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Conserved domains on  [gi|446712338|ref|WP_000789682|]
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MULTISPECIES: methyl-accepting chemotaxis citrate transducer [Salmonella]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 1003728)

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

 Zoom to residue level

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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 ...
 1-547 0e+00

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


The actual alignment was detected with superfamily member PRK15041:

Pssm-ID: 481250 [Multi-domain]  Cd Length: 554  Bit Score: 543.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   1 MKNIKVITGVIATLGIFSALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDP 80
Cdd:PRK15041   2 LKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  81 ASLDAMNTLLTNAGASLNEAEKHFNNYvnsEAIAgKDPALDAQAEASFKQMYDV----LQQSIHYLKADNYAAYGNLDAQ 156
Cdd:PRK15041  82 GSGSTVAELMQSASISLKQAEKNWADY---EALP-RDPRQSTAAAAEIKRNYDIyhnaLAELIQLLGAGKINEFFDQPTQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 157 KAQDDMEQVYDQWLSQNAQLIKLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDL 236
Cdd:PRK15041 158 GYQDGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 237 THEIEAEGRSEMGQLAAGLKTMQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVR 316
Cdd:PRK15041 238 VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVK 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 317 QNTDNARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFA 396
Cdd:PRK15041 318 QNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 397 VVAGEVRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAV 476
Cdd:PRK15041 398 VVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAV 477

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446712338 477 SEMDSVTQQNASLVEESAAAAAALEDQANELRQAVAAFRIQKQPRREASPTPLSKGLTPQPAAEQA------NWESF 547
Cdd:PRK15041 478 AEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPATPRKMAvadsgeNWETF 554
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
1-547 0e+00

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 543.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   1 MKNIKVITGVIATLGIFSALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDP 80
Cdd:PRK15041   2 LKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  81 ASLDAMNTLLTNAGASLNEAEKHFNNYvnsEAIAgKDPALDAQAEASFKQMYDV----LQQSIHYLKADNYAAYGNLDAQ 156
Cdd:PRK15041  82 GSGSTVAELMQSASISLKQAEKNWADY---EALP-RDPRQSTAAAAEIKRNYDIyhnaLAELIQLLGAGKINEFFDQPTQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 157 KAQDDMEQVYDQWLSQNAQLIKLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDL 236
Cdd:PRK15041 158 GYQDGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 237 THEIEAEGRSEMGQLAAGLKTMQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVR 316
Cdd:PRK15041 238 VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVK 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 317 QNTDNARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFA 396
Cdd:PRK15041 318 QNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 397 VVAGEVRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAV 476
Cdd:PRK15041 398 VVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAV 477

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446712338 477 SEMDSVTQQNASLVEESAAAAAALEDQANELRQAVAAFRIQKQPRREASPTPLSKGLTPQPAAEQA------NWESF 547
Cdd:PRK15041 478 AEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPATPRKMAvadsgeNWETF 554
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
18-516 2.20e-97

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 305.79  E-value: 2.20e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  18 SALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDPASLDAMNTLLTNAGASL 97
Cdd:COG0840    7 LLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  98 NEAEKHFNNYVNSEAIAGKDPALDAQAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDMEQVYDQWLSQNAQLI 177
Cdd:COG0840   87 ALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 178 KLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKT 257
Cdd:COG0840  167 LEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNR 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 258 MQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETAR 337
Cdd:COG0840  247 MIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAE 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 338 KGGRVVDNVVS--------------TMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 403
Cdd:COG0840  327 EGGEVVEEAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVR 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 404 TLASRSAQAAKEIKVLIENSVSR--------------IDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGI 469
Cdd:COG0840  407 KLAERSAEATKEIEELIEEIQSEteeaveameegseeVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGT 486

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 446712338 470 EQVAQAVSEMDSVTQQNASLVEESAAAAAALEDQANELRQAVAAFRI 516
Cdd:COG0840  487 EEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 268-515 2.00e-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: 224.09  E-value: 2.00e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   268 AVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGGRVVDNVV 347
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   348 STMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIEN----- 422
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   423 ---------SVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEES 493
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 446712338   494 AAAAAALEDQANELRQAVAAFR 515
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 326-483 1.04e-63

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 205.74  E-value: 1.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  326 TGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTL 405
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  406 ASRSAQAAKEIKVLI--------------ENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQ 471
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 446712338  472 VAQAVSEMDSVT 483
Cdd:pfam00015 161 VNQAVARMDQVT 172
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 295-493 3.76e-61

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 200.16  E-value: 3.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 295 EQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQT 374
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 375 NILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDI 454
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446712338 455 MGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEES 493
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-510 5.83e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   272 NADSIYTGAGEiSAGSSDLSSRTE-----QQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGgrvvdnV 346
Cdd:TIGR02168  656 RPGGVITGGSA-KTNSSILERRREieeleEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ------I 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   347 VSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIENSVS- 425
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEl 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   426 -------RIDTGSTQVR------EAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEE 492
Cdd:TIGR02168  809 raeltllNEEAANLRERleslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888

                          250
                   ....*....|....*...
gi 446712338   493 SAAAAAALEDQANELRQA 510
Cdd:TIGR02168  889 LALLRSELEELSEELREL 906
 
Name Accession Description Interval E-value
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
1-547 0e+00

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 543.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   1 MKNIKVITGVIATLGIFSALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDP 80
Cdd:PRK15041   2 LKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  81 ASLDAMNTLLTNAGASLNEAEKHFNNYvnsEAIAgKDPALDAQAEASFKQMYDV----LQQSIHYLKADNYAAYGNLDAQ 156
Cdd:PRK15041  82 GSGSTVAELMQSASISLKQAEKNWADY---EALP-RDPRQSTAAAAEIKRNYDIyhnaLAELIQLLGAGKINEFFDQPTQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 157 KAQDDMEQVYDQWLSQNAQLIKLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDL 236
Cdd:PRK15041 158 GYQDGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 237 THEIEAEGRSEMGQLAAGLKTMQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVR 316
Cdd:PRK15041 238 VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVK 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 317 QNTDNARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFA 396
Cdd:PRK15041 318 QNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 397 VVAGEVRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAV 476
Cdd:PRK15041 398 VVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAV 477

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446712338 477 SEMDSVTQQNASLVEESAAAAAALEDQANELRQAVAAFRIQKQPRREASPTPLSKGLTPQPAAEQA------NWESF 547
Cdd:PRK15041 478 AEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPATPRKMAvadsgeNWETF 554
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 4-547 0e+00

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 533.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   4 IKVITGVIATLGIFSALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDPASl 83
Cdd:PRK15048   5 IRVVTLLVMVLGVFALLQLISGSLFFSSLHHSQKSFVVSNQLREQQGELTSTWDLMLQTRINLSRSAVRMMMDSSNQQS- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  84 DAMNTLLTNAGASLNEAEKHFNNYVNSEAIAGKDPAlDAQAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDME 163
Cdd:PRK15048  84 NAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVAT-SRNIDEKYKNYYTALTELIDYLDYGNTGAYFAQPTQGMQNAMG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 164 QVYDQWLSQNAQLIKLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDLTHEIEAE 243
Cdd:PRK15048 163 EAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTID 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 244 GRSEMGQLAAGLKTMQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDNAR 323
Cdd:PRK15048 243 GRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNAR 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 324 QATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 403
Cdd:PRK15048 323 QASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 404 TLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVT 483
Cdd:PRK15048 403 NLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVT 482

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446712338 484 QQNASLVEESAAAAAALEDQANELRQAVAAFRIQKQPR-----REASPTPLSKGLTPQPAA--EQANWESF 547
Cdd:PRK15048 483 QQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLtnkpqTPSRPASEQPPAQPRLRIaeQDPNWETF 553
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
84-519 2.15e-134

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 400.99  E-value: 2.15e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  84 DAMNTLLTNAGASLNEAEKHFNNYVNSEAIAGKDPALDAQAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDME 163
Cdd:PRK09793  81 DDIKTLMTTARASLTQSTTLFKSFMAMTAGNEHVRALQKETEKSFARWHNDLEHQATWLESNQLSDFLTAPVQGSQNAFD 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 164 QVYDQWLSQNAQLIKLASDQNQSSF--TQMQWTLGIILLIVLIVLAFIWLglQRVLLRPLQRIMAHIQTIADGDLTHEIE 241
Cdd:PRK09793 161 VNFEAWQLEINHVLEAASAQSQRNYqiSALVFISMIIVAAIYISSALWWT--RKMIVQPLAIIGSHFDSIAAGNLARPIA 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 242 AEGRSEMGQLAAGLKTMQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDN 321
Cdd:PRK09793 239 VYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADN 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 322 ARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGE 401
Cdd:PRK09793 319 ARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGE 398

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 402 VRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDS 481
Cdd:PRK09793 399 VRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQ 478

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 446712338 482 VTQQNASLVEESAAAAAALEDQANELRQAVAAFRIQKQ 519
Cdd:PRK09793 479 VTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEH 516
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
18-516 2.20e-97

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 305.79  E-value: 2.20e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  18 SALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDPASLDAMNTLLTNAGASL 97
Cdd:COG0840    7 LLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  98 NEAEKHFNNYVNSEAIAGKDPALDAQAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDMEQVYDQWLSQNAQLI 177
Cdd:COG0840   87 ALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 178 KLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKT 257
Cdd:COG0840  167 LEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNR 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 258 MQQSLIRTVSAVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETAR 337
Cdd:COG0840  247 MIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAE 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 338 KGGRVVDNVVS--------------TMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 403
Cdd:COG0840  327 EGGEVVEEAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVR 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 404 TLASRSAQAAKEIKVLIENSVSR--------------IDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGI 469
Cdd:COG0840  407 KLAERSAEATKEIEELIEEIQSEteeaveameegseeVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGT 486

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 446712338 470 EQVAQAVSEMDSVTQQNASLVEESAAAAAALEDQANELRQAVAAFRI 516
Cdd:COG0840  487 EEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 268-515 2.00e-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: 224.09  E-value: 2.00e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   268 AVRDNADSIYTGAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGGRVVDNVV 347
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   348 STMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIEN----- 422
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   423 ---------SVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEES 493
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 446712338   494 AAAAAALEDQANELRQAVAAFR 515
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 326-483 1.04e-63

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 205.74  E-value: 1.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  326 TGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTL 405
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  406 ASRSAQAAKEIKVLI--------------ENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQ 471
Cdd:pfam00015  81 AERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 446712338  472 VAQAVSEMDSVT 483
Cdd:pfam00015 161 VNQAVARMDQVT 172
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 295-493 3.76e-61

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 200.16  E-value: 3.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 295 EQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQT 374
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 375 NILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDI 454
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446712338 455 MGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEES 493
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
 43-181 6.03e-38

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: 136.06  E-value: 6.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338    43 SALSYQQQELGGSFQTLIETRVTINRVAIRMlkNQRDPASLdaMNTLLTNAGASLNEAEKHFNNYVNSEAIAGKDPALDA 122
Cdd:smart00319   1 ATSSYQQAALSLSRVLLLQARNNLNRAGIRM--MQNNIGSK--AKKLMTAASESLKQAEKNYKSYENMTALPRADRALDA 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 446712338   123 QAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDMEQVYDQWLSQNAQLIKLAS 181
Cdd:smart00319  77 ELKEKFQQYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQAV 135
Tar_Tsr_sensor cd19407
ligand binding sensor domain of Tar- and Tsr-related chemoreceptors; Escherichia coli Tar ...
 44-173 4.46e-30

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: 114.34  E-value: 4.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  44 ALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDPASlDAMNTLLTNAGASLNEAEKHFNNYVNSEAIAGKDPALDAQ 123
Cdd:cd19407    2 QLRQQQSALNDSWVALLQARNTLNRAAIRYLLDANNGGG-AAVAELLDQAKKSLAQAEKHFAQFKALPKLPGQDEALAAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446712338 124 AEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDMEQVYDQWLSQN 173
Cdd:cd19407   81 LEQSYQAYHDALAELIQFLEAGNIDAFLDQPTQGYQDAFEKAYNAYLAQN 130
TarH pfam02203
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a ...
 25-183 2.99e-26

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: 104.31  E-value: 2.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   25 GILFYSAVSSDRLNFQNASALSYQQQ-ELGGSFQTLIETRVTINRVAIRMLKNQRDPasldaMNTLLTNAGASLNEAEKH 103
Cdd:pfam02203   1 GGLGLSGLSRSNDALREVYTNRLQQQaALADAWLLLLQARLTLNRAGIAALLPDAPD-----AAELLARARESLAQSDAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  104 FNNYVNSEAIAGKDPALDAQAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDMEQVYDQWLsqnaQLIKLASDQ 183
Cdd:pfam02203  76 WKAYLALPRTPDEEEALAAELKAKYDALQDGLAPLIAALRAGDLDAFFDQPTQKIQPLFEALYNAYL----ALRKFQNDA 151
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
215-267 1.85e-10

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 56.49  E-value: 1.85e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 446712338   215 RVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKTMQQSLIRTVS 267
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP pfam00672
HAMP domain;
215-262 5.40e-10

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 54.94  E-value: 5.40e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446712338  215 RVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKTMQQSL 262
Cdd:pfam00672   4 RRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 218-262 5.20e-09

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: 52.06  E-value: 5.20e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446712338 218 LRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKTMQQSL 262
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
10-524 3.37e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 46.64  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  10 VIATLGIFSALLLVTGILFYSAVSSDRLNFQNASALSYQQQELGGSFQTLIETRVTINRVAIRMLKNQRDPASLDAMNTL 89
Cdd:COG2770   29 ALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338  90 LTNAGASLNEAEKHFNNYVNSEAIAGKDPALDAQAEASFKQMYDVLQQSIHYLKADNYAAYGNLDAQKAQDDMEQVYDQW 169
Cdd:COG2770  109 LLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 170 LSQNAQLIKLASDQNQSSFTQMQWTLGIILLIVLIVLAFIWLGLQRVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMG 249
Cdd:COG2770  189 ALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIG 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 250 QLAAGLKTMQQSLIRTVSAVRDNADSiytgAGEISAGSSDLSSRTEQQASALEETAASMEQLTATVRQNTDNARQATGLA 329
Cdd:COG2770  269 ELARAFNRMADSLRESIEEAEEEEEL----AEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLL 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 330 KTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLASRS 409
Cdd:COG2770  345 LLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLAL 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 410 AQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASL 489
Cdd:COG2770  425 AAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEE 504

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 446712338 490 VEESAAAAAALEDQANELRQAVAAFRIQKQPRREA 524
Cdd:COG2770  505 LAEELLLLEGLLLLLLLEAEALEVAEELLELEEAA 539
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 209-262 6.84e-05

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: 45.34  E-value: 6.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446712338 209 IWLGLQ--RVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKTMQQSL 262
Cdd:COG5000   23 LWLALLlaRRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQL 78
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 207-517 5.03e-04

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 42.56  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 207 AFIWLGLQRVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKTMQQSLIRTVSAVRDNADSIYTGAGEISAG 286
Cdd:COG3850  132 LLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLD 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 287 SSDLSSRTEQQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGGRVVDNVVSTMNDIAESSEKIVDITSV 366
Cdd:COG3850  212 ELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLE 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338 367 IDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIENSVSRIDTGSTQVREAGETMKEIVN 446
Cdd:COG3850  292 LVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGL 371

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446712338 447 AVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEESAAAAAALEDQANELRQAVAAFRIQ 517
Cdd:COG3850  372 ARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEALAARGLA 442
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
208-262 5.52e-03

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


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 39.65  E-value: 5.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446712338 208 FIWLglQRVLLRPLQRIMAHIQTIADGDLTHEIEAEGRSEMGQLAAGLKTMQQSL 262
Cdd:PRK10600 142 IIWL--RRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAEL 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-510 5.83e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   272 NADSIYTGAGEiSAGSSDLSSRTE-----QQASALEETAASMEQLTATVRQNTDNARQATGLAKTASETARKGgrvvdnV 346
Cdd:TIGR02168  656 RPGGVITGGSA-KTNSSILERRREieeleEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ------I 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   347 VSTMNDIAESSEKIVDITSVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLASRSAQAAKEIKVLIENSVS- 425
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEl 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446712338   426 -------RIDTGSTQVR------EAGETMKEIVNAVTRVTDIMGEIASASDEQSKGIEQVAQAVSEMDSVTQQNASLVEE 492
Cdd:TIGR02168  809 raeltllNEEAANLRERleslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888

                          250
                   ....*....|....*...
gi 446712338   493 SAAAAAALEDQANELRQA 510
Cdd:TIGR02168  889 LALLRSELEELSEELREL 906
 
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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