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Conserved domains on  [gi|516409619|ref|WP_017799017|]
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PAS domain-containing methyl-accepting chemotaxis protein [Erwinia toletana]

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 ...
 211-514 1.27e-87

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: 279.92  E-value: 1.27e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 211 WLEYQIS--RPIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQLGLMFRWLVDDVSGQAINVLSASDAIAQGNND 288
Cdd:PRK15041 211 WFGIKASlvAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNND 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 289 LSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDG 368
Cdd:PRK15041 291 LSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDG 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 369 IAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQ 448
Cdd:PRK15041 371 IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVT 450

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516409619 449 NVTGLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:PRK15041 451 RVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-135 7.28e-21

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 92.01  E-value: 7.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDH 92
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 516409619  93 YWVRANAIPVV-RNGKVHGYMSVRT-----KPTAEEIRQTEQLYREFRE 135
Cdd:COG2202   96 FWVELSISPVRdEDGEITGFVGIARditerKRAEEALRESEERLRLLVE 144
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
211-514 1.27e-87

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 279.92  E-value: 1.27e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 211 WLEYQIS--RPIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQLGLMFRWLVDDVSGQAINVLSASDAIAQGNND 288
Cdd:PRK15041 211 WFGIKASlvAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNND 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 289 LSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDG 368
Cdd:PRK15041 291 LSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDG 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 369 IAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQ 448
Cdd:PRK15041 371 IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVT 450

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516409619 449 NVTGLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:PRK15041 451 RVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
186-514 5.91e-84

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 269.58  E-value: 5.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 186 LLGVAGGQVAAFTAGMALLLLLAGSWLEYQISRPIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQLGLMFRWLV 265
Cdd:COG0840  176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 266 DDVSGQAINVLSASDAIAQGNNDLSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDM 345
Cdd:COG0840  256 GQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEA 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 346 IT--------------MMAEITDSSKKIANITSVIDGIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASA 411
Cdd:COG0840  336 VEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEA 415

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 412 ASEIKTLVETS--------------ATRVRIGTEHVNDAGKTMESIVSQVQNVTGLISQISSATAEQATALSEVSLAVED 477
Cdd:COG0840  416 TKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQ 495

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 516409619 478 LDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:COG0840  496 IAAAAQENAASVEEVAAAAEELAELAEELQELVSRFK 532
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 267-514 4.47e-70

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: 224.86  E-value: 4.47e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   267 DVSGQAINVLSASDAIAQGNNDLSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMI 346
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   347 TMMAEITDSSKKIANITSVIDGIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVET----- 421
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   422 ---------SATRVRIGTEHVNDAGKTMESIVSQVQNVTGLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEG 492
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 516409619   493 AEASDRMSRQATRLVEAISVFR 514
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 294-491 7.75e-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: 190.53  E-value: 7.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 294 EQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDGIAFQT 373
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 374 NILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQNVTGL 453
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 516409619 454 ISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQE 491
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 325-482 1.75e-47

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: 162.60  E-value: 1.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  325 NNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDGIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSL 404
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  405 AQRSASAASEIKTLV--------------ETSATRVRIGTEHVNDAGKTMESIVSQVQNVTGLISQISSATAEQATALSE 470
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 516409619  471 VSLAVEDLDNIT 482
Cdd:pfam00015 161 VNQAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-135 7.28e-21

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 92.01  E-value: 7.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDH 92
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 516409619  93 YWVRANAIPVV-RNGKVHGYMSVRT-----KPTAEEIRQTEQLYREFRE 135
Cdd:COG2202   96 FWVELSISPVRdEDGEITGFVGIARditerKRAEEALRESEERLRLLVE 144
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 3.32e-18

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: 79.30  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   30 ITYANDAFIEVSGFTPEEI--NGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPV-VRNG 106
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELlgKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIrDENG 80


                  ....*....
gi 516409619  107 KVHGYMSVR 115
Cdd:pfam08447  81 KPVRVIGVA 89
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 21-103 1.39e-13

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: 73.01  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   21 MSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAI 100
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96


                  ...
gi 516409619  101 PVV 103
Cdd:TIGR02938  97 PVL 99
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 24-114 3.95e-10

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 56.87  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  24 TDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPVV 103
Cdd:cd00130    8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87

                         90
                 ....*....|.
gi 516409619 104 RNGKVHGYMSV 114
Cdd:cd00130   88 DEGGEVIGLLG 98
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 30-120 5.79e-08

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 55.23  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  30 ITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPV-VRNGKV 108
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIrDEDGTV 252

                         90
                 ....*....|..
gi 516409619 109 HGYMSVRTKPTA 120
Cdd:PRK13558 253 THYVGFQTDVTE 264
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 13-74 9.03e-05

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: 40.46  E-value: 9.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516409619    13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLK 74
Cdd:smart00091   6 ILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
211-514 1.27e-87

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 279.92  E-value: 1.27e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 211 WLEYQIS--RPIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQLGLMFRWLVDDVSGQAINVLSASDAIAQGNND 288
Cdd:PRK15041 211 WFGIKASlvAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNND 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 289 LSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDG 368
Cdd:PRK15041 291 LSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDG 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 369 IAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQ 448
Cdd:PRK15041 371 IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVT 450

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516409619 449 NVTGLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:PRK15041 451 RVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 219-514 6.13e-87

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 278.04  E-value: 6.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 219 PIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQlglMFRWLVDDVSgqaiNVLSASDAI-------AQGNNDLSR 291
Cdd:PRK15048 219 PLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSH---MQRSLTDTVT----HVREGSDAIyagtreiAAGNTDLSS 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 292 RTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDGIAF 371
Cdd:PRK15048 292 RTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAF 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 372 QTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQNVT 451
Cdd:PRK15048 372 QTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVT 451

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516409619 452 GLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:PRK15048 452 DIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFR 514
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
186-514 5.91e-84

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 269.58  E-value: 5.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 186 LLGVAGGQVAAFTAGMALLLLLAGSWLEYQISRPIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQLGLMFRWLV 265
Cdd:COG0840  176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 266 DDVSGQAINVLSASDAIAQGNNDLSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDM 345
Cdd:COG0840  256 GQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEA 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 346 IT--------------MMAEITDSSKKIANITSVIDGIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASA 411
Cdd:COG0840  336 VEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEA 415

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 412 ASEIKTLVETS--------------ATRVRIGTEHVNDAGKTMESIVSQVQNVTGLISQISSATAEQATALSEVSLAVED 477
Cdd:COG0840  416 TKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQ 495

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 516409619 478 LDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:COG0840  496 IAAAAQENAASVEEVAAAAEELAELAEELQELVSRFK 532
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
211-514 4.36e-78

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 254.23  E-value: 4.36e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 211 WLEYQISRPIEQVCKQALSVATGTSHKVDQMDRVDEVGMTLRAIGQLGLMFRWLVDDVSGQAINVLSASDAIAQGNNDLS 290
Cdd:PRK09793 209 WTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLS 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 291 RRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDGIA 370
Cdd:PRK09793 289 SRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIA 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 371 FQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQNV 450
Cdd:PRK09793 369 FQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRV 448

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516409619 451 TGLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEGAEASDRMSRQATRLVEAISVFR 514
Cdd:PRK09793 449 NDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 267-514 4.47e-70

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: 224.86  E-value: 4.47e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   267 DVSGQAINVLSASDAIAQGNNDLSRRTEQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMI 346
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   347 TMMAEITDSSKKIANITSVIDGIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVET----- 421
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   422 ---------SATRVRIGTEHVNDAGKTMESIVSQVQNVTGLISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQEG 492
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 516409619   493 AEASDRMSRQATRLVEAISVFR 514
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 294-491 7.75e-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: 190.53  E-value: 7.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 294 EQAAANVQQTAATMNEMTATVKSNTETAAQVNNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDGIAFQT 373
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619 374 NILALNAAVEAARAGEQGKGFAVVAGEVRSLAQRSASAASEIKTLVETSATRVRIGTEHVNDAGKTMESIVSQVQNVTGL 453
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 516409619 454 ISQISSATAEQATALSEVSLAVEDLDNITHQNAARVQE 491
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 325-482 1.75e-47

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: 162.60  E-value: 1.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  325 NNLSMSTSTAAVAGGKAMSDMITMMAEITDSSKKIANITSVIDGIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRSL 404
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  405 AQRSASAASEIKTLV--------------ETSATRVRIGTEHVNDAGKTMESIVSQVQNVTGLISQISSATAEQATALSE 470
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 516409619  471 VSLAVEDLDNIT 482
Cdd:pfam00015 161 VNQAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-135 7.28e-21

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 92.01  E-value: 7.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDH 92
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSL 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 516409619  93 YWVRANAIPVV-RNGKVHGYMSVRT-----KPTAEEIRQTEQLYREFRE 135
Cdd:COG2202   96 FWVELSISPVRdEDGEITGFVGIARditerKRAEEALRESEERLRLLVE 144
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 30-115 3.32e-18

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: 79.30  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   30 ITYANDAFIEVSGFTPEEI--NGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPV-VRNG 106
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELlgKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIrDENG 80


                  ....*....
gi 516409619  107 KVHGYMSVR 115
Cdd:pfam08447  81 KPVRVIGVA 89
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 21-103 1.39e-13

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: 73.01  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   21 MSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAI 100
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96


                  ...
gi 516409619  101 PVV 103
Cdd:TIGR02938  97 PVL 99
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 14-114 4.31e-12

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: 63.08  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   14 FDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKN-RRKNGDH 92
Cdd:TIGR00229   9 FESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSE 88

                          90       100
                  ....*....|....*....|..
gi 516409619   93 YWVRANAIPVVRNGKVHGYMSV 114
Cdd:TIGR00229  89 IWVEVSVSPIRTNGGELGVVGI 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 13-129 1.45e-10

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: 63.46  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDH 92
Cdd:COG5809  146 IFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRW 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 516409619  93 YWVRANAIPVVRNGKVHGYMSV---RT--KPTAEEIRQTEQL 129
Cdd:COG5809  226 RLLEASGAPIKKNGEVDGIVIIfrdITerKKLEELLRKSEKL 267
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 27-108 2.31e-10

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 57.09  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   27 NSYITYANDAFIEVSGFTPEEINGQP-HNMVRHPDmPPEAFADMWSTLKHGepWTALVKNRRKNGDHYWVRANAIPVVRN 105
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPE-DSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDD 77


                  ...
gi 516409619  106 GKV 108
Cdd:pfam13426  78 GGE 80
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 24-114 3.95e-10

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 56.87  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  24 TDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPVV 103
Cdd:cd00130    8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87

                         90
                 ....*....|.
gi 516409619 104 RNGKVHGYMSV 114
Cdd:cd00130   88 DEGGEVIGLLG 98
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 13-114 1.39e-09

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 55.50  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTA-LVKNRRKNGD 91
Cdd:pfam00989   6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGfEVSFRVPDGR 85

                          90       100
                  ....*....|....*....|....
gi 516409619   92 HYWVRANAIPVV-RNGKVHGYMSV 114
Cdd:pfam00989  86 PRHVEVRASPVRdAGGEILGFLGV 109
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 1-142 9.16e-09

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: 57.47  E-value: 9.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   1 MRNNQPVTQQEYVFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQP-HNMVRHPDMPpeafadmwSTLKHGEPW 79
Cdd:COG3829    4 LELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNvTELIPNSPLL--------EVLKTGKPV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516409619  80 TALVKNRRKNGDHywVRANAIPVVRNGKVHGYMSvrtkpTAEEIRQTEQLYREFREGEGKNRR 142
Cdd:COG3829   76 TGVIQKTGGKGKT--VIVTAIPIFEDGEVIGAVE-----TFRDITELKRLERKLREEELERGL 131
PAS COG2202
PAS domain [Signal transduction mechanisms];
13-128 1.95e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.42  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHG-EPWTALVKNRRKNGD 91
Cdd:COG2202  142 LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGR 221

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 516409619  92 HYWVRANAIPVVRNGKVHGYMSVRTKPTaeEIRQTEQ 128
Cdd:COG2202  222 WVWVEASAVPLRDGGEVIGVLGIVRDIT--ERKRAEE 256
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 30-120 5.79e-08

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 55.23  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  30 ITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPV-VRNGKV 108
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIrDEDGTV 252

                         90
                 ....*....|..
gi 516409619 109 HGYMSVRTKPTA 120
Cdd:PRK13558 253 THYVGFQTDVTE 264
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1-129 1.70e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 53.31  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   1 MRNNQPVTQQeyVFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFadMWSTLKHGEPWT 80
Cdd:COG3852    2 LRESEELLRA--ILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLREL--LERALAEGQPVT 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516409619  81 AL-VKNRRKNGDHYWVRANAIPVVRNGKVHGYMSV-----RTKPTAEEIRQTEQL 129
Cdd:COG3852   78 EReVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVlrditERKRLERELRRAEKL 132
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 13-74 9.03e-05

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: 40.46  E-value: 9.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516409619    13 VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLK 74
Cdd:smart00091   6 ILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 25-112 4.90e-04

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: 39.70  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   25 DLNSYITYANDAFIEVSGFTPEEINGqphnmVRHPDMPP----EAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAI 100
Cdd:pfam08448  12 DPDGRVRYANAAAAELFGLPPEELLG-----KTLAELLPpedaARLERALRRALEGEEPIDFLEELLLNGEERHYELRLT 86

                          90
                  ....*....|...
gi 516409619  101 PVV-RNGKVHGYM 112
Cdd:pfam08448  87 PLRdPDGEVIGVL 99
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 8-133 6.13e-04

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: 42.27  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619   8 TQQEY--VFDNDATLMSTTDLNSYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEaFADMWSTLKHGEPWTALVKN 85
Cdd:COG5809   13 SEQRFrsLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKE-LREILKLLKEGESRDELEFE 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516409619  86 RR-KNGDHYWVRANAIPV-VRNGKVHGYMSV-----RTKPTAEEIRQTEQLYREF 133
Cdd:COG5809   92 LRhKNGKRLEFSSKLSPIfDQNGDIEGMLAIsrditERKRMEEALRESEEKFRLI 146
PRK13557 PRK13557
histidine kinase; Provisional
 21-102 1.13e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 41.58  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409619  21 MSTTDLN---SYITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWvra 97
Cdd:PRK13557  43 MIVTDPNqpdNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFW--- 119


                 ....*...
gi 516409619  98 NAI---PV 102
Cdd:PRK13557 120 NALfvsPV 127
PRK13559 PRK13559
hypothetical protein; Provisional
 30-102 6.39e-03

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 39.03  E-value: 6.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516409619  30 ITYANDAFIEVSGFTPEEINGQPHNMVRHPDMPPEAFADMWSTLKHGEPWTALVKNRRKNGDHYWVRANAIPV 102
Cdd:PRK13559  68 IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPV 140
 
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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