ID A0A3S0ZWE6_ELYCH Unreviewed; 175 AA.
AC A0A3S0ZWE6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=EGW08_015288 {ECO:0000313|EMBL:RUS76939.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS76939.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS76939.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS76939.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS76939.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS76939.1}.
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DR EMBL; RQTK01000622; RUS76939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0ZWE6; -.
DR STRING; 188477.A0A3S0ZWE6; -.
DR Proteomes; UP000271974; 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:UP000271974};
KW Zinc {ECO:0000256|RuleBase:RU365044}.
FT DOMAIN 50..172
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 19295 MW; 16C78E0273704ADF CRC64;
MNILHYVTQK QEISPKLKKL KASCDAAVAE GAKDDEGGGG AKSPPGLYDK DELQKRLSPA
QFRITQKLGT EKPFSGKYVH QKDEGQYNCV VCGTALFTSD VKFESGSGWP AFYDVISKDR
VVLKEESLGG LQRMEVKCSE CRAHLGHVFD DGPKPTGFRF CVNSCSLDFK KHTTV
//
