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Conserved domains on  [gi|1957526454|ref|WP_200921564|]
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MULTISPECIES: PAS domain-containing methyl-accepting chemotaxis protein [Citrobacter]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 11451354)

methyl-accepting chemotaxis protein (MCP) 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

CATH:  3.30.450.20|1.10.287.950
Gene Ontology:  GO:0098561|GO:0007165|GO:0006935|GO:0016020|GO:0004888
PubMed:  28409190|15009198|9382818|18165013|20738376
SCOP:  3000471|4003862

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
111-511 2.05e-72

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 239.54  E-value: 2.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 111 YISVRTVPSRDEITQSESLYHKINNQQIKGFRLFKGIVIRRGILSWASMFKWLSISQRVNYSLGVIALLAVLFLFAPVNP 190
Cdd:COG0840   101 AALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALA 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 191 FIQAGGLLFLFLMLAIYLKY----QICQPVNTLLTQMKKVVSGRKPDNCHLNRVDEIGMLMRLVNQSGLNLNSLVDDVST 266
Cdd:COG0840   181 LALLAAALLALVALAIILALllsrSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRE 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 267 QISGIRAISQRVSKEGTALHKRSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQ 346
Cdd:COG0840   261 SAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIE 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 347 AISRDN--------------GQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIK 412
Cdd:COG0840   341 EIRESVeetaetieelgessQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIE 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 413 QLIEKNVANVNSGVKMVEQTETH--------------LTGMIGDVLQMSMMIKDISLATREQTQALDLINDSISRVGTMT 478
Cdd:COG0840   421 ELIEEIQSETEEAVEAMEEGSEEveegvelveeageaLEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAA 500

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1957526454 479 HNNAEMVERVTDATADLTQRSSRLQQAVQVFGV 511
Cdd:COG0840   501 QENAASVEEVAAAAEELAELAEELQELVSRFKL 533
PAS COG2202
PAS domain [Signal transduction mechanisms];
23-125 1.06e-15

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.99  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPV 102
Cdd:COG2202    26 ITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105

                          90       100
                  ....*....|....*....|....
gi 1957526454 103 W-HNEKLTGYISVrtvpSRDeITQ 125
Cdd:COG2202   106 RdEDGEITGFVGI----ARD-ITE 124
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
111-511 2.05e-72

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 239.54  E-value: 2.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 111 YISVRTVPSRDEITQSESLYHKINNQQIKGFRLFKGIVIRRGILSWASMFKWLSISQRVNYSLGVIALLAVLFLFAPVNP 190
Cdd:COG0840   101 AALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALA 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 191 FIQAGGLLFLFLMLAIYLKY----QICQPVNTLLTQMKKVVSGRKPDNCHLNRVDEIGMLMRLVNQSGLNLNSLVDDVST 266
Cdd:COG0840   181 LALLAAALLALVALAIILALllsrSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRE 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 267 QISGIRAISQRVSKEGTALHKRSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQ 346
Cdd:COG0840   261 SAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIE 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 347 AISRDN--------------GQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIK 412
Cdd:COG0840   341 EIRESVeetaetieelgessQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIE 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 413 QLIEKNVANVNSGVKMVEQTETH--------------LTGMIGDVLQMSMMIKDISLATREQTQALDLINDSISRVGTMT 478
Cdd:COG0840   421 ELIEEIQSETEEAVEAMEEGSEEveegvelveeageaLEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAA 500

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1957526454 479 HNNAEMVERVTDATADLTQRSSRLQQAVQVFGV 511
Cdd:COG0840   501 QENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 263-509 3.22e-64

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: 209.45  E-value: 3.22e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  263 DVSTQISGIRAISQRVSKEGTALHKRSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTI 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  343 AMMQAISRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLI------- 415
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  416 -------EKNVANVNSGVKMVEQTETHLTGMIGDVLQMSMMIKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERV 488
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|.
gi 1957526454  489 TDATADLTQRSSRLQQAVQVF 509
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
208-509 1.08e-59

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 205.96  E-value: 1.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 208 LKYQICQPVNTLLTQMKKVVSGRKPDNCHLNRVDEIGMLMRLVNQSGLNLNSLVDDVSTQISGIRAISQRVSKEGTALHK 287
Cdd:PRK15041  214 IKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSS 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 288 RSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAF 367
Cdd:PRK15041  294 RTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAF 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 368 QTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLIEKNVANVNSGVKMVEQTETHLTGMIGDVLQMS 447
Cdd:PRK15041  374 QTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVT 453

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957526454 448 MMIKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERVTDATADLTQRSSRLQQAVQVF 509
Cdd:PRK15041  454 DIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 290-489 1.53e-50

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: 171.65  E-value: 1.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 290 EETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAFQT 369
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 370 NILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLIEKNVANVNSGVKMVEQTETHLTGMIGDVLQMSMM 449
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1957526454 450 IKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERVT 489
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 323-478 7.61e-45

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: 155.28  E-value: 7.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 323 MADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQ 402
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 403 HSASAAKEIKQLIEKNVANVN--------------SGVKMVEQTETHLTGMIGDVLQMSMMIKDISLATREQTQALDLIN 468
Cdd:pfam00015  83 RSAQAAKEIEALIIEIQKQTNdstasiestrqrveVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVN 162

                         170
                  ....*....|
gi 1957526454 469 DSISRVGTMT 478
Cdd:pfam00015 163 QAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
23-125 1.06e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.99  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPV 102
Cdd:COG2202    26 ITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105

                          90       100
                  ....*....|....*....|....
gi 1957526454 103 W-HNEKLTGYISVrtvpSRDeITQ 125
Cdd:COG2202   106 RdEDGEITGFVGI----ARD-ITE 124
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 2.21e-12

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: 62.74  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  30 ITYANSAFIDASGFNEQQLMG--EPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPVW-HNE 106
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*....
gi 1957526454 107 KLTGYISVR 115
Cdd:pfam08447  81 KPVRVIGVA 89
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 16-138 1.12e-09

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: 60.69  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  16 DKATL-LSTTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYW 94
Cdd:TIGR02938  11 DQAPLaISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYL 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1957526454  95 VRANVTPVWhNE--KLTGYISVRtvpsRDeITQSESLYHKINNQQI 138
Cdd:TIGR02938  91 AELTVAPVL-NEagETTHFLGMH----RD-ITELHRLEQVVANQKL 130
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 24-114 2.32e-06

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: 46.09  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  24 TDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPVW 103
Cdd:cd00130     8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87

                          90
                  ....*....|.
gi 1957526454 104 HNEKLTGYISV 114
Cdd:cd00130    88 DEGGEVIGLLG 98
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 10-102 1.45e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 44.44  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  10 IEHALNDKA---TLLSTTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNR 86
Cdd:PRK13558  150 KERALDEAPvgiTIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNY 229

                          90
                  ....*....|....*.
gi 1957526454  87 RQNGDHYWVRANVTPV 102
Cdd:PRK13558  230 RKDGSTFWNQVDIAPI 245
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
111-511 2.05e-72

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 239.54  E-value: 2.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 111 YISVRTVPSRDEITQSESLYHKINNQQIKGFRLFKGIVIRRGILSWASMFKWLSISQRVNYSLGVIALLAVLFLFAPVNP 190
Cdd:COG0840   101 AALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALA 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 191 FIQAGGLLFLFLMLAIYLKY----QICQPVNTLLTQMKKVVSGRKPDNCHLNRVDEIGMLMRLVNQSGLNLNSLVDDVST 266
Cdd:COG0840   181 LALLAAALLALVALAIILALllsrSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRE 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 267 QISGIRAISQRVSKEGTALHKRSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQ 346
Cdd:COG0840   261 SAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIE 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 347 AISRDN--------------GQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIK 412
Cdd:COG0840   341 EIRESVeetaetieelgessQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIE 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 413 QLIEKNVANVNSGVKMVEQTETH--------------LTGMIGDVLQMSMMIKDISLATREQTQALDLINDSISRVGTMT 478
Cdd:COG0840   421 ELIEEIQSETEEAVEAMEEGSEEveegvelveeageaLEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAA 500

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1957526454 479 HNNAEMVERVTDATADLTQRSSRLQQAVQVFGV 511
Cdd:COG0840   501 QENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 263-509 3.22e-64

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: 209.45  E-value: 3.22e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  263 DVSTQISGIRAISQRVSKEGTALHKRSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTI 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  343 AMMQAISRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLI------- 415
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  416 -------EKNVANVNSGVKMVEQTETHLTGMIGDVLQMSMMIKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERV 488
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|.
gi 1957526454  489 TDATADLTQRSSRLQQAVQVF 509
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
208-509 1.08e-59

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 205.96  E-value: 1.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 208 LKYQICQPVNTLLTQMKKVVSGRKPDNCHLNRVDEIGMLMRLVNQSGLNLNSLVDDVSTQISGIRAISQRVSKEGTALHK 287
Cdd:PRK15041  214 IKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSS 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 288 RSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAF 367
Cdd:PRK15041  294 RTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAF 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 368 QTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLIEKNVANVNSGVKMVEQTETHLTGMIGDVLQMS 447
Cdd:PRK15041  374 QTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVT 453

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957526454 448 MMIKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERVTDATADLTQRSSRLQQAVQVF 509
Cdd:PRK15041  454 DIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 208-513 6.38e-59

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 204.08  E-value: 6.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 208 LKYQICQPVNTLLTQMKKVVSGRKPDNCHLNRVDEIGMLMRLVNQSGLNLNSLVDDVSTQISGIRAISQRVSKEGTALHK 287
Cdd:PRK15048  212 IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSS 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 288 RSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAF 367
Cdd:PRK15048  292 RTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAF 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 368 QTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLIEKNVANVNSGVKMVEQTETHLTGMIGDVLQMS 447
Cdd:PRK15048  372 QTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVT 451

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957526454 448 MMIKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERVTDATADLTQRSSRLQQAVQVFGVSA 513
Cdd:PRK15048  452 DIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAA 517
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
285-511 2.04e-53

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 188.74  E-value: 2.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 285 LHKRSEETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDS 364
Cdd:PRK09793  287 LSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDG 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 365 IAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLIEKNVANVNSGVKMVEQTETHLTGMIGDVL 444
Cdd:PRK09793  367 IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVT 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1957526454 445 QMSMMIKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERVTDATADLTQRSSRLQQAVQVFGV 511
Cdd:PRK09793  447 RVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 290-489 1.53e-50

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: 171.65  E-value: 1.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 290 EETSADLQQTAAAIEEIGSAVQQTAETAAHTMTMADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAFQT 369
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 370 NILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKQLIEKNVANVNSGVKMVEQTETHLTGMIGDVLQMSMM 449
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1957526454 450 IKDISLATREQTQALDLINDSISRVGTMTHNNAEMVERVT 489
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 323-478 7.61e-45

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: 155.28  E-value: 7.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 323 MADKTSANAAEGGDIMKQTIAMMQAISRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQ 402
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454 403 HSASAAKEIKQLIEKNVANVN--------------SGVKMVEQTETHLTGMIGDVLQMSMMIKDISLATREQTQALDLIN 468
Cdd:pfam00015  83 RSAQAAKEIEALIIEIQKQTNdstasiestrqrveVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVN 162

                         170
                  ....*....|
gi 1957526454 469 DSISRVGTMT 478
Cdd:pfam00015 163 QAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
23-125 1.06e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.99  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPV 102
Cdd:COG2202    26 ITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105

                          90       100
                  ....*....|....*....|....
gi 1957526454 103 W-HNEKLTGYISVrtvpSRDeITQ 125
Cdd:COG2202   106 RdEDGEITGFVGI----ARD-ITE 124
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 2.21e-12

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: 62.74  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  30 ITYANSAFIDASGFNEQQLMG--EPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPVW-HNE 106
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*....
gi 1957526454 107 KLTGYISVR 115
Cdd:pfam08447  81 KPVRVIGVA 89
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 16-138 1.12e-09

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: 60.69  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  16 DKATL-LSTTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYW 94
Cdd:TIGR02938  11 DQAPLaISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYL 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1957526454  95 VRANVTPVWhNE--KLTGYISVRtvpsRDeITQSESLYHKINNQQI 138
Cdd:TIGR02938  91 AELTVAPVL-NEagETTHFLGMH----RD-ITELHRLEQVVANQKL 130
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 23-114 1.67e-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: 49.98  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKN-RRQNGDHYWVRANVTP 101
Cdd:TIGR00229  18 VIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSEIWVEVSVSP 97

                          90
                  ....*....|...
gi 1957526454 102 VWHNEKLTGYISV 114
Cdd:TIGR00229  98 IRTNGGELGVVGI 110
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 23-148 7.63e-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: 7.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEP-HNIIRHPDMPPAafadmwytLQQGDSWTGMVKNRRQNGDHywVRANVTP 101
Cdd:COG3829    26 VVDADGRITYVNRAAERILGLPREEVIGKNvTELIPNSPLLEV--------LKTGKPVTGVIQKTGGKGKT--VIVTAIP 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1957526454 102 VWHNEKLTGYISVrtvpSRDeITQSESLYHKINNQQIKGFRL----FKGIV 148
Cdd:COG3829    96 IFEDGEVIGAVET----FRD-ITELKRLERKLREEELERGLSakytFDDII 141
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 27-114 2.15e-06

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: 45.92  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  27 ESHITYANSAFIDASGFNEQQLMGEP-HNIIRHPDmppaAFADMWYTLQQGDS-WTGMVKNRRQNGDHYWVRANVTPVWH 104
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPE----DSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRD 76

                          90
                  ....*....|.
gi 1957526454 105 NEK-LTGYISV 114
Cdd:pfam13426  77 DGGeLVGIIAI 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 24-114 2.32e-06

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: 46.09  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  24 TDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPVW 103
Cdd:cd00130     8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87

                          90
                  ....*....|.
gi 1957526454 104 HNEKLTGYISV 114
Cdd:cd00130    88 DEGGEVIGLLG 98
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 8-114 4.22e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 45.87  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454   8 TQIEHALNDKATLLSTTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGM-VKNR 86
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFeVSFR 80

                          90       100
                  ....*....|....*....|....*....
gi 1957526454  87 RQNGDHYWVRANVTPV-WHNEKLTGYISV 114
Cdd:pfam00989  81 VPDGRPRHVEVRASPVrDAGGEILGFLGV 109
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
23-114 5.08e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 45.61  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEP-HNIIRHPDMPPAAFADmwyTLQQGDS-WTGMVKNRRQNGDHYWVRANVT 100
Cdd:COG3852    22 VLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPEDSPLRELLER---ALAEGQPvTEREVTLRRKDGEERPVDVSVS 98

                          90
                  ....*....|....
gi 1957526454 101 PVWHNEKLTGYISV 114
Cdd:COG3852    99 PLRDAEGEGGVLLV 112
PAS COG2202
PAS domain [Signal transduction mechanisms];
23-125 1.35e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 43.86  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  23 TTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQG-DSWTGMVKNRRQNGDHYWVRANVTP 101
Cdd:COG2202   152 VLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVP 231

                          90       100
                  ....*....|....*....|....
gi 1957526454 102 VWHNEKLTGYISVrtvpSRDeITQ 125
Cdd:COG2202   232 LRDGGEVIGVLGI----VRD-ITE 250
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 10-102 1.45e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 44.44  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957526454  10 IEHALNDKA---TLLSTTDKESHITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNR 86
Cdd:PRK13558  150 KERALDEAPvgiTIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNY 229

                          90
                  ....*....|....*.
gi 1957526454  87 RQNGDHYWVRANVTPV 102
Cdd:PRK13558  230 RKDGSTFWNQVDIAPI 245
PRK13559 PRK13559
hypothetical protein; Provisional
 30-106 3.83e-03

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 39.42  E-value: 3.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1957526454  30 ITYANSAFIDASGFNEQQLMGEPHNIIRHPDMPPAAFADMWYTLQQGDSWTGMVKNRRQNGDHYWVRANVTPVwHNE 106
Cdd:PRK13559   68 IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPV-YGE 143
 
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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