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Database: UniProt
Entry: A0A2K6AGY6_MANLE
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ID   A0A2K6AGY6_MANLE        Unreviewed;       151 AA.
AC   A0A2K6AGY6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Methionine-R-sulfoxide reductase B1 {ECO:0000256|ARBA:ARBA00040935};
DE            EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499};
DE            EC=1.8.4.14 {ECO:0000256|ARBA:ARBA00012498};
DE   AltName: Full=Selenoprotein X {ECO:0000256|ARBA:ARBA00042752};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000039329.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000039329.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, 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:58773; EC=1.8.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000502};
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|ARBA:ARBA00001795};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|ARBA:ARBA00007174}.
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DR   AlphaFoldDB; A0A2K6AGY6; -.
DR   Ensembl; ENSMLET00000062945.1; ENSMLEP00000039329.1; ENSMLEG00000043698.1.
DR   GeneTree; ENSGT00510000047678; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   PANTHER; PTHR46755; METHIONINE-R-SULFOXIDE REDUCTASE B1; 1.
DR   PANTHER; PTHR46755:SF5; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Selenocysteine {ECO:0000256|ARBA:ARBA00022933}.
FT   DOMAIN          1..65
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   151 AA;  16723 MW;  C2EF0E9680CEA795 CRC64;
     MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE
     HNRPGALKLQ GLRAVCSRPV ASARELPPQA IGRDWPSGAN VGNRTGFLYG LQDKGVLWQV
     WQRVGPRVPE RWPQAGAVPI LNIQQLAEVC P
//
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