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UniProtKB/Swiss-Prot entry P54150


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MSRA_ARATH
Primary accession number P54150
Secondary accession number Q9SW13
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 56)
Name and origin of the protein
Protein name Peptide methionine sulfoxide reductase
Synonyms EC 1.8.4.11
Protein-methionine-S-oxide reductase
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase
Gene name
Name: PMSR
OrderedLocusNames: At4g25130
ORFNames: F13M23.270
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Piffanelli P., Batchedler C., Murphy D.J.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X97326; CAA65991.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035523; CAB36755.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161562; CAB79422.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05534; T05534.
RefSeq NP_194243.1; -.
UniGene At.24140
3D structure databases
HSSP P27110; 1FF3. [HSSP ENTRY / PDB]
SMR P54150; 78-258.
ModBase P54150.
Protein-protein interaction databases
IntAct P54150; 1.
Organism-specific databases
TAIR At4g25130; -.
Gene expression databases
ArrayExpress P54150; -.
GermOnline AT4G25130; Arabidopsis thaliana.
Ontologies
GO
GO:0009570; Cellular component: chloroplast stroma (inferred from direct assay from TAIR).
GO:0008113; Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019538; Biological process: protein metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002569; MsrA.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1060.10; MsrA; 1.
Pfam PF01625; PMSR; 1.
Pfam graphical view of domain structure.
ProDom PD003489; PMSR; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00401; msrA; 1.
Proteomics databases
PRIDE P54150; -.
Genome annotation databases
GeneID 828616; -.
GenomeReviews CT486007_GR; AT4G25130.
KEGG ath:AT4G25130; -.
NMPDR fig|3702.1.peg.20418; -.
Other
ProtoNet P54150.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   258  258     Peptide methionine sulfoxide reductase. PRO_0000138632
CONFLICT   131   131        Y -> S (in Ref. 1; CAA65991). 
Sequence information
Length: 258 AA [This is the length of the unprocessed precursor] Molecular weight: 28644 Da [This is the MW of the unprocessed precursor] CRC64: DCB95E4B4CF88EA1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQVLVVSPPL IAAASLSKPL NSLSKAALSF SRAKPICPFP QTSRRPISVY KSPMNNLFNR 

        70         80         90        100        110        120 
LGFGSRPQAQ ADPSSAAIAQ GPDDDVPSSG QQFAQFGAGC FWGVELAYQR VPGVTKTEVG 

       130        140        150        160        170        180 
YSHGIVHNPS YEDVCTGTTG HNEVVRVQYD PKECSFESLL DVFWNRHDPT TLNRQGGDVG 

       190        200        210        220        230        240 
TQYRSGIYYY TDEQERIARE AVEKQQKILN KRIVTEILPA TKFYRAENYH QQYLAKGGRM 

       250 
GLRQSAEKGC KDPIRCYG 

P54150 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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