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Conserved domains on  [gi|53723482|ref|YP_102936.1|]
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methyl-accepting chemotaxis domain-containing protein [Burkholderia mallei ATCC 23344]

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List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
497-688 5.43e-55

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


:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 187.83  E-value: 5.43e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 497 EQQAASLQETAASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQT 576
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 577 NILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIETSIDTVRDGVSKADEVGQHIVEVKQAIRRVADL 656
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 53723482 657 VGEITAASEEQTRGIEQVDAAVSQMDRVTQQN 688
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
414-460 7.68e-03

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 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: 100122  Cd Length: 48  Bit Score: 35.30  E-value: 7.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 53723482 414 VLAGLEAAASTASRVAAGDLTshfdaHRVDPQAKDEISRVMRALQTM 460
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLD-----VRLPVTGRDEIGELARAFNQM 42
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
363-718 2.78e-72

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 242.59  E-value: 2.78e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 363 IDDFLKLLDARTEGAIARAQASAQTWKIISAAVAIGILAFFALMLHMMFKRVLAGLEAAASTASRVAAGDLTshfdaHRV 442
Cdd:COG0840  33 LGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLT-----KRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 443 DPQAKDEISRVMRALQTMNDGLVRIVTDVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLE 522
Cdd:COG0840 108 DESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAF 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 523 NARQANMIGSNAVSTVEKGSVSVEQLVTTVNAI-----------STNSGKIADIISLIEGIAFQTNILALNAAVEAARAG 591
Cdd:COG0840 188 NAKEAAALASEASQVAEEGGEEVRQAVEQMQEIaeelaevvkklSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAG 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 592 EQGRGFAVVASEVRSLAQRSSSAAKEIKDLIET--------------SIDTVRDGVSKADEVGQHIVEVKQAIRRVADLV 657
Cdd:COG0840 268 EAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIEEVSQLI 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53723482 658 GEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:COG0840 348 SEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
497-688 5.43e-55

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


Pssm-ID: 206779  Cd Length: 200  Bit Score: 187.83  E-value: 5.43e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 497 EQQAASLQETAASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQT 576
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 577 NILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIETSIDTVRDGVSKADEVGQHIVEVKQAIRRVADL 656
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 53723482 657 VGEITAASEEQTRGIEQVDAAVSQMDRVTQQN 688
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
414-460 7.68e-03

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 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: 100122  Cd Length: 48  Bit Score: 35.30  E-value: 7.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 53723482 414 VLAGLEAAASTASRVAAGDLTshfdaHRVDPQAKDEISRVMRALQTM 460
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLD-----VRLPVTGRDEIGELARAFNQM 42
HAMP pfam00672
HAMP domain;
392-464 1.78e-04

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 40.29  E-value: 1.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53723482   392 SAAVAIGILAFFALMLHMMFKRVLAGLEAAASTASRVAAGDLTShfdahRVDPQAKDEISRVMRALQTMNDGL 464
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDD-----RVPVSGPDEIGELARAFNQMADRL 68
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
412-469 3.72e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 36.07  E-value: 3.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 53723482    412 KRVLAGLEAAASTASRVAAGDLTshfdaHRVDPQAKDEISRVMRALQTMNDGLVRIVT 469
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLT-----VRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
363-718 2.78e-72

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 242.59  E-value: 2.78e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 363 IDDFLKLLDARTEGAIARAQASAQTWKIISAAVAIGILAFFALMLHMMFKRVLAGLEAAASTASRVAAGDLTshfdaHRV 442
Cdd:COG0840  33 LGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLT-----KRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 443 DPQAKDEISRVMRALQTMNDGLVRIVTDVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLE 522
Cdd:COG0840 108 DESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAF 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 523 NARQANMIGSNAVSTVEKGSVSVEQLVTTVNAI-----------STNSGKIADIISLIEGIAFQTNILALNAAVEAARAG 591
Cdd:COG0840 188 NAKEAAALASEASQVAEEGGEEVRQAVEQMQEIaeelaevvkklSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAG 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 592 EQGRGFAVVASEVRSLAQRSSSAAKEIKDLIET--------------SIDTVRDGVSKADEVGQHIVEVKQAIRRVADLV 657
Cdd:COG0840 268 EAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIEEVSQLI 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53723482 658 GEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:COG0840 348 SEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
428-718 2.10e-94

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 306.11  E-value: 2.10e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  428 VAAGDLtshfdAHRVDPQAKDEISRVMRALQTMNDGLVRIVTDVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETA 507
Cdd:PRK15041 232 IAGGDL-----VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETA 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  508 ASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEA 587
Cdd:PRK15041 307 ASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEA 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  588 ARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIETSIDTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQ 667
Cdd:PRK15041 387 ARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQ 466
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 53723482  668 TRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:PRK15041 467 SRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
470-717 6.40e-63

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 212.15  E-value: 6.40e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482    470 DVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLV 549
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482    550 TTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIET----- 624
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482    625 ---------SIDTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVEQA 695
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 53723482    696 AAASKAMDDQAGNLRAAASIFK 717
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
522-718 3.31e-50

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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 174.94  E-value: 3.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482   522 ENARQANmigSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEAARAGEQGRGFAVVA 601
Cdd:pfam00015   5 DLAQLAS---EEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482   602 SEVRSLAQRSSSAAKEIKDLIETSI--------------DTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQ 667
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 53723482   668 TRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
497-688 5.43e-55

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


Pssm-ID: 206779  Cd Length: 200  Bit Score: 187.83  E-value: 5.43e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 497 EQQAASLQETAASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQT 576
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 577 NILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIETSIDTVRDGVSKADEVGQHIVEVKQAIRRVADL 656
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 53723482 657 VGEITAASEEQTRGIEQVDAAVSQMDRVTQQN 688
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
414-460 7.68e-03

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 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: 100122  Cd Length: 48  Bit Score: 35.30  E-value: 7.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 53723482 414 VLAGLEAAASTASRVAAGDLTshfdaHRVDPQAKDEISRVMRALQTM 460
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLD-----VRLPVTGRDEIGELARAFNQM 42
HAMP pfam00672
HAMP domain;
392-464 1.78e-04

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 40.29  E-value: 1.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53723482   392 SAAVAIGILAFFALMLHMMFKRVLAGLEAAASTASRVAAGDLTShfdahRVDPQAKDEISRVMRALQTMNDGL 464
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDD-----RVPVSGPDEIGELARAFNQMADRL 68
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
412-469 3.72e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 36.07  E-value: 3.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 53723482    412 KRVLAGLEAAASTASRVAAGDLTshfdaHRVDPQAKDEISRVMRALQTMNDGLVRIVT 469
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLT-----VRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
363-718 2.78e-72

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 242.59  E-value: 2.78e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 363 IDDFLKLLDARTEGAIARAQASAQTWKIISAAVAIGILAFFALMLHMMFKRVLAGLEAAASTASRVAAGDLTshfdaHRV 442
Cdd:COG0840  33 LGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLT-----KRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 443 DPQAKDEISRVMRALQTMNDGLVRIVTDVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLE 522
Cdd:COG0840 108 DESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAF 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 523 NARQANMIGSNAVSTVEKGSVSVEQLVTTVNAI-----------STNSGKIADIISLIEGIAFQTNILALNAAVEAARAG 591
Cdd:COG0840 188 NAKEAAALASEASQVAEEGGEEVRQAVEQMQEIaeelaevvkklSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAG 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482 592 EQGRGFAVVASEVRSLAQRSSSAAKEIKDLIET--------------SIDTVRDGVSKADEVGQHIVEVKQAIRRVADLV 657
Cdd:COG0840 268 EAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIEEVSQLI 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53723482 658 GEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:COG0840 348 SEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
428-718 2.10e-94

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 306.11  E-value: 2.10e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  428 VAAGDLtshfdAHRVDPQAKDEISRVMRALQTMNDGLVRIVTDVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETA 507
Cdd:PRK15041 232 IAGGDL-----VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETA 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  508 ASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEA 587
Cdd:PRK15041 307 ASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEA 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  588 ARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIETSIDTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQ 667
Cdd:PRK15041 387 ARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQ 466
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 53723482  668 TRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:PRK15041 467 SRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
390-722 6.87e-92

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 299.61  E-value: 6.87e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  390 IISAAVAIGILAFFALMLHMMfkrvLAGLEAAASTASRVAAGDLTSHFDAhrvdpQAKDEISRVMRALQTMNDGLVRIVT 469
Cdd:PRK15048 196 VIALVVVLILLVAWYGIRRML----LTPLAKIIAHIREIAGGNLANTLTI-----DGRSEMGDLAQSVSHMQRSLTDTVT 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  470 DVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLV 549
Cdd:PRK15048 267 HVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVV 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  550 TTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIETSIDTV 629
Cdd:PRK15048 347 KTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRV 426
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  630 RDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNL 709
Cdd:PRK15048 427 DTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRL 506
                        330
                 ....*....|...
gi 53723482  710 RAAASIFKLPGRA 722
Cdd:PRK15048 507 TQAVSAFRLAASP 519
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
378-718 7.00e-91

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 296.21  E-value: 7.00e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  378 IARAQASAQTWKIISAAVAIGILAFFALM----LHMMFKRVLAGLEAAASTASRVAAGDLtshfdAHRVDPQAKDEISRV 453
Cdd:PRK09793 174 LEAASAQSQRNYQISALVFISMIIVAAIYissaLWWTRKMIVQPLAIIGSHFDSIAAGNL-----ARPIAVYGRNEITAI 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  454 MRALQTMNDGLVRIVTDVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLENARQANMIGSN 533
Cdd:PRK09793 249 FASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKN 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  534 AVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSS 613
Cdd:PRK09793 329 AATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQ 408
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482  614 AAKEIKDLIETSIDTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVE 693
Cdd:PRK09793 409 AAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVE 488
                        330       340
                 ....*....|....*....|....*
gi 53723482  694 QAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:PRK09793 489 EAAVATEQLANQADHLSSRVAVFTL 513
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
470-717 6.40e-63

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 212.15  E-value: 6.40e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482    470 DVRSGTDTIATASHEIMAGNNDLSARTEQQAASLQETAASMSELTATVKLNLENARQANMIGSNAVSTVEKGSVSVEQLV 549
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482    550 TTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRSLAQRSSSAAKEIKDLIET----- 624
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482    625 ---------SIDTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQTRGIEQVDAAVSQMDRVTQQNAALVEQA 695
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 53723482    696 AAASKAMDDQAGNLRAAASIFK 717
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
522-718 3.31e-50

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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 174.94  E-value: 3.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482   522 ENARQANmigSNAVSTVEKGSVSVEQLVTTVNAISTNSGKIADIISLIEGIAFQTNILALNAAVEAARAGEQGRGFAVVA 601
Cdd:pfam00015   5 DLAQLAS---EEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53723482   602 SEVRSLAQRSSSAAKEIKDLIETSI--------------DTVRDGVSKADEVGQHIVEVKQAIRRVADLVGEITAASEEQ 667
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 53723482   668 TRGIEQVDAAVSQMDRVTQQNAALVEQAAAASKAMDDQAGNLRAAASIFKL 718
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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