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Entry: A0A0K0DTF9_STRER
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ID   A0A0K0DTF9_STRER        Unreviewed;       204 AA.
AC   A0A0K0DTF9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|ARBA:ARBA00012499, ECO:0000256|RuleBase:RU365044};
DE            EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499, ECO:0000256|RuleBase:RU365044};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0000052000.1};
RN   [1] {ECO:0000313|Proteomes:UP000035681}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SSTP_0000052000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
CC       methionine (R)-sulfoxide back to methionine. While in many cases
CC       methionine oxidation is the result of random oxidation following
CC       oxidative stress, methionine oxidation is also a post-translational
CC       modification that takes place on specific residues.
CC       {ECO:0000256|RuleBase:RU365044}.
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}.
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DR   AlphaFoldDB; A0A0K0DTF9; -.
DR   STRING; 6248.A0A0K0DTF9; -.
DR   WBParaSite; SSTP_0000052000.1; SSTP_0000052000.1; SSTP_0000052000.
DR   Proteomes; UP000035681; 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; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR10173:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B1; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365044};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU365044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365044}.
FT   DOMAIN          77..201
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   204 AA;  23661 MW;  6734D9A8017083FD CRC64;
     MKTLVTYTFE IISYCMLSQK LYSILNIIYT NRRLNVHCIT SKLFYLKYNN FNNFCLRKMS
     CGLDKLNTKK NPKEISDNEW KNVLSPDEYH VTRESGTEPK FSGEYDKFFK PGKYTCKCCG
     IDLFLSENKF DSGCGWPAFD KSVGEDLNII RLEDTSYGRI RTEVRCKNCN AHLGHVFDDG
     PKNTTGERYC INSVSINFES KESE
//
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