ID   MSRA_BOVIN              Reviewed;         233 AA.
AC   P54149; Q3ZC16; Q5E976;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-NOV-2008, entry version 58.
DE   RecName: Full=Peptide methionine sulfoxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Protein-methionine-S-oxide reductase;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=MSRA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal medulla;
RX   MEDLINE=96312545; PubMed=8700890; DOI=10.1073/pnas.93.5.2095;
RA   Moskovitz J., Weissbach H., Brot N.;
RT   "Cloning the expression of a mammalian gene involved in the reduction
RT   of methionine sulfoxide residues in proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:2095-2099(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   MEDLINE=20519025; PubMed=11063566; DOI=10.1021/bi0020269;
RA   Lowther W.T., Brot N., Weissbach H., Matthews B.W.;
RT   "Structure and mechanism of peptide methionine sulfoxide reductase, an
RT   'anti-oxidation' enzyme.";
RL   Biochemistry 39:13307-13312(2000).
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins
CC       to methionine.
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
CC   -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
CC       L-methionine (S)-S-oxide + thioredoxin.
CC   -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.
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DR   EMBL; U37150; AAC48539.1; -; mRNA.
DR   EMBL; BT021044; AAX09061.1; -; mRNA.
DR   EMBL; BC102980; AAI02981.1; -; mRNA.
DR   RefSeq; NP_776539.1; -.
DR   UniGene; Bt.4655; -.
DR   PDB; 1FVA; X-ray; 1.70 A; A/B=13-229.
DR   PDB; 1FVG; X-ray; 1.60 A; A=21-219.
DR   PDBsum; 1FVA; -.
DR   PDBsum; 1FVG; -.
DR   GeneID; 281312; -.
DR   KEGG; bta:281312; -.
DR   HOVERGEN; P54149; -.
DR   GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase.
FT   CHAIN         1    233       Peptide methionine sulfoxide reductase.
FT                                /FTId=PRO_0000138625.
FT   CONFLICT      4      4       A -> V (in Ref. 1; AAC48539).
FT   CONFLICT    125    125       H -> R (in Ref. 2; AAX09061).
FT   TURN         31     33
FT   TURN         49     51
FT   STRAND       54     58
FT   STRAND       64     72
FT   HELIX        73     81
FT   STRAND       86    100
FT   HELIX       103    107
FT   STRAND      114    121
FT   TURN        123    125
FT   HELIX       128    137
FT   STRAND      143    147
FT   STRAND      150    152
FT   HELIX       153    155
FT   STRAND      157    159
FT   HELIX       164    183
FT   HELIX       204    206
FT   TURN        207    211
SQ   SEQUENCE   233 AA;  25818 MW;  DA09151E42FB6C08 CRC64;
     MLSATRRALQ LFHSLFPIPR MGDSAAKIVS PQEALPGRKE PLVVAAKHHV NGNRTVEPFP
     EGTQMAVFGM GCFWGAERKF WTLKGVYSTQ VGFAGGYTPN PTYKEVCSGK TGHAEVVRVV
     FQPEHISFEE LLKVFWENHD PTQGMRQGND HGSQYRSAIY PTSAEHVGAA LKSKEDYQKV
     LSEHGFGLIT TDIREGQTFY YAEDYHQQYL SKDPDGYCGL GGTGVSCPLG IKK
//