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Conserved domains on  [gi|1236137327|ref|WP_094935460|]
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MULTISPECIES: methyl-accepting chemotaxis protein [Enterobacter cloacae complex]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 1000955)

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:  1.10.287.950
Gene Ontology:  GO:0006935
PubMed:  18165013|20738376
SCOP:  4003862

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 ...
 16-563 1.73e-141

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 PRK15048:

Pssm-ID: 481250 [Multi-domain]  Cd Length: 553  Bit Score: 420.57  E-value: 1.73e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  16 LHHIRLVPLFSSILGGIILLFALSSGLAgYFLLQADNDQQDVTSEIQVRMG-LSNSSNHLRTARINLihAGAASRIAeMD 94
Cdd:PRK15048    2 INRIRVVTLLVMVLGVFALLQLISGSLF-FSSLHHSQKSFVVSNQLREQQGeLTSTWDLMLQTRINL--SRSAVRMM-MD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  95 AMKQNIS-------EAETRIKQSQESFTAYMNRAVRTAEGAAlDEDLKARYDAYIAGMQPMVKFAKNGMFEAIInhenet 167
Cdd:PRK15048   78 SSNQQSNakvelldSARKTLAQAATHYKKFKSMAPLPEMVAT-SRNIDEKYKNYYTALTELIDYLDYGNTGAYF------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 168 ARPLDDAYNAV--LLKAIKIRTER--ANALTAQAH----SRTQLGLMfmvgAFALALVLTAMTFVVlRRTVINPLQRAAK 239
Cdd:PRK15048  151 AQPTQGMQNAMgeAFAQYALSSEKlyRDIVTDNADdyrfAQWQLAVI----ALVVVLILLVAWYGI-RRMLLTPLAKIIA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 240 RIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAA 319
Cdd:PRK15048  226 HIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 320 SMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAA 399
Cdd:PRK15048  306 SMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 400 RAGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQS 479
Cdd:PRK15048  386 RAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQS 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 480 RGIVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQGARLTEAVGAFRLSG----AKSGRVVTSAPVAKNAPLRPAATV 555
Cdd:PRK15048  466 RGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAAspltNKPQTPSRPASEQPPAQPRLRIAE 545


                  ....*...
gi 1236137327 556 PGDNWETF 563
Cdd:PRK15048  546 QDPNWETF 553
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 16-563 1.73e-141

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 420.57  E-value: 1.73e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  16 LHHIRLVPLFSSILGGIILLFALSSGLAgYFLLQADNDQQDVTSEIQVRMG-LSNSSNHLRTARINLihAGAASRIAeMD 94
Cdd:PRK15048    2 INRIRVVTLLVMVLGVFALLQLISGSLF-FSSLHHSQKSFVVSNQLREQQGeLTSTWDLMLQTRINL--SRSAVRMM-MD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  95 AMKQNIS-------EAETRIKQSQESFTAYMNRAVRTAEGAAlDEDLKARYDAYIAGMQPMVKFAKNGMFEAIInhenet 167
Cdd:PRK15048   78 SSNQQSNakvelldSARKTLAQAATHYKKFKSMAPLPEMVAT-SRNIDEKYKNYYTALTELIDYLDYGNTGAYF------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 168 ARPLDDAYNAV--LLKAIKIRTER--ANALTAQAH----SRTQLGLMfmvgAFALALVLTAMTFVVlRRTVINPLQRAAK 239
Cdd:PRK15048  151 AQPTQGMQNAMgeAFAQYALSSEKlyRDIVTDNADdyrfAQWQLAVI----ALVVVLILLVAWYGI-RRMLLTPLAKIIA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 240 RIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAA 319
Cdd:PRK15048  226 HIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 320 SMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAA 399
Cdd:PRK15048  306 SMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 400 RAGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQS 479
Cdd:PRK15048  386 RAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQS 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 480 RGIVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQGARLTEAVGAFRLSG----AKSGRVVTSAPVAKNAPLRPAATV 555
Cdd:PRK15048  466 RGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAAspltNKPQTPSRPASEQPPAQPRLRIAE 545


                  ....*...
gi 1236137327 556 PGDNWETF 563
Cdd:PRK15048  546 QDPNWETF 553
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
24-529 6.15e-87

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 279.21  E-value: 6.15e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  24 LFSSILGGIILLFALSSGLAGYFLLQADNDQQDVTSEIQVRMGLSNSSNHLRTARINLIHAGAASRIAEMDAMKQNISEA 103
Cdd:COG0840     6 LLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 104 ETRIKQSQESFTAYMNRAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETARPLDDAYNAVLLKAI 183
Cdd:COG0840    86 LALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 184 KIRTERANALTAQAHSRTQLGLMFMVGAFALALVLtamtfvVLRRTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGR 263
Cdd:COG0840   166 LLEAAALALAAAALALALLAAALLALVALAIILAL------LLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 264 LTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAE 343
Cdd:COG0840   240 LADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 344 DASGKASRGGQMVSGVV--------------KTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFA 409
Cdd:COG0840   320 EASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 410 VVASEVRTLASRSANAAKEIESLINESVS--------------LIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAAS 475
Cdd:COG0840   400 VVADEVRKLAERSAEATKEIEELIEEIQSeteeaveameegseEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAAS 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1236137327 476 DEQSRGIVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQGARLTEAVGAFRL 529
Cdd:COG0840   480 EEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 281-528 3.98e-63

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: 207.91  E-value: 3.98e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  281 TVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVV 360
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  361 KTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTLASRSANAAKEIESLINE----- 435
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  436 ---------SVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRGIVQVSQAISEMDKVTQQNASLVEEA 506
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 1236137327  507 SAAAASLEEQGARLTEAVGAFR 528
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 308-503 1.50e-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: 193.61  E-value: 1.50e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 308 EQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQT 387
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 388 NILALNAAVEAARAGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDI 467
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1236137327 468 MLEIAAASDEQSRGIVQVSQAISEMDKVTQQNASLV 503
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 339-496 2.21e-57

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: 189.57  E-value: 2.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 339 SKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTL 418
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 419 ASRSANAAKEIESLINE--------------SVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRGIVQ 484
Cdd:pfam00015  81 AERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 1236137327 485 VSQAISEMDKVT 496
Cdd:pfam00015 161 VNQAVARMDQVT 172
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 16-563 1.73e-141

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 420.57  E-value: 1.73e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  16 LHHIRLVPLFSSILGGIILLFALSSGLAgYFLLQADNDQQDVTSEIQVRMG-LSNSSNHLRTARINLihAGAASRIAeMD 94
Cdd:PRK15048    2 INRIRVVTLLVMVLGVFALLQLISGSLF-FSSLHHSQKSFVVSNQLREQQGeLTSTWDLMLQTRINL--SRSAVRMM-MD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  95 AMKQNIS-------EAETRIKQSQESFTAYMNRAVRTAEGAAlDEDLKARYDAYIAGMQPMVKFAKNGMFEAIInhenet 167
Cdd:PRK15048   78 SSNQQSNakvelldSARKTLAQAATHYKKFKSMAPLPEMVAT-SRNIDEKYKNYYTALTELIDYLDYGNTGAYF------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 168 ARPLDDAYNAV--LLKAIKIRTER--ANALTAQAH----SRTQLGLMfmvgAFALALVLTAMTFVVlRRTVINPLQRAAK 239
Cdd:PRK15048  151 AQPTQGMQNAMgeAFAQYALSSEKlyRDIVTDNADdyrfAQWQLAVI----ALVVVLILLVAWYGI-RRMLLTPLAKIIA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 240 RIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAA 319
Cdd:PRK15048  226 HIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 320 SMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAA 399
Cdd:PRK15048  306 SMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 400 RAGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQS 479
Cdd:PRK15048  386 RAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQS 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 480 RGIVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQGARLTEAVGAFRLSG----AKSGRVVTSAPVAKNAPLRPAATV 555
Cdd:PRK15048  466 RGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAAspltNKPQTPSRPASEQPPAQPRLRIAE 545


                  ....*...
gi 1236137327 556 PGDNWETF 563
Cdd:PRK15048  546 QDPNWETF 553
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
16-563 6.19e-129

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 388.16  E-value: 6.19e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  16 LHHIRLVPLFSSILGgIILLFALSSGlaGYFLLQADNDQQDVTSEIQVRM---GLSNSSNHLRTARINLIHAGA-----A 87
Cdd:PRK15041    2 LKRIKIVTSLLLVLA-VFGLLQLTSG--GLFFNALKNDKENFTVLQTIRQqqsTLNGSWVALLQTRNTLNRAGIrymmdQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  88 SRIAEMDAMKQNISEAETRIKQSQESFTAY--MNRAVRTAEGAALDedLKARYDAYIAGMQPMVKFAKNGMFEAIINHEN 165
Cdd:PRK15041   79 NNIGSGSTVAELMQSASISLKQAEKNWADYeaLPRDPRQSTAAAAE--IKRNYDIYHNALAELIQLLGAGKINEFFDQPT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 166 ETARP-LDDAYNAVLL---KAIKIRTERANALTAQAhsrtqlgLMFMVGAFALALVLTAMTFVVLRRTVINPLQRAAKRI 241
Cdd:PRK15041  157 QGYQDgFEKQYVAYMEqndRLYDIAVSDNNASYSQA-------MWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 242 ENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASM 321
Cdd:PRK15041  230 RHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 322 EQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARA 401
Cdd:PRK15041  310 EQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 402 GEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRG 481
Cdd:PRK15041  390 GEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRG 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 482 IVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQGARLTEAVGAFRLSGAKS-GRVVTS--APVAKNAPLRPAATVPGD 558
Cdd:PRK15041  470 IDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQqQRETSAvvKTVTPATPRKMAVADSGE 549


                  ....*
gi 1236137327 559 NWETF 563
Cdd:PRK15041  550 NWETF 554
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
39-529 6.47e-117

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 356.69  E-value: 6.47e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  39 SSGLAGYFLLQADNDQQDVTSEIQVRMGLSNSSNHLRTARINLIHAGAASRIA-EMDAMKQNISEAETRIKQSQESFTAY 117
Cdd:PRK09793   25 SNGMSFWAFRDDLQRLNQVEQSNQQRAALAQTRAVMLQASTALNKAGTLTALSyPADDIKTLMTTARASLTQSTTLFKSF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 118 MNRAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHE-NETARPLDDAYNAVLLKaIKIRTERANALTAQ 196
Cdd:PRK09793  105 MAMTAGNEHVRALQKETEKSFARWHNDLEHQATWLESNQLSDFLTAPvQGSQNAFDVNFEAWQLE-INHVLEAASAQSQR 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 197 AHSRTQLGLMFMVgafALALVLTAMTFVVLRRTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLE 276
Cdd:PRK09793  184 NYQISALVFISMI---IVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALR 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 277 NTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMV 356
Cdd:PRK09793  261 GTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQV 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 357 SGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTLASRSANAAKEIESLINES 436
Cdd:PRK09793  341 STMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEES 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 437 VSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRGIVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQ 516
Cdd:PRK09793  421 VNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQ 500

                         490
                  ....*....|...
gi 1236137327 517 GARLTEAVGAFRL 529
Cdd:PRK09793  501 ADHLSSRVAVFTL 513
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
24-529 6.15e-87

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 279.21  E-value: 6.15e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  24 LFSSILGGIILLFALSSGLAGYFLLQADNDQQDVTSEIQVRMGLSNSSNHLRTARINLIHAGAASRIAEMDAMKQNISEA 103
Cdd:COG0840     6 LLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 104 ETRIKQSQESFTAYMNRAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETARPLDDAYNAVLLKAI 183
Cdd:COG0840    86 LALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 184 KIRTERANALTAQAHSRTQLGLMFMVGAFALALVLtamtfvVLRRTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGR 263
Cdd:COG0840   166 LLEAAALALAAAALALALLAAALLALVALAIILAL------LLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 264 LTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAE 343
Cdd:COG0840   240 LADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 344 DASGKASRGGQMVSGVV--------------KTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFA 409
Cdd:COG0840   320 EASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 410 VVASEVRTLASRSANAAKEIESLINESVS--------------LIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAAS 475
Cdd:COG0840   400 VVADEVRKLAERSAEATKEIEELIEEIQSeteeaveameegseEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAAS 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1236137327 476 DEQSRGIVQVSQAISEMDKVTQQNASLVEEASAAAASLEEQGARLTEAVGAFRL 529
Cdd:COG0840   480 EEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 281-528 3.98e-63

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: 207.91  E-value: 3.98e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  281 TVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVV 360
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  361 KTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTLASRSANAAKEIESLINE----- 435
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  436 ---------SVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRGIVQVSQAISEMDKVTQQNASLVEEA 506
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 1236137327  507 SAAAASLEEQGARLTEAVGAFR 528
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 308-503 1.50e-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: 193.61  E-value: 1.50e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 308 EQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQT 387
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 388 NILALNAAVEAARAGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDI 467
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1236137327 468 MLEIAAASDEQSRGIVQVSQAISEMDKVTQQNASLV 503
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 339-496 2.21e-57

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: 189.57  E-value: 2.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 339 SKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTL 418
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 419 ASRSANAAKEIESLINE--------------SVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRGIVQ 484
Cdd:pfam00015  81 AERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 1236137327 485 VSQAISEMDKVT 496
Cdd:pfam00015 161 VNQAVARMDQVT 172
TarH pfam02203
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a ...
 40-190 9.37e-29

Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a number of methyl-accepting chemotaxis receptors, such as E.coli Tar (taxis to aspartate and repellents), which is a receptor for the attractant L-aspartate and also recognizes proteogenic amino acids, phthalic acid, Malic acid, 3,4-dihydroxymandelic acid, citrate, benzoate and derivatives, protocatechuate, vanillate, quinate, shikimate and dehydroshikimate (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426656 [Multi-domain]  Cd Length: 152  Bit Score: 111.63  E-value: 9.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  40 SGLAGYFLLQADNDQQDV-TSEIQVRMGLSNSSNHLRTARINLIHAGAASRIAEMDAMKQNISEAETRIKQSQESFTAYM 118
Cdd:pfam02203   1 GGLGLSGLSRSNDALREVyTNRLQQQAALADAWLLLLQARLTLNRAGIAALLPDAPDAAELLARARESLAQSDAAWKAYL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236137327 119 NRAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETARPLDDAYNAVLLKAIKIRTERA 190
Cdd:pfam02203  81 ALPRTPDEEEALAAELKAKYDALQDGLAPLIAALRAGDLDAFFDQPTQKIQPLFEALYNAYLALRKFQNDAA 152
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
 53-190 3.25e-20

Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the wild-type bacterial aspartate receptor, Tar.


Pssm-ID: 128614 [Multi-domain]  Cd Length: 135  Bit Score: 86.75  E-value: 3.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327   53 DQQDVTSEIQVRMGLSNSSNHLRTARINLIHAGAASriaemDAMKQNISEAETrIKQSQESFTAYMNRAVRTAEGAALDE 132
Cdd:smart00319   3 SSYQQAALSLSRVLLLQARNNLNRAGIRMMQNNIGS-----KAKKLMTAASES-LKQAEKNYKSYENMTALPRADRALDA 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1236137327  133 DLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETA-RPLDDAYNAVLLKAIKIRTERA 190
Cdd:smart00319  77 ELKEKFQQYITALQELIQILGNGNLGAFFDQPTQGMqDGFDPAYRDWLQQAVALKGQAV 135
Tar_Tsr_sensor cd19407
ligand binding sensor domain of Tar- and Tsr-related chemoreceptors; Escherichia coli Tar ...
 49-179 8.26e-10

ligand binding sensor domain of Tar- and Tsr-related chemoreceptors; Escherichia coli Tar (taxis to aspartate and repellents) and Tsr (taxis to serine and repellents) are homologous transmembrane chemoreceptors that have a high specificity for aspartate and serine, respectively. Both are homodimeric receptors and contain an N-terminal periplasmic ligand binding domain, a transmembrane region, a HAMP domain and a C-terminal cytosolic signaling domain. E. coli Tar mediates bacterial chemotaxis toward attractants, including aspartate (Asp) and maltose, and away from repellents such as nickel and cobalt ions. Tsr has many roles, including sensing of external (serine, leucine) and internal (pH) environments. In Salmonella enterica serovar Typhimurium, Tsr, also called methyl-accepting chemotaxis protein (MCP), is involved in sensing host-derived nitrate in murine intestinal epithelium, thus contributing to invasion of Peyer's patches. This model represents the ligand binding domain of Tar and Tsr.


Pssm-ID: 438625 [Multi-domain]  Cd Length: 131  Bit Score: 56.95  E-value: 8.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  49 QADNDQQDVtseiqvrmgLSNSSNHLRTARINLIHAGAASRIAEMD----AMKQNISEAETRIKQSQESFTAYMNRAVRT 124
Cdd:cd19407     1 QQLRQQQSA---------LNDSWVALLQARNTLNRAAIRYLLDANNgggaAVAELLDQAKKSLAQAEKHFAQFKALPKLP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1236137327 125 AEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETA-RPLDDAYNAVL 179
Cdd:cd19407    72 GQDEALAAELEQSYQAYHDALAELIQFLEAGNIDAFLDQPTQGYqDAFEKAYNAYL 127
HAMP pfam00672
HAMP domain;
225-277 3.46e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 49.93  E-value: 3.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1236137327 225 VLRRTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLEN 277
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
228-280 8.39e-08

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 48.78  E-value: 8.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1236137327  228 RTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTVG 280
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 231-275 2.54e-06

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 44.36  E-value: 2.54e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1236137327 231 INPLQRAAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSL 275
Cdd:cd06225     1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
1-491 7.79e-06

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 48.96  E-value: 7.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327   1 MDNTTSMQAQRKLSFLHHIRLVPLFSSILGGIILLFALSSGLAGYFLLQADNDQQDVTSEIQVRMGLSNSSNHLRTARIN 80
Cdd:COG2770     7 ALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  81 LIHAGAASRIAEMDAMKQNISEAETRIKQSQESFTAYMNRAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAI 160
Cdd:COG2770    87 LAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 161 INHENETARPLDDAYNAVLLKAIKIRTERANALTAQAHSRTQLGLMFMVGAFALALVLTAMTFVVLRRTVINPLQRAAKR 240
Cdd:COG2770   167 ALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 241 IENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAAS 320
Cdd:COG2770   247 ARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 321 MEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGVVKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAAR 400
Cdd:COG2770   327 ALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLE 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 401 AGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSLIDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSR 480
Cdd:COG2770   407 LALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGA 486

                         490
                  ....*....|.
gi 1236137327 481 GIVQVSQAISE 491
Cdd:COG2770   487 LELLLLEEEEE 497
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
 31-197 1.76e-05

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 432749 [Multi-domain]  Cd Length: 181  Bit Score: 45.71  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  31 GIILLFALSSGLAGYFLLQADNDQQDVTSE---IQVRMgLSNSSNHLRTARINLIHAGAASRIAEMDAMKQNISEAETRI 107
Cdd:pfam12729  13 LLLALLLIIVGVVGLYSLKQINDNLDTMYEdrlLPIKW-LGDIRANLLELRANLLELILTTDPAERDELLKDIEELRAEI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 108 KQSQESFtaymNRAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETARPLDDAYNAVLLKAIKIRT 187
Cdd:pfam12729  92 DKLLEKY----EKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKAGNKDEAYQLYKTEGRPAREAMIEALEELVDYNL 167

                         170
                  ....*....|
gi 1236137327 188 ERANALTAQA 197
Cdd:pfam12729 168 KVAKEAYKDN 177
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 199-271 1.51e-04

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 44.18  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236137327 199 SRTQLGLMFMVGAFALALVLTAMTF-VVLRRTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQTM 271
Cdd:COG5000     1 SGLQILFLLLLLLIALLLLLLALWLaLLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRM 74
MCP2201-like_sensor cd19411
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
 91-197 6.49e-04

ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.


Pssm-ID: 438629 [Multi-domain]  Cd Length: 138  Bit Score: 40.31  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  91 AEMDAMKQNISEAETRIKQSQESFTAymnrAVRTAEGAALDEDLKARYDAYIAGMQPMVKFAKNGMFEAIINHENETARP 170
Cdd:cd19411    36 AERAKELARIAAARARITELLKKLEK----LITSPEGKALLAAIAEARAAYLAARDKVLELKKAGDREEARALLLGELRP 111

                          90       100
                  ....*....|....*....|....*..
gi 1236137327 171 LDDAYNAVLLKAIKIRTERANALTAQA 197
Cdd:cd19411   112 AQAAYLAALDALVDYQEELMDAAAAEA 138
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 277-357 1.30e-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 [Multi-domain]  Cd Length: 262  Bit Score: 40.73  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327  277 NTVGTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMV 356
Cdd:smart00283 179 ELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELV 258


                   .
gi 1236137327  357 S 357
Cdd:smart00283 259 E 259
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 200-488 2.91e-03

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 40.25  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 200 RTQLGLMFMVGAFALALVLTAMTFVVLRRTVINPLQRAAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQTMQHSLENTV 279
Cdd:COG3850   112 AAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELY 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 280 GTVRQGAEEIYRGTSEISAGNTDLSSRTEQQAAAIEQTAASMEQLTATVKQNADNAHHASKLAEDASGKASRGGQMVSGV 359
Cdd:COG3850   192 AELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLL 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 360 VKTMGNISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTLASRSANAAKEIESLINESVSL 439
Cdd:COG3850   272 LLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQA 351

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1236137327 440 IDQGSGEVVAAGNTMNEIVEAVKRVTDIMLEIAAASDEQSRGIVQVSQA 488
Cdd:COG3850   352 ALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQG 400
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 158-269 2.96e-03

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 40.44  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236137327 158 EAIINHENETARPLDDAYNAVLLKAikirTERANALTAQAHSRTQLGLMFMVGAFALALVLT-AMTFVVLRRTVINPLQR 236
Cdd:COG4192   282 EALAEENNSILEQLRTQISGLVGNS----REQLVALNQETAQLVQQSGILLLAIALLSLLLAvLINYFYVRRRLVKRLNA 357

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1236137327 237 AAKRIENIAKGDLTMPDDVAGRSEIGRLTRDLQ 269
Cdd:COG4192   358 LSDAMAAIAAGDLDVPIPVDGNDEIGRIARLLR 390
HAMP_2 pfam18947
HAMP domain;
230-284 3.45e-03

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 36.31  E-value: 3.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1236137327 230 VINPLQRAAKRIENIAKGDLT--MPDDVAGrseigrltrDLQTMQHSLENTVGTVRQ 284
Cdd:pfam18947  20 IITPLNEAADYVDRISKGDIPekITDEYKG---------DFNEIKNNLNALIDAINA 67
 
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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