|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
237-408 |
1.04e-46 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 167.89 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 237 RNVYHLSLSTDRSASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHA 316
Cdd:COG0840 312 QQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 317 GEHGKGFSVVASEVRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKL 396
Cdd:COG0840 392 GEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDL 471
|
170
....*....|..
gi 1206439776 397 MTAFAQVKNQQT 408
Cdd:COG0840 472 IQEIAAASEEQS 483
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
250-408 |
1.32e-43 |
|
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: 150.85 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 250 ASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASE 329
Cdd:cd11386 28 AEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADE 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206439776 330 VRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:cd11386 108 VRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQS 186
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
250-408 |
1.41e-42 |
|
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: 150.13 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 250 ASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASE 329
Cdd:smart00283 55 AEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADE 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206439776 330 VRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:smart00283 135 VRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQA 213
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
1-230 |
6.60e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 129.76 E-value: 6.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYvLSEPYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTY 80
Cdd:COG2202 24 IIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 81 TPVLDNQGRVVEIIKIAHDVTER------ILQSQEHQSLLeALNRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKS 154
Cdd:COG2202 103 SPVRDEDGEITGFVGIARDITERkraeeaLRESEERLRLL-VENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1206439776 155 HQMLCTPEFAhsDDYYQHWQRLARGEFILGRFE--RVNSRGQRVWLEASYNPImDNEGQVFKVVKIAQDITQLMLQQE 230
Cdd:COG2202 182 LLDLLHPEDR--ERLLELLRRLLEGGRESYELElrLKDGDGRWVWVEASAVPL-RDGGEVIGVLGIVRDITERKRAEE 256
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
241-407 |
1.28e-29 |
|
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: 112.91 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 241 HLSLSTDRSASQGAEIVQQAVRGMQEVEsiaretsdvvsdlgRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHG 320
Cdd:pfam00015 2 DLAQLASEEAQDGGKEVANVVGQMEQIA--------------QSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 321 KGFSVVASEVRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKLMTAF 400
Cdd:pfam00015 68 RGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147
|
....*..
gi 1206439776 401 AQVKNQQ 407
Cdd:pfam00015 148 AAASDEQ 154
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
209-408 |
1.74e-21 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 96.56 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 209 EGQVFKVVKIAQDITQLMLQQEHEENLIRNVYHLSLSTDRSASQGAEIVQQAVRGMQevesiaretsdvvsDLGRCSQEI 288
Cdd:PRK15041 296 EQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMR--------------DISTSSQKI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 289 GTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASEVRLLAEHSRKAATEIEQMTKtiqhgvmaaikgmgTCVEQ 368
Cdd:PRK15041 362 ADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIE--------------DSVGK 427
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1206439776 369 AGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:PRK15041 428 VDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQS 467
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
12-97 |
2.02e-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: 65.44 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 12 HANTLFLQAMGYQQNEVIGKHHKLFC-----DPQYVlsepYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTYTPVLDN 86
Cdd:pfam08447 3 YWSPRFEEILGYTPEELLGKGESWLDlvhpdDRERV----REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|.
gi 1206439776 87 QGRVVEIIKIA 97
Cdd:pfam08447 79 NGKPVRVIGVA 89
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
1-100 |
4.06e-11 |
|
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: 59.57 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYVLsEPYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTY 80
Cdd:cd00130 5 VIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83
|
90 100
....*....|....*....|
gi 1206439776 81 TPVLDNQGRVVEIIKIAHDV 100
Cdd:cd00130 84 TPIRDEGGEVIGLLGVVRDI 103
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
1-110 |
7.25e-11 |
|
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: 59.23 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHhklfcdPQYVLSEPYR-----RHWKLL-NEGRPITDNIKRIRKDGSII 74
Cdd:TIGR00229 16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRN------VLELIPEEDReevreRIERRLeGEPEPVSEERRVRRKDGSEI 89
|
90 100 110
....*....|....*....|....*....|....*.
gi 1206439776 75 WLQGTYTPVLDNQGRVVeIIKIAHDVTERILQSQEH 110
Cdd:TIGR00229 90 WVEVSVSPIRTNGGELG-VVGIVRDITERKEAEEAL 124
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
5-199 |
4.93e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 54.44 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 5 KPDGTVKHANTLFLQAMGYQQNEVIGKHHKLF----CDPQYVlsepyRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTY 80
Cdd:PRK13559 63 QPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLqgaaTDPIAV-----AKIRAAIAAEREIVVELLNYRKDGEPFWNALHL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 81 TPVLDNQGRVVEIIKIAHDVTE----RILQSQEHQSLLEALNRSMGMitfspqgiiLAANDNLLRVIGYSL------ADI 150
Cdd:PRK13559 138 GPVYGEDGRLLYFFGSQWDVTDiravRALEAHERRLAREVDHRSKNV---------FAVVDSIVRLTGRADdpslyaAAI 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1206439776 151 QHKShQMLCTPEFAHSDDyyQHWQRLARGEFILGRFERVNSRGQRVWLE 199
Cdd:PRK13559 209 QERV-QALARAHETLLDE--RGWETVEVEELIRAQVAPYAPRATRVAFE 254
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
67-103 |
8.34e-07 |
|
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: 45.25 E-value: 8.34e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1206439776 67 IRKDGSIIWLQGTYTPVLDNQGRVVEIIKIAHDVTER 103
Cdd:smart00086 7 RRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
237-408 |
1.04e-46 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 167.89 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 237 RNVYHLSLSTDRSASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHA 316
Cdd:COG0840 312 QQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 317 GEHGKGFSVVASEVRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKL 396
Cdd:COG0840 392 GEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDL 471
|
170
....*....|..
gi 1206439776 397 MTAFAQVKNQQT 408
Cdd:COG0840 472 IQEIAAASEEQS 483
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
250-408 |
1.32e-43 |
|
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: 150.85 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 250 ASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASE 329
Cdd:cd11386 28 AEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADE 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206439776 330 VRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:cd11386 108 VRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQS 186
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
250-408 |
1.41e-42 |
|
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: 150.13 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 250 ASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASE 329
Cdd:smart00283 55 AEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADE 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206439776 330 VRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:smart00283 135 VRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQA 213
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
1-230 |
6.60e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 129.76 E-value: 6.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYvLSEPYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTY 80
Cdd:COG2202 24 IIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 81 TPVLDNQGRVVEIIKIAHDVTER------ILQSQEHQSLLeALNRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKS 154
Cdd:COG2202 103 SPVRDEDGEITGFVGIARDITERkraeeaLRESEERLRLL-VENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1206439776 155 HQMLCTPEFAhsDDYYQHWQRLARGEFILGRFE--RVNSRGQRVWLEASYNPImDNEGQVFKVVKIAQDITQLMLQQE 230
Cdd:COG2202 182 LLDLLHPEDR--ERLLELLRRLLEGGRESYELElrLKDGDGRWVWVEASAVPL-RDGGEVIGVLGIVRDITERKRAEE 256
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
241-407 |
1.28e-29 |
|
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: 112.91 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 241 HLSLSTDRSASQGAEIVQQAVRGMQEVEsiaretsdvvsdlgRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHG 320
Cdd:pfam00015 2 DLAQLASEEAQDGGKEVANVVGQMEQIA--------------QSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 321 KGFSVVASEVRLLAEHSRKAATEIEQMTKTIQHGVMAAIKGMGTCVEQAGGGVTLTQDAGEVINQVNIGMQDVVKLMTAF 400
Cdd:pfam00015 68 RGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147
|
....*..
gi 1206439776 401 AQVKNQQ 407
Cdd:pfam00015 148 AAASDEQ 154
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
1-235 |
4.76e-24 |
|
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: 103.52 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYvlsEPYRRHWKLLNEGRPITDN--IKRIRKDGSIIWLQG 78
Cdd:COG5809 28 ILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDD---EKELREILKLLKEGESRDEleFELRHKNGKRLEFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 79 TYTPVLDNQGRVVEIIKIAHDVTERI-----LQSQEHQSLLEALNRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHK 153
Cdd:COG5809 105 KLSPIFDQNGDIEGMLAISRDITERKrmeeaLRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 154 SHQmlctpEFAHSDDYYQ----HWQRLARGEFILGRFERVNSRGQRVWLEASYNPIMDNEGQVFKVVkIAQDIT---QLM 226
Cdd:COG5809 185 SIL-----ELIHSDDQENvaafISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVI-IFRDITerkKLE 258
|
....*....
gi 1206439776 227 LQQEHEENL 235
Cdd:COG5809 259 ELLRKSEKL 267
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
209-408 |
1.74e-21 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 96.56 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 209 EGQVFKVVKIAQDITQLMLQQEHEENLIRNVYHLSLSTDRSASQGAEIVQQAVRGMQevesiaretsdvvsDLGRCSQEI 288
Cdd:PRK15041 296 EQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMR--------------DISTSSQKI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 289 GTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASEVRLLAEHSRKAATEIEQMTKtiqhgvmaaikgmgTCVEQ 368
Cdd:PRK15041 362 ADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIE--------------DSVGK 427
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1206439776 369 AGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:PRK15041 428 VDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQS 467
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
209-408 |
2.24e-19 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 90.07 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 209 EGQVFKVVKIAQDITQLMLQQEHEENLIRNVYHLSLSTDRSASQGAEIVQQAVRGMQEVESIARETSDVVSdlgrcsqei 288
Cdd:PRK15048 294 EQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIIS--------- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 289 gtiveAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVASEVRLLAEHSRKAATEIEQMtktiqhgvmaaikgMGTCVEQ 368
Cdd:PRK15048 365 -----VIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKAL--------------IEDSVSR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1206439776 369 AGGGVTLTQDAGEVINQVNIGMQDVVKLMTAFAQVKNQQT 408
Cdd:PRK15048 426 VDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQS 465
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
249-410 |
1.31e-18 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 87.82 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 249 SASQGAEIVQQAVRGMQEVESIARETSDVVSDLGRCSQEIGTIVEAIRKISSQTNLLAINASIEAAHAGEHGKGFSVVAS 328
Cdd:PRK09793 318 NARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAG 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 329 EVRLLAEHSRKAATE----IEQMTKTIQHG---VMAAIKGMGTCVEQagggVTLTQD-AGEVI---NQVNIGMQDVVKLM 397
Cdd:PRK09793 398 EVRNLASRSAQAAKEikglIEESVNRVQQGsklVNNAAATMTDIVSS----VTRVNDiMGEIAsasEEQRRGIEQVAQAV 473
|
170
....*....|...
gi 1206439776 398 TAFAQVKNQQTPL 410
Cdd:PRK09793 474 SQMDQVTQQNASL 486
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
102-248 |
2.01e-15 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 75.83 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 102 ERILQSQEHQSLLEALNRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQMLCTPEFAHsDDYYQHWQRLARGEF 181
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1206439776 182 ILGRFERVNSRGQRVWLEASYNPIMDNEGQVFKVVKIAQDIT-------QLMLQQEHEENLIRNVYHLSLSTDR 248
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITerkraeeALRESEERLRLLVENAPDGIFVLDL 155
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
12-97 |
2.02e-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: 65.44 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 12 HANTLFLQAMGYQQNEVIGKHHKLFC-----DPQYVlsepYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTYTPVLDN 86
Cdd:pfam08447 3 YWSPRFEEILGYTPEELLGKGESWLDlvhpdDRERV----REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|.
gi 1206439776 87 QGRVVEIIKIA 97
Cdd:pfam08447 79 NGKPVRVIGVA 89
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
1-100 |
4.06e-11 |
|
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: 59.57 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYVLsEPYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTY 80
Cdd:cd00130 5 VIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83
|
90 100
....*....|....*....|
gi 1206439776 81 TPVLDNQGRVVEIIKIAHDV 100
Cdd:cd00130 84 TPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
132-219 |
4.17e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 58.89 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 132 ILAANDNLLRVIGYSLADIQHKSHQMLctpEFAHSDDYYQ----HWQRLARGEFILGRFERVNSRGQRVWLEASYNPIMD 207
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWL---DLVHPDDRERvreaLWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD 77
|
90
....*....|..
gi 1206439776 208 NEGQVFKVVKIA 219
Cdd:pfam08447 78 ENGKPVRVIGVA 89
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
1-110 |
7.25e-11 |
|
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: 59.23 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHhklfcdPQYVLSEPYR-----RHWKLL-NEGRPITDNIKRIRKDGSII 74
Cdd:TIGR00229 16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRN------VLELIPEEDReevreRIERRLeGEPEPVSEERRVRRKDGSEI 89
|
90 100 110
....*....|....*....|....*....|....*.
gi 1206439776 75 WLQGTYTPVLDNQGRVVeIIKIAHDVTERILQSQEH 110
Cdd:TIGR00229 90 WVEVSVSPIRTNGGELG-VVGIVRDITERKEAEEAL 124
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
7-102 |
1.73e-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: 57.47 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 7 DGTVKHANTLFLQAMGYQQNEVIGKH-HKLFCDPQYvlSEPYRRHWKLLNEGRPitDNIKRIRKDGSIIWLQGTYTPVLD 85
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPED--SERLREALREGKAVRE--FEVVLYRKDGEPFPVLVSLAPIRD 76
|
90
....*....|....*..
gi 1206439776 86 NQGRVVEIIKIAHDVTE 102
Cdd:pfam13426 77 DGGELVGIIAILRDITE 93
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
120-222 |
3.00e-10 |
|
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: 56.87 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 120 SMGMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQmlctpEFAHSDDYYQHWQRL----ARGEFILGRFERVNSRGQR 195
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLL-----DLIHPEDREELRERLenllSGGEPVTLEVRLRRKDGSV 76
|
90 100
....*....|....*....|....*..
gi 1206439776 196 VWLEASYNPIMDNEGQVFKVVKIAQDI 222
Cdd:cd00130 77 IWVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
2-103 |
3.40e-10 |
|
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: 57.04 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 2 IIFKPDGTVKHANTLFLQAMGYQQNEVIGKH-HKLFCDPQYvlsEPYRRHW-KLLNEGRPITDNIKRIRkDGSIIWLQGT 79
Cdd:pfam08448 9 AVLDPDGRVRYANAAAAELFGLPPEELLGKTlAELLPPEDA---ARLERALrRALEGEEPIDFLEELLL-NGEERHYELR 84
|
90 100
....*....|....*....|....
gi 1206439776 80 YTPVLDNQGRVVEIIKIAHDVTER 103
Cdd:pfam08448 85 LTPLRDPDGEVIGVLVISRDITER 108
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
118-225 |
4.06e-09 |
|
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: 53.96 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 118 NRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQMLCTPEfaHSDDYYQHWQRLARGEFILGRFERVNSRGQRVW 197
Cdd:pfam08448 3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPE--DAARLERALRRALEGEEPIDFLEELLLNGEERH 80
|
90 100
....*....|....*....|....*...
gi 1206439776 198 LEASYNPIMDNEGQVFKVVKIAQDITQL 225
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDITER 108
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
122-235 |
2.25e-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: 52.29 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 122 GMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQMLCTPEFAHSDDYYQhWQRLARGEFILGRFERV-NSRGQRVWLEA 200
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERI-ERRLEGEPEPVSEERRVrRKDGSEIWVEV 93
|
90 100 110
....*....|....*....|....*....|....*
gi 1206439776 201 SYNPIMDNEGQVFkVVKIAQDITQLmlqQEHEENL 235
Cdd:TIGR00229 94 SVSPIRTNGGELG-VVGIVRDITER---KEAEEAL 124
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
1-118 |
4.79e-08 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 54.47 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYVLSEPYRRhwkLLNEGRPITDN-IKRIRKDGSIIWLQGT 79
Cdd:COG3852 20 VIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLER---ALAEGQPVTEReVTLRRKDGEERPVDVS 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1206439776 80 YTPVLDNQGRvVEIIKIAHDVTERILQSQEHQsLLEALN 118
Cdd:COG3852 97 VSPLRDAEGE-GGVLLVLRDITERKRLERELR-RAEKLA 133
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
5-199 |
4.93e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 54.44 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 5 KPDGTVKHANTLFLQAMGYQQNEVIGKHHKLF----CDPQYVlsepyRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTY 80
Cdd:PRK13559 63 QPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLqgaaTDPIAV-----AKIRAAIAAEREIVVELLNYRKDGEPFWNALHL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 81 TPVLDNQGRVVEIIKIAHDVTE----RILQSQEHQSLLEALNRSMGMitfspqgiiLAANDNLLRVIGYSL------ADI 150
Cdd:PRK13559 138 GPVYGEDGRLLYFFGSQWDVTDiravRALEAHERRLAREVDHRSKNV---------FAVVDSIVRLTGRADdpslyaAAI 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1206439776 151 QHKShQMLCTPEFAHSDDyyQHWQRLARGEFILGRFERVNSRGQRVWLE 199
Cdd:PRK13559 209 QERV-QALARAHETLLDE--RGWETVEVEELIRAQVAPYAPRATRVAFE 254
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
129-224 |
1.15e-07 |
|
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: 49.38 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 129 QGIILAANDNLLRVIGYSLADIQHKSHQMLCTPEfAHSDDYYQHWQRLarGEFILGRFERVNSRGQRVWLEASYNPIMDN 208
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEP-EDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 1206439776 209 EGQVFKVVKIAQDITQ 224
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
6-125 |
3.80e-07 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 52.15 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 6 PDGTVKHANTLFLQAMGYQQNEVIGKHHKlFCDPQYVLSEPYRRHWKLLNEGRPITDNIKRIRKDGSIIWLQGTYTPVLD 85
Cdd:PRK13558 169 PDEPLIYINDAFERITGYSPDEVLGRNCR-FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1206439776 86 NQGRVVEIIKIAHDVTERI-------LQSQEHQSLLEALNRSMGMIT 125
Cdd:PRK13558 248 EDGTVTHYVGFQTDVTERKeaelalqRERRKLQRLLERVEGLVNDVT 294
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
1-129 |
5.57e-07 |
|
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: 51.31 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKH-HKLFcdpqyvlsePYRRHWKLLNEGRPITDNIKRIRKDGsiIWLQGT 79
Cdd:COG3829 24 IIVVDADGRITYVNRAAERILGLPREEVIGKNvTELI---------PNSPLLEVLKTGKPVTGVIQKTGGKG--KTVIVT 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1206439776 80 YTPVLDNqGRVVEIIKIAHDVTE-----RILQSQEHQSLLEALNRSMGMITFSPQ 129
Cdd:COG3829 93 AIPIFED-GEVIGAVETFRDITElkrleRKLREEELERGLSAKYTFDDIIGKSPA 146
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
107-238 |
6.47e-07 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 51.00 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 107 SQEHQSLLEALnrSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQMLctpeFAHSDDYYQHWQR-LARGE-FILG 184
Cdd:COG3852 6 EELLRAILDSL--PDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAEL----FPEDSPLRELLERaLAEGQpVTER 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1206439776 185 RFERVNSRGQRVWLEASYNPIMDNEGQVFkVVKIAQDITQlmlQQEHEENLIRN 238
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGEGG-VLLVLRDITE---RKRLERELRRA 129
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
67-103 |
8.34e-07 |
|
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: 45.25 E-value: 8.34e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1206439776 67 IRKDGSIIWLQGTYTPVLDNQGRVVEIIKIAHDVTER 103
Cdd:smart00086 7 RRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
1-100 |
1.19e-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: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKH-HKLF--CDPQYVlsepYRRHWKLLNEGRPITD-NIKRIRKDGSIIWL 76
Cdd:pfam00989 14 IFVVDEDGRILYVNAAAEELLGLSREEVIGKSlLDLIpeEDDAEV----AELLRQALLQGEESRGfEVSFRVPDGRPRHV 89
|
90 100
....*....|....*....|....
gi 1206439776 77 QGTYTPVLDNQGRVVEIIKIAHDV 100
Cdd:pfam00989 90 EVRASPVRDAGGEILGFLGVLRDI 113
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
102-247 |
4.57e-06 |
|
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: 48.61 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 102 ERILQSQEHQSLLEAL--NRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKShqmlCTPEFAHSddyyQHWQRLARG 179
Cdd:COG3829 1 AEELELKELEEELEAIldSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKN----VTELIPNS----PLLEVLKTG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206439776 180 EFILGRFERVNSRGQRVwlEASYNPIMDNeGQVFKVVKIAQDITQLM-LQQEHEENLIRNVYHLSLSTD 247
Cdd:COG3829 73 KPVTGVIQKTGGKGKTV--IVTAIPIFED-GEVIGAVETFRDITELKrLERKLREEELERGLSAKYTFD 138
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
22-274 |
1.92e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 47.07 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 22 GYQQNEVIGKHHKLFCDPQYVLSEP-YRRHWKLLNEGRPITDN--IKRIRKDGSIIWLQGTYTPVlDNQGRVVEIIkIAH 98
Cdd:PRK11359 46 GYKREEVIGNNIDMLIPRDLRPAHPeYIRHNREGGKARVEGMSreLQLEKKDGSKIWTRFALSKV-SAEGKVYYLA-LVR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 99 DVTERILQSQEHQSLLEALNRS-MGMITFSPQGIILAANDNLLRVIGYSLADIQHKS-HQMLCTPEFahSDDYYQHWQRL 176
Cdd:PRK11359 124 DASVEMAQKEQTRQLIIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQpDTLLNIPEF--PADNRIRLQQL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 177 ARG-EFILGRFERVNSRGQRVWLEASYNPIMDNEGQVFKVVKIAQDITqlmlQQEHEENLIRNVYHLSLSTDRSASQGAE 255
Cdd:PRK11359 202 LWKtARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDIT----EERQIRQLEGNILAAMCSSPPFHEMGEI 277
|
250
....*....|....*....
gi 1206439776 256 IVQQavrgmqeVESIARET 274
Cdd:PRK11359 278 ICRN-------IESVLNES 289
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
1-109 |
3.99e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 45.02 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 1 MIIFKPDGTVKHANTLFLQAMGYQQNEVIGKHHKLFCDPQYVlsEPYRRHWKLLNEG--RPITDNIKRIRKDGSIIWLQG 78
Cdd:COG2202 150 IFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDR--ERLLELLRRLLEGgrESYELELRLKDGDGRWVWVEA 227
|
90 100 110
....*....|....*....|....*....|.
gi 1206439776 79 TYTPVlDNQGRVVEIIKIAHDVTERILQSQE 109
Cdd:COG2202 228 SAVPL-RDGGEVIGVLGIVRDITERKRAEEA 257
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
6-145 |
5.39e-05 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 45.43 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 6 PDGTVKHANTLFLQAMGYQQNEVIGKHHKLF----CDPQYVLSepYRRhwkLLNEGRPITDNIKRIRKDGSIIWLQGTYT 81
Cdd:PRK13557 51 PDNPIVFANRAFLEMTGYAAEEIIGNNCRFLqgpeTDRATVAE--VRD---AIAERREIATEILNYRKDGSSFWNALFVS 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206439776 82 PVLDNQGRVVEIIKIAHDVTER------ILQSQEhqslLEALNRSMGmitfspqGIilaAND--NLLRVI-GY 145
Cdd:PRK13557 126 PVYNDAGDLVYFFGSQLDVSRRrdaedaLRQAQK----MEALGQLTG-------GI---AHDfnNLLQVMsGY 184
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
102-272 |
1.17e-04 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 44.18 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 102 ERILQSQEHQSLLEAL--NRSMGMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQMLcTPEFAHSDDYYQHWQRLARG 179
Cdd:COG5000 80 EQREELEERRRYLETIleNLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEEL-LPELDLAELLREALERGWQE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 180 EFILgrfervnSRGQRVWLEASYNPIMDnEGQVFkvvkIAQDITQLMLQQE------------HEenlIRN--------V 239
Cdd:COG5000 159 EIEL-------TRDGRRTLLVRASPLRD-DGYVI----VFDDITELLRAERlaawgelarriaHE---IKNpltpiqlsA 223
|
170 180 190
....*....|....*....|....*....|....
gi 1206439776 240 YHLSLSTDRSASQGAEIVQQAVRG-MQEVESIAR 272
Cdd:COG5000 224 ERLRRKLADKLEEDREDLERALDTiIRQVDRLKR 257
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
108-179 |
2.23e-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: 39.30 E-value: 2.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1206439776 108 QEHQSLLEALNrsMGMITFSPQGIILAANDNLLRVIGYSLADIQHKShqmlcTPEFAHSDDYYQHWQRLARG 179
Cdd:smart00091 1 ERLRAILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKS-----LLELIHPEDRERVQEALQRL 65
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
122-239 |
4.28e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 39.27 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206439776 122 GMITFSPQGIILAANDNLLRVIGYSLADIQHKSHQMLCTPEFAHSDdyYQHWQRLARGEFILGRFER--VNSRGQRVWLE 199
Cdd:PRK09776 295 GMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKD--LQQVEKLLSGEINSYSMEKryYRRDGEVVWAL 372
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1206439776 200 ASYNPIMDNEGQVFKVVKIAQDITQLMLQQEHEENLIRNV 239
Cdd:PRK09776 373 LAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERLMERI 412
|
|
| |
