ID A0A026WQ06_OOCBI Unreviewed; 136 AA.
AC A0A026WQ06;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN ORFNames=X777_01785 {ECO:0000313|EMBL:EZA57179.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA57179.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA57179.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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|ARBA:ARBA00001795,
CC 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 EMBL; KK107152; EZA57179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WQ06; -.
DR STRING; 2015173.A0A026WQ06; -.
DR EnsemblMetazoa; XM_011336212.3; XP_011334514.1; LOC105277672.
DR OMA; DEQWRAE; -.
DR Proteomes; UP000053097; 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 HAMAP; MF_01400; MsrB; 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 B3; 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:UP000053097};
KW Zinc {ECO:0000256|RuleBase:RU365044}.
FT DOMAIN 7..129
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 136 AA; 15231 MW; 68C9FF8A204C5FAE CRC64;
MTTAVDKEEA RKRLTPLQWH VTQEKGTERP FTGCYDKFYQ KGTYACIVCD QELFSSDTKY
DSGCGWPAFN EVLDQGRIKL TKDTSHNKVR TEVTCSKCDA HLGHVFSDGP KPAGKRFCIN
SASINFHSAG EEKSSV
//
