MSRB_CAEEL
ID MSRB_CAEEL Reviewed; 152 AA.
AC P34436;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable methionine-R-sulfoxide reductase B {ECO:0000305};
DE EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
GN ORFNames=F44E2.6 {ECO:0000312|WormBase:F44E2.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
CC methionine (R)-sulfoxide back to methionine (By similarity). While in
CC many cases, methionine oxidation is the result of random oxidation
CC following oxidative stress, methionine oxidation is also a post-
CC translational modification that takes place on specific residue (By
CC similarity). {ECO:0000250|UniProtKB:Q9JLC3}.
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:0000250|UniProtKB:Q9JLC3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9JLC3};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; FO081383; CCD71223.1; -; Genomic_DNA.
DR PIR; S44820; S44820.
DR RefSeq; NP_001254966.1; NM_001268037.1.
DR AlphaFoldDB; P34436; -.
DR SMR; P34436; -.
DR STRING; 6239.F44E2.6a; -.
DR EPD; P34436; -.
DR PaxDb; P34436; -.
DR PeptideAtlas; P34436; -.
DR EnsemblMetazoa; F44E2.6a.1; F44E2.6a.1; WBGene00018419.
DR EnsemblMetazoa; F44E2.6a.2; F44E2.6a.2; WBGene00018419.
DR UCSC; F44E2.6b; c. elegans.
DR WormBase; F44E2.6a; CE00184; WBGene00018419; -.
DR eggNOG; KOG0856; Eukaryota.
DR InParanoid; P34436; -.
DR OMA; CDVPLFS; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; P34436; -.
DR Reactome; R-CEL-5676934; Protein repair.
DR PRO; PR:P34436; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018419; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; P34436; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..152
FT /note="Probable methionine-R-sulfoxide reductase B"
FT /id="PRO_0000140325"
FT DOMAIN 27..151
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ SEQUENCE 152 AA; 17212 MW; F6D0219B52F20D00 CRC64;
MTTKKFRMED VGLSKLKVEK NPKDVKQTEW KSVLPNEVYR VARESGTETP HTGGFNDHFE
KGRYVCLCCG SELFNSDAKF WAGCGWPAFS ESVGQDANIV RIVDRSHGMH RTEVRCKTCD
AHLGHVFNDG PKETTGERYC INSVCMAFEK KD
