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Conserved domains on  [gi|1222409393|ref|WP_090461241|]
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PAS domain-containing methyl-accepting chemotaxis protein [Enterobacter sp. kpr-6]

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];
169-509 1.89e-73

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 242.23  E-value: 1.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 169 INAGIIISALAILALQLIALPLAAKMAATVVMFILLALFLQKQVSSPLKKILTQMQKVVSGRKADYFQFNRVDEIGLLMR 248
Cdd:COG0840   163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 249 MVNQSGLNLNSLVGDVNTQLLGIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTS 328
Cdd:COG0840   243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 329 ANAMKSGDVMKQTISMMQSVSRDN--------------GQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVA 394
Cdd:COG0840   323 ELAEEGGEVVEEAVEGIEEIRESVeetaetieelgessQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 395 AEVRNLAQHSASAAKEIKSLIEKNVANVSSGVVMVESTESH--------------LTAMIDSVIQMSTMIKEIGTATQEQ 460
Cdd:COG0840   403 DEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEveegvelveeageaLEEIVEAVEEVSDLIQEIAAASEEQ 482

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1222409393 461 TLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQVF 509
Cdd:COG0840   483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRF 531
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-136 1.87e-17

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.99  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  13 LLKDGSTLMSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDH 92
Cdd:COG2202    16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1222409393  93 YWVRANVTPVY-HQDELTGYISV-RNIPLR----EEIDAAEKLYNAVNEN 136
Cdd:COG2202    96 FWVELSISPVRdEDGEITGFVGIaRDITERkraeEALRESEERLRLLVEN 145
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
169-509 1.89e-73

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 242.23  E-value: 1.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 169 INAGIIISALAILALQLIALPLAAKMAATVVMFILLALFLQKQVSSPLKKILTQMQKVVSGRKADYFQFNRVDEIGLLMR 248
Cdd:COG0840   163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 249 MVNQSGLNLNSLVGDVNTQLLGIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTS 328
Cdd:COG0840   243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 329 ANAMKSGDVMKQTISMMQSVSRDN--------------GQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVA 394
Cdd:COG0840   323 ELAEEGGEVVEEAVEGIEEIRESVeetaetieelgessQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 395 AEVRNLAQHSASAAKEIKSLIEKNVANVSSGVVMVESTESH--------------LTAMIDSVIQMSTMIKEIGTATQEQ 460
Cdd:COG0840   403 DEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEveegvelveeageaLEEIVEAVEEVSDLIQEIAAASEEQ 482

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1222409393 461 TLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQVF 509
Cdd:COG0840   483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRF 531
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
190-509 4.04e-64

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 217.90  E-value: 4.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 190 LAAKMAATVVMFILLALFLQKQVSSPLKKILTQMQKVVSGRKADYFQFNRVDEIGLLMRMVNQSGLNLNSLVGDVNTQLL 269
Cdd:PRK15041  196 LVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGAN 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 270 GIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTISMMQSVS 349
Cdd:PRK15041  276 AIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIS 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 350 RDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLIEKNVANVSSGVVMV 429
Cdd:PRK15041  356 TSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLV 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 430 ESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQVF 509
Cdd:PRK15041  436 ESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 263-509 4.12e-61

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: 201.36  E-value: 4.12e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  263 DVNTQLLGIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTI 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  343 SMMQSVSRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLI------- 415
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  416 -------EKNVANVSSGVVMVESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRIGVMTHNNNSMVEHV 488
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|.
gi 1222409393  489 TDAACDLSSRAARLQRAVQVF 509
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 290-474 7.50e-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: 169.73  E-value: 7.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 290 EETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTISMMQSVSRDNGQIVDIIGVIDSIAFQT 369
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 370 NILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLI--------------EKNVANVSSGVVMVESTESH 435
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIeeiqeqteeaveamEETSEEVEEGVELVEETGRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1222409393 436 LTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRI 474
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 324-474 4.36e-44

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: 153.36  E-value: 4.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 324 ADQTSANAMKSGDVMKQTISMMQSVSRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQH 403
Cdd:pfam00015   4 AQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 404 SASAAKEIKSLIEKNVAN--------------VSSGVVMVESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQ 469
Cdd:pfam00015  84 SAQAAKEIEALIIEIQKQtndstasiestrqrVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQ 163


                  ....*
gi 1222409393 470 SVSRI 474
Cdd:pfam00015 164 AVARM 168
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-136 1.87e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.99  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  13 LLKDGSTLMSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDH 92
Cdd:COG2202    16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1222409393  93 YWVRANVTPVY-HQDELTGYISV-RNIPLR----EEIDAAEKLYNAVNEN 136
Cdd:COG2202    96 FWVELSISPVRdEDGEITGFVGIaRDITERkraeEALRESEERLRLLVEN 145
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-103 4.04e-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: 65.05  E-value: 4.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222409393  30 ISYANSAFIEASGYEEGELMG--EPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVTPVY 103
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 21-117 1.35e-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: 57.22  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  21 MSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVT 100
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96

                          90
                  ....*....|....*....
gi 1222409393 101 PVYHQ-DELTGYISV-RNI 117
Cdd:TIGR02938  97 PVLNEaGETTHFLGMhRDI 115
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 32-128 4.25e-08

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 56.00  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  32 YANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVTPVYHQD-ELTG 110
Cdd:PRK13558  175 YINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDgTVTH 254

                          90
                  ....*....|....*....
gi 1222409393 111 YISVRN-IPLREEIDAAEK 128
Cdd:PRK13558  255 YVGFQTdVTERKEAELALQ 273
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 18-114 2.04e-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: 46.47  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  18 STLMSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRA 97
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81

                          90
                  ....*....|....*..
gi 1222409393  98 NVTPVYHQDELTGYISV 114
Cdd:cd00130    82 SLTPIRDEGGEVIGLLG 98
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
169-509 1.89e-73

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 242.23  E-value: 1.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 169 INAGIIISALAILALQLIALPLAAKMAATVVMFILLALFLQKQVSSPLKKILTQMQKVVSGRKADYFQFNRVDEIGLLMR 248
Cdd:COG0840   163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 249 MVNQSGLNLNSLVGDVNTQLLGIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTS 328
Cdd:COG0840   243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 329 ANAMKSGDVMKQTISMMQSVSRDN--------------GQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVA 394
Cdd:COG0840   323 ELAEEGGEVVEEAVEGIEEIRESVeetaetieelgessQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 395 AEVRNLAQHSASAAKEIKSLIEKNVANVSSGVVMVESTESH--------------LTAMIDSVIQMSTMIKEIGTATQEQ 460
Cdd:COG0840   403 DEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEveegvelveeageaLEEIVEAVEEVSDLIQEIAAASEEQ 482

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1222409393 461 TLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQVF 509
Cdd:COG0840   483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRF 531
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
190-509 4.04e-64

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 217.90  E-value: 4.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 190 LAAKMAATVVMFILLALFLQKQVSSPLKKILTQMQKVVSGRKADYFQFNRVDEIGLLMRMVNQSGLNLNSLVGDVNTQLL 269
Cdd:PRK15041  196 LVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGAN 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 270 GIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTISMMQSVS 349
Cdd:PRK15041  276 AIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIS 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 350 RDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLIEKNVANVSSGVVMV 429
Cdd:PRK15041  356 TSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLV 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 430 ESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQVF 509
Cdd:PRK15041  436 ESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 196-509 4.80e-64

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 217.57  E-value: 4.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 196 ATVVMFILLALF--LQKQVSSPLKKILTQMQKVVSGRKADYFQFNRVDEIGLLMRMVNQSGLNLNSLVGDVNTQLLGIRK 273
Cdd:PRK15048  198 ALVVVLILLVAWygIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 274 ISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTISMMQSVSRDNG 353
Cdd:PRK15048  278 GTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSK 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 354 QIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLIEKNVANVSSGVVMVESTE 433
Cdd:PRK15048  358 KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAG 437

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222409393 434 SHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQVF 509
Cdd:PRK15048  438 ETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAF 513
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 263-509 4.12e-61

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: 201.36  E-value: 4.12e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  263 DVNTQLLGIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTI 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  343 SMMQSVSRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLI------- 415
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  416 -------EKNVANVSSGVVMVESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRIGVMTHNNNSMVEHV 488
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|.
gi 1222409393  489 TDAACDLSSRAARLQRAVQVF 509
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
198-509 1.50e-58

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 202.61  E-value: 1.50e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 198 VVMFILLALFL-------QKQVSSPLKKILTQMQKVVSG---RKADYFQFNRVDEIGLLMRMVNQSglnLNSLVGDVNTQ 267
Cdd:PRK09793  193 ISMIIVAAIYIssalwwtRKMIVQPLAIIGSHFDSIAAGnlaRPIAVYGRNEITAIFASLKTMQQA---LRGTVSDVRKG 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 268 LLGIRKISQRIAEEGESLQKRTEETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTISMMQS 347
Cdd:PRK09793  270 SQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQE 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 348 VSRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLIEKNVANVSSGVV 427
Cdd:PRK09793  350 IATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSK 429

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 428 MVESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRIGVMTHNNNSMVEHVTDAACDLSSRAARLQRAVQ 507
Cdd:PRK09793  430 LVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVA 509


                  ..
gi 1222409393 508 VF 509
Cdd:PRK09793  510 VF 511
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 290-474 7.50e-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: 169.73  E-value: 7.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 290 EETSADLHQTAAAVEEIASAVKQTAETASEAMTRADQTSANAMKSGDVMKQTISMMQSVSRDNGQIVDIIGVIDSIAFQT 369
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 370 NILALNAAVEAARAGESGRGFAVVAAEVRNLAQHSASAAKEIKSLI--------------EKNVANVSSGVVMVESTESH 435
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIeeiqeqteeaveamEETSEEVEEGVELVEETGRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1222409393 436 LTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQSVSRI 474
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 324-474 4.36e-44

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: 153.36  E-value: 4.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 324 ADQTSANAMKSGDVMKQTISMMQSVSRDNGQIVDIIGVIDSIAFQTNILALNAAVEAARAGESGRGFAVVAAEVRNLAQH 403
Cdd:pfam00015   4 AQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393 404 SASAAKEIKSLIEKNVAN--------------VSSGVVMVESTESHLTAMIDSVIQMSTMIKEIGTATQEQTLALQLINQ 469
Cdd:pfam00015  84 SAQAAKEIEALIIEIQKQtndstasiestrqrVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQ 163


                  ....*
gi 1222409393 470 SVSRI 474
Cdd:pfam00015 164 AVARM 168
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-136 1.87e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.99  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  13 LLKDGSTLMSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDH 92
Cdd:COG2202    16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1222409393  93 YWVRANVTPVY-HQDELTGYISV-RNIPLR----EEIDAAEKLYNAVNEN 136
Cdd:COG2202    96 FWVELSISPVRdEDGEITGFVGIaRDITERkraeEALRESEERLRLLVEN 145
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-103 4.04e-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: 65.05  E-value: 4.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222409393  30 ISYANSAFIEASGYEEGELMG--EPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVTPVY 103
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 21-117 1.35e-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: 57.22  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  21 MSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVT 100
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96

                          90
                  ....*....|....*....
gi 1222409393 101 PVYHQ-DELTGYISV-RNI 117
Cdd:TIGR02938  97 PVLNEaGETTHFLGMhRDI 115
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 32-128 4.25e-08

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 56.00  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  32 YANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVTPVYHQD-ELTG 110
Cdd:PRK13558  175 YINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDgTVTH 254

                          90
                  ....*....|....*....
gi 1222409393 111 YISVRN-IPLREEIDAAEK 128
Cdd:PRK13558  255 YVGFQTdVTERKEAELALQ 273
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 21-129 7.48e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 51.14  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  21 MSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKN-RRTNGDHYWVRANV 99
Cdd:TIGR00229  16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSEIWVEVSV 95

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1222409393 100 TPVYHQDELTGYIS-VRNIPLREEidAAEKL 129
Cdd:TIGR00229  96 SPIRTNGGELGVVGiVRDITERKE--AEEAL 124
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 6.17e-07

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 48.18  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  30 ISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESW-TGLVKNRRTNGDHYWVRANVTPVYHQDEL 108
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESrGFEVSFRVPDGRPRHVEVRASPVRDAGGE 102


                  ....*..
gi 1222409393 109 TGYISVR 115
Cdd:pfam00989 103 ILGFLGV 109
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 27-117 8.25e-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: 47.07  E-value: 8.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  27 QSYISYANSAFIEASGYEEGELMGEP-HNIIRHPDmPPAAFADMWFTIQQGesWTGLVKNRRTNGDHYWVRANVTPVYHQ 105
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPE-DSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....
gi 1222409393 106 D-ELTGYISV-RNI 117
Cdd:pfam13426  78 GgELVGIIAIlRDI 91
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 18-114 2.04e-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: 46.47  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  18 STLMSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRA 97
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81

                          90
                  ....*....|....*..
gi 1222409393  98 NVTPVYHQDELTGYISV 114
Cdd:cd00130    82 SLTPIRDEGGEVIGLLG 98
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
23-129 2.76e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 46.38  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  23 TTNTQSYISYANSAFIEASGYEEGELMGEP-HNIIRHPDMPPAAFADmwfTIQQGES-WTGLVKNRRTNGDHYWVRANVT 100
Cdd:COG3852    22 VLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPEDSPLRELLER---ALAEGQPvTEREVTLRRKDGEERPVDVSVS 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1222409393 101 PVYHQDELTGYISV-RNIPLREEIDA----AEKL 129
Cdd:COG3852    99 PLRDAEGEGGVLLVlRDITERKRLERelrrAEKL 132
PRK13559 PRK13559
hypothetical protein; Provisional
 30-106 4.76e-05

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 45.58  E-value: 4.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222409393  30 ISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVTPVYHQD 106
Cdd:PRK13559   68 IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGED 144
PAS COG2202
PAS domain [Signal transduction mechanisms];
20-126 5.72e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.02  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222409393  20 LMSTTNTQSYISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQG-ESWTGLVKNRRTNGDHYWVRAN 98
Cdd:COG2202   149 GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEAS 228

                          90       100
                  ....*....|....*....|....*....
gi 1222409393  99 VTPVYHQDELTGYISV-RNIPLREEIDAA 126
Cdd:COG2202   229 AVPLRDGGEVIGVLGIvRDITERKRAEEA 257
PRK13557 PRK13557
histidine kinase; Provisional
 30-106 5.85e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 42.35  E-value: 5.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222409393  30 ISYANSAFIEASGYEEGELMGEPHNIIRHPDMPPAAFADMWFTIQQGESWTGLVKNRRTNGDHYWVRANVTPVYHQD 106
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131
 
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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