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Conserved domains on  [gi|1081172886|gb|OFT19037|]
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hypothetical protein HMPREF3068_02360 [Lactobacillus sp. HMSC17G08]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MCP_signal super family cl46910
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 6-62 2.46e-03

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


The actual alignment was detected with superfamily member PRK15048:

Pssm-ID: 481250 [Multi-domain]  Cd Length: 553  Bit Score: 35.37  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1081172886   6 EEIIASMEQLSVTLSHNHPNSETARYVAKSLKELKNSHGTAFTGALQSFFNSAPSVK 62
Cdd:PRK15048  301 EETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSK 357
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 6-62 2.46e-03

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 35.37  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1081172886   6 EEIIASMEQLSVTLSHNHPNSETARYVAKSLKELKNSHGTAFTGALQSFFNSAPSVK 62
Cdd:PRK15048  301 EETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSK 357
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 6-62 2.46e-03

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 35.37  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1081172886   6 EEIIASMEQLSVTLSHNHPNSETARYVAKSLKELKNSHGTAFTGALQSFFNSAPSVK 62
Cdd:PRK15048  301 EETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSK 357
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
6-68 3.45e-03

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 34.93  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081172886   6 EEIIASMEQLSVTLSHNHPNSETARYVAKSLKELKNSHGTAFTGALQSFFN-SAPSVKLSDRFS 68
Cdd:PRK15041  303 EETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDiSTSSQKIADIIS 366
 
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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