ID H0ZSW6_TAEGU Unreviewed; 159 AA. AC H0ZSW6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 03-OCT-2012, entry version 7. DE RecName: Full=Peptide methionine sulfoxide reductase MsrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; GN Name=MSRA; Synonyms=msrA; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Passeriformes; Passeroidea; Estrildidae; Estrildinae; OC Taeniopygia. OX NCBI_TaxID=59729; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSTGUT00000013870; ENSTGUP00000013712; ENSTGUG00000013321. DR GeneTree; ENSGT00390000003823; -. DR OMA; TEISEAK; -. DR GO; GO:0005739; C:mitochondrion; IEA:Compara. DR GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase activity; IEA:Compara. DR GO; GO:0019538; P:protein metabolic process; IEA:InterPro. DR Gene3D; G3DSA:3.30.1060.10; MsrA; 1. DR HAMAP; MF_01401; MsrA; 1; -. DR InterPro; IPR002569; Peptide_Met_Sox_Rdtase_MsrA. DR Pfam; PF01625; PMSR; 1. DR SUPFAM; SSF55068; MsrA; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT ACT_SITE 52 52 By similarity. SQ SEQUENCE 159 AA; 18018 MW; EF57AE5D988EE290 CRC64; MGDQASRLPQ AGEALPGRTQ RMAVPDKHHV NGNRMVEPFP EGTQMALFGM GCFWGAERKF WRQKGVYSTQ VGYAGGHTPN PTYKEVCSGR TGHTEAVRVV FEPQNISFEQ LLKVFWENHD PTQGMRQGND VGTQYRSAIY TFSQEQMEAA LRSKEEYQK //