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Conserved domains on  [gi|53717276|ref|YP_106083|]
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methyl-accepting chemotaxis protein [Burkholderia mallei ATCC 23344]

Protein Classification

PAS and MCP_signal domain-containing protein (domain architecture ID 12092684)

PAS and MCP_signal domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MCPsignal super family cl28165
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
199-494 3.84e-92

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.


The actual alignment was detected with superfamily member PRK15041:

Pssm-ID: 332985  Cd Length: 554  Bit Score: 294.55  E-value: 3.84e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  199 PLRTLRRQALDVATGASRRGVNMNRVDEIGMSLRTINQLGLMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSARTEQAAT 278
Cdd:PRK15041 221 PMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAA 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  279 SVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQTNILAL 358
Cdd:PRK15041 301 SLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILAL 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  359 NAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEIS 438
Cdd:PRK15041 381 NAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIA 460
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 53717276  439 ASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVFR 494
Cdd:PRK15041 461 SASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
10-82 1.25e-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: 312074  Cd Length: 89  Bit Score: 65.05  E-value: 1.25e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53717276    10 ITYANATFVHVSGFSSDEIVGAPHNVVR--HPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPV 82
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDlvHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPI 75
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
199-494 3.84e-92

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 294.55  E-value: 3.84e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  199 PLRTLRRQALDVATGASRRGVNMNRVDEIGMSLRTINQLGLMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSARTEQAAT 278
Cdd:PRK15041 221 PMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAA 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  279 SVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQTNILAL 358
Cdd:PRK15041 301 SLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILAL 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  359 NAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEIS 438
Cdd:PRK15041 381 NAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIA 460
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 53717276  439 ASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVFR 494
Cdd:PRK15041 461 SASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
247-494 2.89e-76

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  Cd Length: 262  Bit Score: 243.73  E-value: 2.89e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    247 DVSEQVLTVQRAVNEIAQGNHDLSARTEQAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVV 326
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    327 STMGEITESSRRISEIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIG------ 400
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    401 --------ASVERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQS 472
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 53717276    473 AAASESLRQQATLLVDAVGVFR 494
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
195-494 4.13e-70

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 232.19  E-value: 4.13e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 195 QIARPLRTLRRQALDVATGASRRGVNMNRVDEIGMSLRTINQLGLMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSARTE 274
Cdd:COG0840  83 AILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARAD 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 275 QAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEIT-----------ESSRRISEII 343
Cdd:COG0840 163 QQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEIT 242
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 344 GVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIG--------------ASVERVESG 409
Cdd:COG0840 243 SVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEeiqneaadavehmeESASEVSEG 322
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 410 AQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDA 489
Cdd:COG0840 323 VKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLEL 402

                ....*
gi 53717276 490 VGVFR 494
Cdd:COG0840 403 VAKFK 407
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
308-493 6.98e-63

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: 278444  Cd Length: 207  Bit Score: 206.53  E-value: 6.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   308 SESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRALAQR 387
Cdd:pfam00015   8 SEEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAER 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   388 SANAAKEIKALIGASV--------------ERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQRAGVTQVDD 453
Cdd:pfam00015  88 SAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQ 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 53717276   454 AVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVF 493
Cdd:pfam00015 168 AVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
274-473 8.09e-61

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  Cd Length: 200  Bit Score: 200.93  E-value: 8.09e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 274 EQAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQT 353
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 354 NILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSDL 433
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 53717276 434 IAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSA 473
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
10-82 1.25e-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: 312074  Cd Length: 89  Bit Score: 65.05  E-value: 1.25e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53717276    10 ITYANATFVHVSGFSSDEIVGAPHNVVR--HPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPV 82
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDlvHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPI 75
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
1-92 7.73e-10

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  Cd Length: 494  Bit Score: 60.69  E-value: 7.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276     1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAV 80
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96
                          90
                  ....*....|...
gi 53717276    81 PVI-RGGQTQGYM 92
Cdd:TIGR02938  97 PVLnEAGETTHFL 109
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
4-94 2.74e-07

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


Pssm-ID: 238075  Cd Length: 103  Bit Score: 49.55  E-value: 2.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   4 TDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPVI 83
Cdd:cd00130   8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87
                        90
                ....*....|.
gi 53717276  84 RGGQTQGYMSV 94
Cdd:cd00130  88 DEGGEVIGLLG 98
PRK13558 PRK13558
bacterio-opsin activator; Provisional
4-82 4.95e-06

bacterio-opsin activator; Provisional


Pssm-ID: 237426  Cd Length: 665  Bit Score: 49.07  E-value: 4.95e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53717276    4 TDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPV 82
Cdd:PRK13558 167 TLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPI 245
PAS COG2202
PAS domain [Signal transduction mechanisms];
1-96 6.47e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112  Cd Length: 232  Bit Score: 47.15  E-value: 6.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATL--KRGEPWTALVKNRRKNGDHY-WVRA 77
Cdd:COG2202 125 IWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALaeGRGGPLEIEYRVRRKDGERVrWILS 204
                        90
                ....*....|....*....
gi 53717276  78 NAVPVIRGGQTQGYMSVRT 96
Cdd:COG2202 205 RISPVRDDGEIVGVVGIAR 223
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
199-494 3.84e-92

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 294.55  E-value: 3.84e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  199 PLRTLRRQALDVATGASRRGVNMNRVDEIGMSLRTINQLGLMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSARTEQAAT 278
Cdd:PRK15041 221 PMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAA 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  279 SVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQTNILAL 358
Cdd:PRK15041 301 SLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILAL 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  359 NAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEIS 438
Cdd:PRK15041 381 NAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIA 460
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 53717276  439 ASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVFR 494
Cdd:PRK15041 461 SASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
196-494 6.41e-92

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 293.13  E-value: 6.41e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  196 IARPLRTLRRQALDVATGASRRGVNM---NRVDEIGMSLRTINQlglMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSAR 272
Cdd:PRK09793 214 IVQPLAIIGSHFDSIAAGNLARPIAVygrNEITAIFASLKTMQQ---ALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSR 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  273 TEQAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQ 352
Cdd:PRK09793 291 TEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQ 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  353 TNILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSD 432
Cdd:PRK09793 371 TNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVND 450
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53717276  433 LIAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVFR 494
Cdd:PRK09793 451 IMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
209-494 1.27e-91

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 293.07  E-value: 1.27e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  209 DVATGASRRGVNMNRVDEIGMSLRTINQlglMFRWLIDDVS---EQVLTVQRAVNEIAQGNHDLSARTEQAATSVQQTAA 285
Cdd:PRK15048 229 EIAGGNLANTLTIDGRSEMGDLAQSVSH---MQRSLTDTVThvrEGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  286 SMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQTNILALNAAVEAA 365
Cdd:PRK15048 306 SMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAA 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276  366 RAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQR 445
Cdd:PRK15048 386 RAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQS 465
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 53717276  446 AGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVFR 494
Cdd:PRK15048 466 RGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFR 514
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
247-494 2.89e-76

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  Cd Length: 262  Bit Score: 243.73  E-value: 2.89e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    247 DVSEQVLTVQRAVNEIAQGNHDLSARTEQAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVV 326
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    327 STMGEITESSRRISEIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIG------ 400
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    401 --------ASVERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQS 472
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 53717276    473 AAASESLRQQATLLVDAVGVFR 494
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
195-494 4.13e-70

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 232.19  E-value: 4.13e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 195 QIARPLRTLRRQALDVATGASRRGVNMNRVDEIGMSLRTINQLGLMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSARTE 274
Cdd:COG0840  83 AILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARAD 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 275 QAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEIT-----------ESSRRISEII 343
Cdd:COG0840 163 QQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEIT 242
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 344 GVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIG--------------ASVERVESG 409
Cdd:COG0840 243 SVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEeiqneaadavehmeESASEVSEG 322
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 410 AQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSAAASESLRQQATLLVDA 489
Cdd:COG0840 323 VKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLEL 402

                ....*
gi 53717276 490 VGVFR 494
Cdd:COG0840 403 VAKFK 407
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
308-493 6.98e-63

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: 278444  Cd Length: 207  Bit Score: 206.53  E-value: 6.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   308 SESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRALAQR 387
Cdd:pfam00015   8 SEEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAER 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   388 SANAAKEIKALIGASV--------------ERVESGAQTVDYAGRTMGEIVSQVKRVSDLIAEISASTSEQRAGVTQVDD 453
Cdd:pfam00015  88 SAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQ 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 53717276   454 AVVHLDSITQQNAALVEQSAAASESLRQQATLLVDAVGVF 493
Cdd:pfam00015 168 AVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
274-473 8.09e-61

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  Cd Length: 200  Bit Score: 200.93  E-value: 8.09e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 274 EQAATSVQQTAASMAQMTATVSSNAQTATQANRLSESASHAAERGGQAVREVVSTMGEITESSRRISEIIGVIDGIAFQT 353
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276 354 NILALNAAVEAARAGEQGRGFAVVAGEVRALAQRSANAAKEIKALIGASVERVESGAQTVDYAGRTMGEIVSQVKRVSDL 433
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 53717276 434 IAEISASTSEQRAGVTQVDDAVVHLDSITQQNAALVEQSA 473
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
10-82 1.25e-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: 312074  Cd Length: 89  Bit Score: 65.05  E-value: 1.25e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53717276    10 ITYANATFVHVSGFSSDEIVGAPHNVVR--HPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPV 82
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDlvHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPI 75
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
1-92 7.73e-10

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  Cd Length: 494  Bit Score: 60.69  E-value: 7.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276     1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAV 80
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96
                          90
                  ....*....|...
gi 53717276    81 PVI-RGGQTQGYM 92
Cdd:TIGR02938  97 PVLnEAGETTHFL 109
PAS_9 pfam13426
PAS domain;
1-88 7.61e-09

PAS domain;


Pssm-ID: 315989  Cd Length: 102  Bit Score: 54.39  E-value: 7.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276     1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAP-HNVVRHPDmPRDAFADMWATLKrgEPWTALVKNRRKNGDHYWVRANA 79
Cdd:pfam13426   4 ILITDPDGRIIYVNPAALRLLGYTREELLGKSlTDLFGEPE-DAERLREALREGR--KVRELEVVLVRKDGEPFPVLVSA 80

                  ....*....
gi 53717276    80 VPVIRGGQT 88
Cdd:pfam13426  81 SPIKDDGGE 89
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1-94 2.33e-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  Cd Length: 124  Bit Score: 49.98  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276     1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKN-RRKNGDHYWVRANA 79
Cdd:TIGR00229  16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSEIWVEVSV 95
                          90
                  ....*....|....*
gi 53717276    80 VPVIRGGQTQGYMSV 94
Cdd:TIGR00229  96 SPIRTNGGELGVVGI 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
4-94 2.74e-07

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


Pssm-ID: 238075  Cd Length: 103  Bit Score: 49.55  E-value: 2.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   4 TDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPVI 83
Cdd:cd00130   8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87
                        90
                ....*....|.
gi 53717276  84 RGGQTQGYMSV 94
Cdd:cd00130  88 DEGGEVIGLLG 98
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1-94 9.11e-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.


Pssm-ID: 307226  Cd Length: 113  Bit Score: 48.18  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276     1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTA-LVKNRRKNGDHYWVRANA 79
Cdd:pfam00989  14 IFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGfEVSFRVPDGRPRHVEVRA 93
                          90
                  ....*....|....*.
gi 53717276    80 VPVI-RGGQTQGYMSV 94
Cdd:pfam00989  94 SPVRdAGGEILGFLGV 109
PRK13558 PRK13558
bacterio-opsin activator; Provisional
4-82 4.95e-06

bacterio-opsin activator; Provisional


Pssm-ID: 237426  Cd Length: 665  Bit Score: 49.07  E-value: 4.95e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53717276    4 TDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPV 82
Cdd:PRK13558 167 TLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPI 245
PAS COG2202
PAS domain [Signal transduction mechanisms];
1-96 6.47e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112  Cd Length: 232  Bit Score: 47.15  E-value: 6.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276   1 MSTTDPHGRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATL--KRGEPWTALVKNRRKNGDHY-WVRA 77
Cdd:COG2202 125 IWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALaeGRGGPLEIEYRVRRKDGERVrWILS 204
                        90
                ....*....|....*....
gi 53717276  78 NAVPVIRGGQTQGYMSVRT 96
Cdd:COG2202 205 RISPVRDDGEIVGVVGIAR 223
PRK13557 PRK13557
histidine kinase; Provisional
1-74 6.37e-04

histidine kinase; Provisional


Pssm-ID: 237425  Cd Length: 540  Bit Score: 41.97  E-value: 6.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53717276    1 MSTTDPH---GRITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYW 74
Cdd:PRK13557  43 MIVTDPNqpdNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFW 119
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
5-92 1.17e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 312075  Cd Length: 110  Bit Score: 38.55  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276     5 DPHGRITYANATFVHVSGFSSDEIVGAPHNVVrHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRANAVPVI- 83
Cdd:pfam08448  12 DPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPLRd 90

                  ....*....
gi 53717276    84 RGGQTQGYM 92
Cdd:pfam08448  91 PDGEVIGVL 99
PRK13559 PRK13559
hypothetical protein; Provisional
1-82 1.28e-03

hypothetical protein; Provisional


Pssm-ID: 237427  Cd Length: 361  Bit Score: 40.96  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    1 MSTTDPHGR---ITYANATFVHVSGFSSDEIVGAPHNVVRHPDMPRDAFADMWATLKRGEPWTALVKNRRKNGDHYWVRA 77
Cdd:PRK13559  56 MCITDPHQPdlpIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135

                 ....*
gi 53717276   78 NAVPV 82
Cdd:PRK13559 136 HLGPV 140
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
226-340 2.40e-03

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  Cd Length: 262  Bit Score: 39.58  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53717276    226 EIGMSLRTINQLGLMFRWLIDDVSEQVLTVQRAVNEIAQGNHDLSARTEQAATSVQQTAASMAQMTATVSSNAQTATQAN 305
Cdd:smart00283 148 EIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIA 227
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 53717276    306 RLSESASHAAERGGQAVREVVSTMGEITESSRRIS 340
Cdd:smart00283 228 QVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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