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Conserved domains on  [gi|521289789|ref|WP_020454057|]
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MULTISPECIES: PAS domain-containing methyl-accepting chemotaxis protein [Enterobacteriaceae]

Protein Classification

PAS domain-containing methyl-accepting chemotaxis protein( domain architecture ID 13751798)

PAS domain-containing methyl-accepting chemotaxis protein is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MCP_signal super family cl46910
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 200-514 1.68e-85

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.


The actual alignment was detected with superfamily member PRK15041:

Pssm-ID: 481250 [Multi-domain]  Cd Length: 554  Bit Score: 274.14  E-value: 1.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 200 FMTLLLLFINIWLELQ--IVRPIERLYRQALQVASGEAHQ---VDQPNRVDEVGMTLRAISqlGLMFRwLVNDVSGQAMT 274
Cdd:PRK15041 200 MIVVLAVIFAVWFGIKasLVAPMNRLIDSIRHIAGGDLVKpieVDGSNEMGQLAESLRHMQ--GELMR-TVGDVRNGANA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 275 VLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEMMTAIAE 354
Cdd:PRK15041 277 IYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIST 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 355 SSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNSGSQLAD 434
Cdd:PRK15041 357 SSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVE 436

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 435 DAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEGAEATGRLNQQAIRLAEAISVFR 514
Cdd:PRK15041 437 SAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-116 6.32e-16

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 77.76  E-value: 6.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDH 92
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                         90       100
                 ....*....|....*....|....*
gi 521289789  93 YWVRANAIPVI-RQGKVKGYMSVRT 116
Cdd:COG2202   96 FWVELSISPVRdEDGEITGFVGIAR 120
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
200-514 1.68e-85

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 274.14  E-value: 1.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 200 FMTLLLLFINIWLELQ--IVRPIERLYRQALQVASGEAHQ---VDQPNRVDEVGMTLRAISqlGLMFRwLVNDVSGQAMT 274
Cdd:PRK15041 200 MIVVLAVIFAVWFGIKasLVAPMNRLIDSIRHIAGGDLVKpieVDGSNEMGQLAESLRHMQ--GELMR-TVGDVRNGANA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 275 VLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEMMTAIAE 354
Cdd:PRK15041 277 IYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIST 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 355 SSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNSGSQLAD 434
Cdd:PRK15041 357 SSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVE 436

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 435 DAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEGAEATGRLNQQAIRLAEAISVFR 514
Cdd:PRK15041 437 SAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
193-514 2.94e-83

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 268.04  E-value: 2.94e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 193 QLVSFASFMTLLLLFINIWLELQIVRPIERLYRQALQVASGEAHQVDQPNRVDEVGMTLRAISQLGLMFRWLVNDVSGQA 272
Cdd:COG0840  183 LLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 273 MTVLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMI------ 346
Cdd:COG0840  263 EQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieei 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 347 --------EMMTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKAL 418
Cdd:COG0840  343 resveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEEL 422

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 419 IENSVTHVNSGSQL--------------ADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQ 484
Cdd:COG0840  423 IEEIQSETEEAVEAmeegseeveegvelVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQE 502

                        330       340       350
                 ....*....|....*....|....*....|
gi 521289789 485 NAQRVQEGAEATGRLNQQAIRLAEAISVFR 514
Cdd:COG0840  503 NAASVEEVAAAAEELAELAEELQELVSRFK 532
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 267-514 1.76e-72

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: 231.02  E-value: 1.76e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   267 DVSGQAMTVLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMI 346
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   347 EMMTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIEN----- 421
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   422 ---------SVTHVNSGSQLADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEG 492
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 521289789   493 AEATGRLNQQAIRLAEAISVFR 514
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 294-491 3.21e-58

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: 191.68  E-value: 3.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 294 EQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEMMTAIAESSRQIASITSIIDSIAFQT 373
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 374 NILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNSGSQLADDAGKTMKEIVEQVQNVTSL 453
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 521289789 454 IAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQE 491
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 325-482 1.93e-51

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: 173.00  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  325 TALSQGTRDAARQGGQVMHQMIEMMTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSL 404
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  405 AQRSARAASEIKALI--------------ENSVTHVNSGSQLADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSE 470
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 521289789  471 ASLAVEDLDKIT 482
Cdd:pfam00015 161 VNQAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-116 6.32e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 77.76  E-value: 6.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDH 92
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                         90       100
                 ....*....|....*....|....*
gi 521289789  93 YWVRANAIPVI-RQGKVKGYMSVRT 116
Cdd:COG2202   96 FWVELSISPVRdEDGEITGFVGIAR 120
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 2.65e-14

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: 68.13  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   30 INYANDAFIDVSGFSLEEIKGQPHNLVR--HPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRANAIPVI-RQG 106
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDlvHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*....
gi 521289789  107 KVKGYMSVR 115
Cdd:pfam08447  81 KPVRVIGVA 89
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 14-114 1.39e-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: 53.06  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   14 FDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKN-RRSNGDH 92
Cdd:TIGR00229   9 FESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSE 88

                          90       100
                  ....*....|....*....|..
gi 521289789   93 YWVRANAIPVIRQGKVKGYMSV 114
Cdd:TIGR00229  89 IWVEVSVSPIRTNGGELGVVGI 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 24-117 1.41e-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: 49.55  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  24 TDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRANAIPV- 102
Cdd:cd00130    8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIr 87

                         90
                 ....*....|....*
gi 521289789 103 IRQGKVKGYMSVRTR 117
Cdd:cd00130   88 DEGGEVIGLLGVVRD 102
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 19-102 3.72e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 52.92  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  19 TLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRAN 98
Cdd:PRK13558 162 TIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVD 241


                 ....
gi 521289789  99 AIPV 102
Cdd:PRK13558 242 IAPI 245
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 13-63 4.89e-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: 35.84  E-value: 4.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 521289789    13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQP-HNLVRHPDMPK 63
Cdd:smart00091   6 ILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSlLELIHPEDRER 57
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
200-514 1.68e-85

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 274.14  E-value: 1.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 200 FMTLLLLFINIWLELQ--IVRPIERLYRQALQVASGEAHQ---VDQPNRVDEVGMTLRAISqlGLMFRwLVNDVSGQAMT 274
Cdd:PRK15041 200 MIVVLAVIFAVWFGIKasLVAPMNRLIDSIRHIAGGDLVKpieVDGSNEMGQLAESLRHMQ--GELMR-TVGDVRNGANA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 275 VLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEMMTAIAE 354
Cdd:PRK15041 277 IYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIST 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 355 SSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNSGSQLAD 434
Cdd:PRK15041 357 SSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVE 436

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 435 DAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEGAEATGRLNQQAIRLAEAISVFR 514
Cdd:PRK15041 437 SAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
193-514 2.94e-83

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 268.04  E-value: 2.94e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 193 QLVSFASFMTLLLLFINIWLELQIVRPIERLYRQALQVASGEAHQVDQPNRVDEVGMTLRAISQLGLMFRWLVNDVSGQA 272
Cdd:COG0840  183 LLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 273 MTVLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMI------ 346
Cdd:COG0840  263 EQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieei 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 347 --------EMMTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKAL 418
Cdd:COG0840  343 resveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEEL 422

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 419 IENSVTHVNSGSQL--------------ADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQ 484
Cdd:COG0840  423 IEEIQSETEEAVEAmeegseeveegvelVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQE 502

                        330       340       350
                 ....*....|....*....|....*....|
gi 521289789 485 NAQRVQEGAEATGRLNQQAIRLAEAISVFR 514
Cdd:COG0840  503 NAASVEEVAAAAEELAELAEELQELVSRFK 532
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 193-514 1.11e-82

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 266.87  E-value: 1.11e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 193 QLVSFASFMTLLLLFINIWLELQIVRPIERLYRQALQVASGEAHQVDQPNRVDEVGMTLRAISQLGLMFRWLVNDVSGQA 272
Cdd:PRK15048 193 QLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGS 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 273 MTVLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEMMTAI 352
Cdd:PRK15048 273 DAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEI 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 353 AESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNSGSQL 432
Cdd:PRK15048 353 ADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVL 432

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 433 ADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEGAEATGRLNQQAIRLAEAISV 512
Cdd:PRK15048 433 VESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSA 512


                 ..
gi 521289789 513 FR 514
Cdd:PRK15048 513 FR 514
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
195-514 3.39e-73

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 241.51  E-value: 3.39e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 195 VSFASFMTLLLLFIN---IWLELQIVRPIERLYRQALQVASGEAHQ---VDQPNRVDEVGMTLRAISQlglMFRWLVNDV 268
Cdd:PRK09793 190 LVFISMIIVAAIYISsalWWTRKMIVQPLAIIGSHFDSIAAGNLARpiaVYGRNEITAIFASLKTMQQ---ALRGTVSDV 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 269 SGQAMTVLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEM 348
Cdd:PRK09793 267 RKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHT 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 349 MTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNS 428
Cdd:PRK09793 347 MQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQ 426

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 429 GSQLADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEGAEATGRLNQQAIRLAE 508
Cdd:PRK09793 427 GSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSS 506


                 ....*.
gi 521289789 509 AISVFR 514
Cdd:PRK09793 507 RVAVFT 512
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 267-514 1.76e-72

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: 231.02  E-value: 1.76e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   267 DVSGQAMTVLKASESLRQGNDDLSRQTEQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMI 346
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   347 EMMTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIEN----- 421
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   422 ---------SVTHVNSGSQLADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQEG 492
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 521289789   493 AEATGRLNQQAIRLAEAISVFR 514
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 294-491 3.21e-58

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: 191.68  E-value: 3.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 294 EQAAANVEQTAATMNELTATVKSNRETAAEVTALSQGTRDAARQGGQVMHQMIEMMTAIAESSRQIASITSIIDSIAFQT 373
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 374 NILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSARAASEIKALIENSVTHVNSGSQLADDAGKTMKEIVEQVQNVTSL 453
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 521289789 454 IAQISAATAEQATALSEASLAVEDLDKITHQNAQRVQE 491
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 325-482 1.93e-51

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: 173.00  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  325 TALSQGTRDAARQGGQVMHQMIEMMTAIAESSRQIASITSIIDSIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSL 404
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  405 AQRSARAASEIKALI--------------ENSVTHVNSGSQLADDAGKTMKEIVEQVQNVTSLIAQISAATAEQATALSE 470
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 521289789  471 ASLAVEDLDKIT 482
Cdd:pfam00015 161 VNQAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-116 6.32e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 77.76  E-value: 6.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDH 92
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                         90       100
                 ....*....|....*....|....*
gi 521289789  93 YWVRANAIPVI-RQGKVKGYMSVRT 116
Cdd:COG2202   96 FWVELSISPVRdEDGEITGFVGIAR 120
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 2.65e-14

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: 68.13  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   30 INYANDAFIDVSGFSLEEIKGQPHNLVR--HPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRANAIPVI-RQG 106
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDlvHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*....
gi 521289789  107 KVKGYMSVR 115
Cdd:pfam08447  81 KPVRVIGVA 89
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 14-114 1.39e-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: 53.06  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   14 FDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKN-RRSNGDH 92
Cdd:TIGR00229   9 FESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSE 88

                          90       100
                  ....*....|....*....|..
gi 521289789   93 YWVRANAIPVIRQGKVKGYMSV 114
Cdd:TIGR00229  89 IWVEVSVSPIRTNGGELGVVGI 110
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 27-108 2.38e-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: 51.69  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   27 DSYINYANDAFIDVSGFSLEEIKGQP-HNLVRHPDmPKQAFADMWSTLKQGepWTALVKNRRSNGDHYWVRANAIPVIRQ 105
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPE-DSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDD 77


                  ...
gi 521289789  106 GKV 108
Cdd:pfam13426  78 GGE 80
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 21-103 2.54e-08

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


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 56.45  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   21 MSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRANAI 100
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96


                  ...
gi 521289789  101 PVI 103
Cdd:TIGR02938  97 PVL 99
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 13-114 5.11e-08

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: 51.26  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTA-LVKNRRSNGD 91
Cdd:pfam00989   6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGfEVSFRVPDGR 85

                          90       100
                  ....*....|....*....|....
gi 521289789   92 HYWVRANAIPVI-RQGKVKGYMSV 114
Cdd:pfam00989  86 PRHVEVRASPVRdAGGEILGFLGV 109
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 24-117 1.41e-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: 49.55  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  24 TDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRANAIPV- 102
Cdd:cd00130    8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIr 87

                         90
                 ....*....|....*
gi 521289789 103 IRQGKVKGYMSVRTR 117
Cdd:cd00130   88 DEGGEVIGLLGVVRD 102
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 1-114 2.80e-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: 52.85  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   1 MRNNEPVTQQEYVFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQP-HNLVRHPDMPKqafadmwsTLKQGEPW 79
Cdd:COG3829    4 LELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNvTELIPNSPLLE--------VLKTGKPV 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 521289789  80 TALVKNRRSNGDHywVRANAIPVIRQGKVKGYMSV 114
Cdd:COG3829   76 TGVIQKTGGKGKT--VIVTAIPIFEDGEVIGAVET 108
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 19-102 3.72e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 52.92  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  19 TLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRAN 98
Cdd:PRK13558 162 TIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVD 241


                 ....
gi 521289789  99 AIPV 102
Cdd:PRK13558 242 IAPI 245
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 13-114 5.89e-07

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: 51.90  E-value: 5.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDH 92
Cdd:COG5809  146 IFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRW 225

                         90       100
                 ....*....|....*....|..
gi 521289789  93 YWVRANAIPVIRQGKVKGYMSV 114
Cdd:COG5809  226 RLLEASGAPIKKNGEVDGIVII 247
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1-114 2.78e-06

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.46  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   1 MRNNEPVTQQeyVFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQP-HNLVRHPDmpkQAFADMWSTLKQGEPW 79
Cdd:COG3852    2 LRESEELLRA--ILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPEDS---PLRELLERALAEGQPV 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 521289789  80 TAL-VKNRRSNGDHYWVRANAIPVIRQGKVKGYMSV 114
Cdd:COG3852   77 TEReVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLV 112
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-114 3.94e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 48.48  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQG-EPWTALVKNRRSNGD 91
Cdd:COG2202  142 LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGR 221

                         90       100
                 ....*....|....*....|...
gi 521289789  92 HYWVRANAIPVIRQGKVKGYMSV 114
Cdd:COG2202  222 WVWVEASAVPLRDGGEVIGVLGI 244
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
197-302 4.56e-04

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 42.74  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789 197 FASFMTLLLLFINIWLELQIVRPIERLYRQALQVASGEAHQVDQPNRVDEVGMTlraisqlglmfrwlvndvsGQAMTVL 276
Cdd:PRK10600 130 FAVFMALLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAML-------------------GTALNNM 190

                         90       100
                 ....*....|....*....|....*.
gi 521289789 277 kaSESLRQGNDDLSRQTEQAAANVEQ 302
Cdd:PRK10600 191 --SAELAESYAVLEQRVQEKTAGLEQ 214
PRK13557 PRK13557
histidine kinase; Provisional
 21-102 1.54e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 41.19  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789  21 MSTTDP---DSYINYANDAFIDVSGFSLEEIKGQPHNLVRHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWvra 97
Cdd:PRK13557  43 MIVTDPnqpDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFW--- 119


                 ....*...
gi 521289789  98 NAI---PV 102
Cdd:PRK13557 120 NALfvsPV 127
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 25-112 1.60e-03

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: 38.16  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289789   25 DPDSYINYANDAFIDVSGFSLEEIKGQPHNLVrHPDMPKQAFADMWSTLKQGEPWTALVKNRRSNGDHYWVRANAIPVI- 103
Cdd:pfam08448  12 DPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPLRd 90


                  ....*....
gi 521289789  104 RQGKVKGYM 112
Cdd:pfam08448  91 PDGEVIGVL 99
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 13-63 4.89e-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: 35.84  E-value: 4.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 521289789    13 VFDNDATLMSTTDPDSYINYANDAFIDVSGFSLEEIKGQP-HNLVRHPDMPK 63
Cdd:smart00091   6 ILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSlLELIHPEDRER 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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