ID   MSRA_FRAAN              Reviewed;         191 AA.
AC   P54152; Q9FF06;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Peptide methionine sulfoxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Fruit-ripening protein E4;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
DE   AltName: Full=Protein-methionine-S-oxide reductase;
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Receptacle;
RA   Pedraza-Lopez A., Cardenas-Torres J., Rodriguez-Franco A.;
RT   "A specific late-ripening induced cDNA from strawberry receptacles that
RT   showed extense homology with the fruit-specific gene E4 isolated from
RT   tomato fruits.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11;
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; Z69596; CAA93442.2; -; mRNA.
DR   EMBL; AJ297967; CAC17011.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54152; -.
DR   SMR; P54152; -.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase.
FT   CHAIN           1..191
FT                   /note="Peptide methionine sulfoxide reductase"
FT                   /id="PRO_0000138634"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        106
FT                   /note="R -> C (in Ref. 1; CAC17011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   191 AA;  21567 MW;  57849573E31FB1CB CRC64;
     MASSTTNNPA LDLDSDTPEN PGHELAQFAS GCFWGSELRF QRVVGVIKTE VGYSQGHVHD
     PNYRLVCSGT TNHSEVVRVQ FDPQVCPYSD LLSVFWSRHD PTTLNRQGGD VGTQYRSGIY
     YYNEEQDCLA KKSKEAKQKE FKDKRVVTEI LPAKRFYRAE EYHQQYLEKG GGNGNKQSAQ
     KGCNDPIKCY G