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Database: UniProt
Entry: D2VVR4_NAEGR
LinkDB: D2VVR4_NAEGR
Original site: D2VVR4_NAEGR 
ID   D2VVR4_NAEGR            Unreviewed;       168 AA.
AC   D2VVR4;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=NAEGRDRAFT_55441 {ECO:0000313|EMBL:EFC39086.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC39086.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC39086.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
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; GG738902; EFC39086.1; -; Genomic_DNA.
DR   RefSeq; XP_002671830.1; XM_002671784.1.
DR   AlphaFoldDB; D2VVR4; -.
DR   STRING; 5762.D2VVR4; -.
DR   EnsemblProtists; EFC39086; EFC39086; NAEGRDRAFT_55441.
DR   GeneID; 8858434; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_55441; -.
DR   eggNOG; KOG0856; Eukaryota.
DR   InParanoid; D2VVR4; -.
DR   OMA; DEQWRAE; -.
DR   OrthoDB; 1074224at2759; -.
DR   Proteomes; UP000006671; 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:UP000006671};
KW   Zinc {ECO:0000256|RuleBase:RU365044}.
FT   DOMAIN          37..168
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   168 AA;  18979 MW;  50C3693FF5B1746B CRC64;
     MSYSQSVREL IKQVESEDAI IVDDHSKLPP ALVQHSDVEW MKILTSKQYE VLRRAGTEPS
     FCSGYKVFKD QLKENNQEEG VFHCSGCDAP LFSAKTSFDS GSGWPSFWAP FKPKAIGYVV
     DKKFGMERVE VVCTNCHSHL GHVFEDGPRD KTKLRYCINA VCLALKKL
//
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