ID A0A0M8N919_9HYPO Unreviewed; 147 AA.
AC A0A0M8N919;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|RuleBase:RU365044};
DE EC=1.8.4.12 {ECO:0000256|RuleBase:RU365044};
GN ORFNames=ESCO_003836 {ECO:0000313|EMBL:KOS23244.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS23244.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS23244.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC Evidence={ECO:0000256|RuleBase:RU365044};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU365044};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU365044};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|ARBA:ARBA00007174, ECO:0000256|RuleBase:RU365044}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS23244.1}.
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DR EMBL; LGSR01000002; KOS23244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N919; -.
DR STRING; 150374.A0A0M8N919; -.
DR OrthoDB; 1074224at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR PANTHER; PTHR46081; PEPTIDE METHIONINE SULFOXIDE REDUCTASE 2; 1.
DR PANTHER; PTHR46081:SF8; PEPTIDE METHIONINE SULFOXIDE REDUCTASE 2; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU365044};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365044};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Zinc {ECO:0000256|RuleBase:RU365044}.
FT DOMAIN 9..133
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 147 AA; 16198 MW; 05B756F2F584A5F2 CRC64;
MSYPDQRSDE EWRAVLNPQQ FRILREKGTE RPGTGEYDKH YPQDGAYHCA GCSAPLYKAS
HKFSSGCGWP AYFDSIPGAV TRHEDRSFGV SRTEIVCSNC GGHLGHVFKG EGFPTPTDER
HCVNSISLKF APGDKVVDTT GAKESKA
//
