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Conserved domains on  [gi|501231529|ref|WP_012274547|]
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MULTISPECIES: chemotaxis protein CheW [Pseudomonas]

Protein Classification

chemotaxis protein CheW( domain architecture ID 10481941)

CheW couples methyl-accepting chemoreceptors and histidine kinase CheA and is essential for chemotaxis

Gene Ontology:  GO:0007165|GO:0006935
PubMed:  10049806|12011495

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 14-143 1.34e-10

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


:

Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 55.67  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231529   14 GLLLPLGDRTLVLPNVAVAELSGQRNLVCQHGDPAWHLGWIDWRQQRLPLIGFEAACGGETPC-GERARVVVLNalgdTG 92
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEpRERTRVVVVE----VG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 501231529   93 LRYLALLLQDIPRSCKLDS---QLNYVDVALGRLELAAVQVG-EQVARVPDLVAL 143
Cdd:pfam01584  77 GQVVGLLVDEVIGVLEIVIkqiEPPLGLGRVAGYISGATILGdGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 14-143 1.34e-10

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 55.67  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231529   14 GLLLPLGDRTLVLPNVAVAELSGQRNLVCQHGDPAWHLGWIDWRQQRLPLIGFEAACGGETPC-GERARVVVLNalgdTG 92
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEpRERTRVVVVE----VG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 501231529   93 LRYLALLLQDIPRSCKLDS---QLNYVDVALGRLELAAVQVG-EQVARVPDLVAL 143
Cdd:pfam01584  77 GQVVGLLVDEVIGVLEIVIkqiEPPLGLGRVAGYISGATILGdGRVVLILDVEAL 131
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 11-89 2.51e-04

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 238331  Cd Length: 136  Bit Score: 38.79  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231529  11 SLTGLLLPLGDRTLVLPNVAVAELSGQRNLVCQHGDPAWHLGWIDWRQQRLPLIGFEAACG--GETPCGERARVVVLNAL 88
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGleAAEPDTDETRIVVVEVG 80


                 .
gi 501231529  89 G 89
Cdd:cd00588   81 D 81
 
Name Accession Description Interval E-value
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 14-143 1.34e-10

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 55.67  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231529   14 GLLLPLGDRTLVLPNVAVAELSGQRNLVCQHGDPAWHLGWIDWRQQRLPLIGFEAACGGETPC-GERARVVVLNalgdTG 92
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEpRERTRVVVVE----VG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 501231529   93 LRYLALLLQDIPRSCKLDS---QLNYVDVALGRLELAAVQVG-EQVARVPDLVAL 143
Cdd:pfam01584  77 GQVVGLLVDEVIGVLEIVIkqiEPPLGLGRVAGYISGATILGdGRVVLILDVEAL 131
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 11-89 2.51e-04

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 238331  Cd Length: 136  Bit Score: 38.79  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231529  11 SLTGLLLPLGDRTLVLPNVAVAELSGQRNLVCQHGDPAWHLGWIDWRQQRLPLIGFEAACG--GETPCGERARVVVLNAL 88
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGleAAEPDTDETRIVVVEVG 80


                 .
gi 501231529  89 G 89
Cdd:cd00588   81 D 81
 
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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