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Conserved domains on  [gi|16132176|ref|NP_418775|]
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methyl-accepting chemotaxis protein Tsr [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 11487580)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
1-551 0e+00

methyl-accepting chemotaxis protein;


:

Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 1021.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
Cdd:PRK15041   1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   81 IGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
Cdd:PRK15041  81 IGSGSTVAELMQSASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  161 DGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
Cdd:PRK15041 161 DGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
Cdd:PRK15041 241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
Cdd:PRK15041 321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
Cdd:PRK15041 401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132176  481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQ---RETSAVVKTVTPAAPRKMAVADSEENWETF 551
Cdd:PRK15041 481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQqqqRETSAVVKTVTPATPRKMAVADSGENWETF 554
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
1-551 0e+00

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 1021.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
Cdd:PRK15041   1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   81 IGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
Cdd:PRK15041  81 IGSGSTVAELMQSASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  161 DGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
Cdd:PRK15041 161 DGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
Cdd:PRK15041 241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
Cdd:PRK15041 321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
Cdd:PRK15041 401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132176  481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQ---RETSAVVKTVTPAAPRKMAVADSEENWETF 551
Cdd:PRK15041 481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQqqqRETSAVVKTVTPATPRKMAVADSGENWETF 554
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
7-517 1.29e-92

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 293.47  E-value: 1.29e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   7 IVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGST 86
Cdd:COG0840   3 ILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  87 VAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQ 166
Cdd:COG0840  83 ALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 167 YVAYMEQNDRLHDIAVsdnnasysQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGS 246
Cdd:COG0840 163 LAALLEAAALALAAAA--------LALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSK 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 247 NEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQA 326
Cdd:COG0840 235 DEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQA 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 327 SHLALSASETAQRGGKVVDNVV--------------QTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 392
Cdd:COG0840 315 AELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEA 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 393 GRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVES--------------AGETMAEIVSAVTRVTDIMGE 458
Cdd:COG0840 395 GRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEgseeveegvelveeAGEALEEIVEAVEEVSDLIQE 474
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16132176 459 IASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
Cdd:COG0840 475 IAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
269-516 8.11e-69

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: 222.55  E-value: 8.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    269 DVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVV 348
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    349 QTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLI------- 421
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    422 -------EDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEES 494
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 16132176    495 AAAAAALEEQASRLTEAVAVFR 516
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
327-484 1.58e-66

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: 213.45  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   327 SHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNL 406
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   407 AQRSAQAAREIKSLI--------------EDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQ 472
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160
                         170
                  ....*....|..
gi 16132176   473 VGLAVAEMDRVT 484
Cdd:pfam00015 161 VNQAVARMDQVT 172
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
296-487 2.66e-62

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: 203.24  E-value: 2.66e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 296 EQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQT 375
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 376 NILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDI 455
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 16132176 456 MGEIASASDEQSRGIDQVGLAVAEMDRVTQQN 487
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
1-551 0e+00

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 1021.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
Cdd:PRK15041   1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   81 IGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
Cdd:PRK15041  81 IGSGSTVAELMQSASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  161 DGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
Cdd:PRK15041 161 DGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
Cdd:PRK15041 241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
Cdd:PRK15041 321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
Cdd:PRK15041 401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132176  481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQ---RETSAVVKTVTPAAPRKMAVADSEENWETF 551
Cdd:PRK15041 481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQqqqRETSAVVKTVTPATPRKMAVADSGENWETF 554
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
1-551 0e+00

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 617.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNN 80
Cdd:PRK15048   1 MINRIRVVTLLVMVLGVFALLQLISGSLFFSSLHHSQKSFVVSNQLREQQGELTSTWDLMLQTRINLSRSAVRMMMDSSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   81 IGSgSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAaEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
Cdd:PRK15048  81 QQS-NAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVATSR-NIDEKYKNYYTALTELIDYLDYGNTGAYFAQPTQGMQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  161 DGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
Cdd:PRK15048 159 NAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
Cdd:PRK15048 239 LTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
Cdd:PRK15048 319 DNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
Cdd:PRK15048 399 GEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEM 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132176  481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPR----KMAVADSEENWETF 551
Cdd:PRK15048 479 DRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPpaqpRLRIAEQDPNWETF 553
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
1-520 5.83e-154

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 451.45  E-value: 5.83e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    1 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQnn 80
Cdd:PRK09793   1 MFNRIRISTTLFLILILCGILQIGSNGMSFWAFRDDLQRLNQVEQSNQQRAALAQTRAVMLQASTALNKAGTLTALSY-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   81 igSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQ 160
Cdd:PRK09793  79 --PADDIKTLMTTARASLTQSTTLFKSFMAMTAGNEHVRALQKETEKSFARWHNDLEHQATWLESNQLSDFLTAPVQGSQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  161 DGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKP 240
Cdd:PRK09793 157 NAFDVNFEAWQLEINHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  241 IEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA 320
Cdd:PRK09793 237 IAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  321 ENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 400
Cdd:PRK09793 317 DNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVA 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  401 GEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
Cdd:PRK09793 397 GEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQM 476
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 16132176  481 DRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQ 520
Cdd:PRK09793 477 DQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEH 516
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
7-517 1.29e-92

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 293.47  E-value: 1.29e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   7 IVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGST 86
Cdd:COG0840   3 ILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  87 VAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQ 166
Cdd:COG0840  83 ALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 167 YVAYMEQNDRLHDIAVsdnnasysQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGS 246
Cdd:COG0840 163 LAALLEAAALALAAAA--------LALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSK 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 247 NEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQA 326
Cdd:COG0840 235 DEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQA 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 327 SHLALSASETAQRGGKVVDNVV--------------QTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 392
Cdd:COG0840 315 AELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEA 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 393 GRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVES--------------AGETMAEIVSAVTRVTDIMGE 458
Cdd:COG0840 395 GRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEgseeveegvelveeAGEALEEIVEAVEEVSDLIQE 474
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16132176 459 IASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
Cdd:COG0840 475 IAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
269-516 8.11e-69

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: 222.55  E-value: 8.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    269 DVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVV 348
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    349 QTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLI------- 421
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    422 -------EDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEES 494
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 16132176    495 AAAAAALEEQASRLTEAVAVFR 516
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
327-484 1.58e-66

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: 213.45  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   327 SHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNL 406
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176   407 AQRSAQAAREIKSLI--------------EDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQ 472
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160
                         170
                  ....*....|..
gi 16132176   473 VGLAVAEMDRVT 484
Cdd:pfam00015 161 VNQAVARMDQVT 172
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
296-487 2.66e-62

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: 203.24  E-value: 2.66e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 296 EQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQT 375
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 376 NILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDI 455
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 16132176 456 MGEIASASDEQSRGIDQVGLAVAEMDRVTQQN 487
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
Tar_Tsr_sensor cd19407
ligand binding sensor domain of Tar- and Tsr-related chemoreceptors; Escherichia coli Tar ...
44-175 3.47e-52

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: 174.05  E-value: 3.47e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  44 QTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGsGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAA 123
Cdd:cd19407   1 QQLRQQQSALNDSWVALLQARNTLNRAAIRYLLDANNGG-GAAVAELLDQAKKSLAQAEKHFAQFKALPKLPGQDEALAA 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16132176 124 EIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQND 175
Cdd:cd19407  80 ELEQSYQAYHDALAELIQFLEAGNIDAFLDQPTQGYQDAFEKAYNAYLAQNN 131
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
44-182 3.76e-48

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: 163.79  E-value: 3.76e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176     44 QTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMmdQNNIGSGSTvaELMESASISLKQAEKNWADYEALPRDPRQSTAAAA 123
Cdd:smart00319   1 ATSSYQQAALSLSRVLLLQARNNLNRAGIRMM--QNNIGSKAK--KLMTAASESLKQAEKNYKSYENMTALPRADRALDA 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16132176    124 EIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAV 182
Cdd:smart00319  77 ELKEKFQQYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQAV 135
TarH pfam02203
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a ...
26-177 8.08e-41

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: 144.75  E-value: 8.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    26 GGLFFNALKNDKENFTVLQTIR-QQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNigsgsTVAELMESASISLKQAEKN 104
Cdd:pfam02203   1 GGLGLSGLSRSNDALREVYTNRlQQQAALADAWLLLLQARLTLNRAGIAALLPDAP-----DAAELLARARESLAQSDAA 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132176   105 WADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYME----QNDRL 177
Cdd:pfam02203  76 WKAYLALPRTPDEEEALAAELKAKYDALQDGLAPLIAALRAGDLDAFFDQPTQKIQPLFEALYNAYLAlrkfQNDAA 152
chemoreceptor_sensor cd00181
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
44-175 7.50e-26

4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others.


Pssm-ID: 438624 [Multi-domain]  Cd Length: 119  Bit Score: 102.21  E-value: 7.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  44 QTIRQQQSTLNGSWVALLQTRNTLNRAGIRYmmdqnnigsgstVAELMESASISLKQAEKNWADYEALPRDPRqstAAAA 123
Cdd:cd00181   1 QEIRQQASAISSLESLVLQARVTLRAEALTG------------VEELGDALIRALKQTAAVLAQFRALTRDPP---EAEA 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16132176 124 EIKRNYDIYHNALAELIQLLGA-GKINEFFDQP-TQGYQDGFEKQYVAYMEQND 175
Cdd:cd00181  66 EILDKVQDYQKALAALIPALLErGAESALFDQSeAQGGLELLLSLLQQLTAAGI 119
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
217-268 1.21e-09

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 54.18  E-value: 1.21e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 16132176    217 SLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVG 268
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
188-263 3.22e-09

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: 59.21  E-value: 3.22e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132176 188 SYSQAMWILVGVMIVVLAVIFAVWFGIKAS--LVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGEL 263
Cdd:COG5000   1 SGLQILFLLLLLLIALLLLLLALWLALLLArrLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQL 78
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
219-263 1.17e-08

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: 50.91  E-value: 1.17e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 16132176 219 VAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGEL 263
Cdd:cd06225   1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP pfam00672
HAMP domain;
217-263 1.74e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 50.70  E-value: 1.74e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 16132176   217 SLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGEL 263
Cdd:pfam00672   5 RILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
186-258 2.51e-07

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 53.54  E-value: 2.51e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132176 186 NASYSQAMWILVGVMIVVLAVIFAV-WFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRH 258
Cdd:COG4192 318 AQLVQQSGILLLAIALLSLLLAVLInYFYVRRRLVKRLNALSDAMAAIAAGDLDVPIPVDGNDEIGRIARLLRV 391
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
40-547 1.55e-06

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 50.88  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  40 FTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQST 119
Cdd:COG2770  58 LLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLA 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 120 AAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGV 199
Cdd:COG2770 138 LALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLL 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 200 MIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYS 279
Cdd:COG2770 218 ALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEA 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 280 GASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQ 359
Cdd:COG2770 298 ELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLL 377
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 360 KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAG 439
Cdd:COG2770 378 ALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGL 457
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 440 ETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQ 519
Cdd:COG2770 458 AELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEE 537
                       490       500
                ....*....|....*....|....*...
gi 16132176 520 QQRETSAVVKTVTPAAPRKMAVADSEEN 547
Cdd:COG2770 538 AALLLAAAAELAALLALLLALAAVEAAA 565
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
4-189 6.09e-06

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: 46.86  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176     4 RIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENftvLQTIRQQQsTLNGSWVALLQTRNTLNRAGIRYMMDQNNigs 83
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGVVGLYSLKQINDN---LDTMYEDR-LLPIKWLGDIRANLLELRANLLELILTTD--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176    84 GSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAaEIKRNYDIYHNALAELIQLLGAGKINE---FFDQPTQGYQ 160
Cdd:pfam12729  74 PAERDELLKDIEELRAEIDKLLEKYEKTILTDEEKKLFA-EFKENLNAYRAVRNKVLELAKAGNKDEayqLYKTEGRPAR 152
                         170       180
                  ....*....|....*....|....*....
gi 16132176   161 DGFEKQYVAYMEQNDRLHDIAVSDNNASY 189
Cdd:pfam12729 153 EAMIEALEELVDYNLKVAKEAYKDNKASY 181
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
195-263 3.97e-05

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 46.38  E-value: 3.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176  195 ILVGVMIVVLAVIFAVWFgIKASLVAPMNRLIDSIRHIAGGDL-VKPIEVDGSNEMGQLAESLRHMQGEL 263
Cdd:PRK10935 154 SLLGLILILTLVFFTVRF-TRRQVVAPLNQLVTASQQIEKGQFdHIPLDTTLPNELGLLAKAFNQMSSEL 222
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
194-519 7.27e-05

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 45.26  E-value: 7.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 194 WILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNG 273
Cdd:COG3850 118 KLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEE 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 274 ANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRD 353
Cdd:COG3850 198 EELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASA 277
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 354 ISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGST 433
Cdd:COG3850 278 LLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAA 357
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132176 434 LVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVA 513
Cdd:COG3850 358 AGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEALA 437

                ....*.
gi 16132176 514 VFRIQQ 519
Cdd:COG3850 438 ARGLAA 443
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
200-254 1.13e-03

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 41.54  E-value: 1.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16132176  200 MIVVLAVIFA--VWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAE 254
Cdd:PRK10549 168 LIVALSTLLAalATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQ 224
 
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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