The domain within your query sequence starts at position 65 and ends at position 219; the E-value for the PMSR domain shown below is 2.4e-68.



PFAM accession number:PF01625
Interpro abstract (IPR002569):

Peptide methionine sulphoxide reductase (Msr) reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide, Met(O), to methionine [(PUBMED:10841552)]. It is present in most living organisms, and the cognate structural gene belongs to the so-called minimum gene set [(PUBMED:8994848), (PUBMED:8816789)].

The domains MsrA and MsrB reduce different epimeric forms of methionine sulphoxide. This group represent MsrA, the crystal structure of which has been determined in a number of organisms. In Mycobacterium tuberculosis, the MsrA structure has been determined to 1.5 Angstrom resolution [(PUBMED:12837786)]. In contrast to the three catalytic cysteine residues found in previously characterised MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The overall structure shows no resemblance to the structures of MsrB (IPR002579) from other organisms; though the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate.

In a number of pathogenic bacteria including Neisseria gonorrhoeae, the MsrA and MsrB domains are fused; the MsrA being N-terminal to MsrB. This arrangement is reversed in Treponema pallidum. In N. gonorrhoeae and Neisseria meningitidis a thioredoxin domain is fused to the N terminus. This may function to reduce the active sites of the downstream MsrA and MsrB domains.

GO process:oxidation-reduction process (GO:0055114)
GO function:peptide-methionine (S)-S-oxide reductase activity (GO:0008113)

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