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Database: UniProt
Entry: E2BEN1_HARSA
LinkDB: E2BEN1_HARSA
Original site: E2BEN1_HARSA 
ID   E2BEN1_HARSA            Unreviewed;       149 AA.
AC   E2BEN1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=EAI_12517 {ECO:0000313|EMBL:EFN85865.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN85865.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN85865.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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; GL447829; EFN85865.1; -; Genomic_DNA.
DR   RefSeq; XP_011137396.1; XM_011139094.2.
DR   AlphaFoldDB; E2BEN1; -.
DR   STRING; 610380.E2BEN1; -.
DR   EnsemblMetazoa; XM_011139094.3; XP_011137396.1; LOC105181984.
DR   GeneID; 105181984; -.
DR   KEGG; hst:105181984; -.
DR   InParanoid; E2BEN1; -.
DR   OMA; DEQWRAE; -.
DR   OrthoDB; 1074224at2759; -.
DR   PhylomeDB; E2BEN1; -.
DR   Proteomes; UP000008237; 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 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:UP000008237};
KW   Zinc {ECO:0000256|RuleBase:RU365044}.
FT   DOMAIN          7..141
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   149 AA;  16923 MW;  FB3706F6B9D46FA1 CRC64;
     MTTAVDKEEA RKRLTPIQWH VTQEKGTERP FTGCYNKFYE KGMYTCVVCD QELFSSDTKY
     DSGCGWPAFN EVLDQGRIKL TKDTSHVGGN LLLLIANPDM VRTEVTCSKC DAHLGHVFND
     GPKPTRKRFC INSASISFHP RKQEEKSTQ
//
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