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Conserved domains on  [gi|612647215|gb|EZS63688|]
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hypothetical protein W523_00390 [Staphylococcus aureus VET0235R]

Protein Classification

excalibur calcium-binding domain-containing protein( domain architecture ID 10658109)

excalibur calcium-binding domain-containing protein contains a conserved DxDxDGxxCE motif, similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Excalibur smart00894
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ...
 168-204 1.68e-12

Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated.


:

Pssm-ID: 214891 [Multi-domain]  Cd Length: 37  Bit Score: 59.21  E-value: 1.68e-12
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 612647215   168 SFANCKQLRQVYPNGVTADHPAYRPHLDRDKDKRACE 204
Cdd:smart00894   1 YYKNCKEARAAGAAPIYQGDPGYGPHLDRDGDGVACE 37
 
Name Accession Description Interval E-value
Excalibur smart00894
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ...
 168-204 1.68e-12

Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated.


Pssm-ID: 214891 [Multi-domain]  Cd Length: 37  Bit Score: 59.21  E-value: 1.68e-12
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 612647215   168 SFANCKQLRQVYPNGVTADHPAYRPHLDRDKDKRACE 204
Cdd:smart00894   1 YYKNCKEARAAGAAPIYQGDPGYGPHLDRDGDGVACE 37
Excalibur pfam05901
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ...
 169-204 9.28e-12

Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognized and the evolution of EF-hand-like domains is probably more complex than previously appreciated.


Pssm-ID: 428664  Cd Length: 36  Bit Score: 57.47  E-value: 9.28e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 612647215  169 FANCKQLRQVYPNGVTADHPAYRPHLDRDKDKRACE 204
Cdd:pfam05901   1 YKNCTEARSAGEAPIYRGAPGYRSKLDRDGDGIACE 36
 
Name Accession Description Interval E-value
Excalibur smart00894
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ...
 168-204 1.68e-12

Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated.


Pssm-ID: 214891 [Multi-domain]  Cd Length: 37  Bit Score: 59.21  E-value: 1.68e-12
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 612647215   168 SFANCKQLRQVYPNGVTADHPAYRPHLDRDKDKRACE 204
Cdd:smart00894   1 YYKNCKEARAAGAAPIYQGDPGYGPHLDRDGDGVACE 37
Excalibur pfam05901
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ...
 169-204 9.28e-12

Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognized and the evolution of EF-hand-like domains is probably more complex than previously appreciated.


Pssm-ID: 428664  Cd Length: 36  Bit Score: 57.47  E-value: 9.28e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 612647215  169 FANCKQLRQVYPNGVTADHPAYRPHLDRDKDKRACE 204
Cdd:pfam05901   1 YKNCTEARSAGEAPIYRGAPGYRSKLDRDGDGIACE 36
 
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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