The domain within your query sequence starts at position 408 and ends at position 508; the E-value for the Evr1_Alr domain shown below is 1.2e-28.



PFAM accession number:PF04777
Interpro abstract (IPR017905):

The ~100-residue ERV/ALR sulphydryl oxidase domain is a versatile module adapted for catalysis of disulphide bond formation in various organelles and biological settings. The ERV/ALR sulphydryl oxidase domain has a Cys-X-X-Cys dithiol/disulphide motif adjacent to a bound FAD cofactor, enabling transfer of electrons from thiol substrates to non-thiol electron acceptors. ERV/ALR family members differ in their N- or C-terminal extensions, which typically contain at least one additional disulphide bond, the hypothesised 'shuttle' disulphide. In yeast ERV1, a mitochondrial enzyme, the shuttle disulphide is N-terminal to the catalytic core; in yeast ERV2, present in the endoplasmic reticulum, it is C-terminal. The N- and C-terminal extensions can be entire domains, such as the thioredoxin-like domains or short segments that do not seem to be distinct domains. Proteins of the ERV/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses (poxviruses, African swine fever virus, iridoviruses, and Paramecium bursaria Chlorella virus 1) [ (PUBMED:10542195) (PUBMED:11035794) (PUBMED:11740506) (PUBMED:16893552) (PUBMED:17298084) ].

The ERV/ALR sulphydryl oxidase domain contains a four-helix bundle (helices alpha1-alpha4) and an additional single turn of helix (alpha5) packed perpendicular to the bundle [ (PUBMED:1174050) (PUBMED:16893552) ]. The FAD prosthetic group is housed at the mouth of the 4-helix bundle and communicates with the pair of juxtaposed cysteine residues that form the proximal redox active site [ (PUBMED:17298084) ].

GO process:oxidation-reduction process (GO:0055114)
GO function:thiol oxidase activity (GO:0016972)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Evr1_Alr