGRELISEVSDVIKDIEAGAEKVSEIVSQLN 431
Cdd:COG0840 284 EEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELG 357
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
1-152 |
3.06e-05 |
|
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: 46.12 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 1 MFGINKSNSKIEALELQVAQKESVLNAITKHVAY--IEFTAEGIILDANLLFLNTVDYTKDDVVGHHHRMFCEKSYAEsK 78
Cdd:COG5809 119 MLAISRDITERKRMEEALRESEEKFRLIFNHSPDgiIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQE-N 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569300571 79 EYTQFWKNLRDGKSVSGSFLRYNSQGEKIWLEATYFPVEIDGVVVKVIKIASDITanyTQRKAQEAV--AEALSKA 152
Cdd:COG5809 198 VAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDIT---ERKKLEELLrkSEKLSVV 270
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
160-271 |
2.31e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 43.42 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 160 PQGEILTANNNFLSATGYKLNEIIGEHHRmfctdEFYDKNPHFW----DELGKGQFKSGQFKRVKANGDIIWLEATYNPI 235
Cdd:PRK11360 280 RQGKITTMNPAAEVITGLQRHELVGKPYS-----ELFPPNTPFAspllDTLEHGTEHVDLEISFPGRDRTIELSVSTSLL 354
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2569300571 236 LDNKGNVIKVIKFASDITERMSRNRAVTEA----------AAIAHE 271
Cdd:PRK11360 355 HNTHGEMIGALVIFSDLTERKRLQRRVARQerlaalgelvAGVAHE 400
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
31-132 |
3.02e-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. 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: 39.92 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 31 HVAYIEFTAEGIILDANLLFLNTVDYTKDDVVGHHHRMFCEKSYAEsKEYTQFWKNLRDGKSVSGSFLRYNSQGEKIWLE 110
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 2569300571 111 ATYFPVEI-DGVVVKVIKIASDI 132
Cdd:cd00130 81 VSLTPIRDeGGEVIGLLGVVRDI 103
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
161-309 |
5.09e-04 |
|
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: 42.07 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 161 QGEILTANNNFLSATGYKLNEIIGEHhrmfCTDEFydKNPHFWDELGKGQFKSGQFkrVKANGDIIWLEATYNPILDNkG 240
Cdd:COG3829 30 DGRITYVNRAAERILGLPREEVIGKN----VTELI--PNSPLLEVLKTGKPVTGVI--QKTGGKGKTVIVTAIPIFED-G 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569300571 241 NVIKVIKFASDITERMSRNRAVTEAAAIAHESAVSTvktavlgsgiLSDSIANSDAIvnqvLKSVELIK 309
Cdd:COG3829 101 EVIGAVETFRDITELKRLERKLREEELERGLSAKYT----------FDDIIGKSPAM----KELLELAK 155
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
104-310 |
1.82e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 40.52 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 104 GEKIWLEATYFPVEIDGVVVKvIKIASDITANYTQRKAQEAVAEALSKA-LATIEFTPQGEILTANNNFLSATGYKLNEI 182
Cdd:PRK11359 98 GSKIWTRFALSKVSAEGKVYY-LALVRDASVEMAQKEQTRQLIIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 183 IGEHHRMFCT------DEFYDKNPHFWdelGKGQFKSgQFKRVKANGDIIWLEATYNPILDNK---GNVIKVIkfaSDIT 253
Cdd:PRK11359 177 SGMQPDTLLNipefpaDNRIRLQQLLW---KTARDQD-EFLLLTRTGEKIWIKASISPVYDVLahlQNLVMTF---SDIT 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2569300571 254 -ERMSRNRAVTEAAAIahesaVSTVKTAVLGSGILSdsiaNSDAIVNQVLKSVELIKN 310
Cdd:PRK11359 250 eERQIRQLEGNILAAM-----CSSPPFHEMGEIICR----NIESVLNESHVSLFALRN 298
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
143-255 |
8.40e-03 |
|
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: 38.56 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569300571 143 EAVAEALSKALATIEFtpQGEILTANNNFLSATGYKLNEIIGEHHRMFCTDEFYDKNPHFWDELGKGQFKSGQFKRVKAN 222
Cdd:COG5805 37 ETILENLPDAIIAVNR--EGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKD 114
|
90 100 110
....*....|....*....|....*....|...
gi 2569300571 223 GDIIWLEATYNPILDNKGNVIkvIKFASDITER 255
Cdd:COG5805 115 GELIYVEVKLFPIYNQNGQAA--ILALRDITKK 145
|
|
| |
