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Database: UniProt
Entry: A0A3Q0GFZ9_ALLSI
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ID   A0A3Q0GFZ9_ALLSI        Unreviewed;       173 AA.
AC   A0A3Q0GFZ9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|RuleBase:RU365044};
DE            EC=1.8.4.12 {ECO:0000256|RuleBase:RU365044};
GN   Name=MSRB3 {ECO:0000313|RefSeq:XP_025058591.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025058591.1};
RN   [1] {ECO:0000313|RefSeq:XP_025058591.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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-methionine = [thioredoxin]-
CC         dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58773; EC=1.8.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000502};
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   RefSeq; XP_025058591.1; XM_025202806.1.
DR   AlphaFoldDB; A0A3Q0GFZ9; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
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:UP000189705};
KW   Zinc {ECO:0000256|RuleBase:RU365044}.
FT   DOMAIN          29..151
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   REGION          151..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   173 AA;  19080 MW;  3E9C36B0D5FE251C CRC64;
     MGQEPVTPNN PSVKGSCRDK KDCKVVFSQQ DLRKRLTPLQ YHVTQEKGTE SAFEGEYTHH
     KAHGIYKCVV CGTPLFKSDT KFDSNSGWPS FFDVISPDAI TFTDDFSYGM HRVETSCNQC
     GAHLGHIFDD GPRPTGKRYC INSASLSFES VDKNNAGEGS SSTSPAQTEK SEL
//
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