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UniProtKB/Swiss-Prot entry Q6FAL8

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

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Entry information
Entry name MSRB_ACIAD
Primary accession number Q6FAL8
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 33)
Name and origin of the protein
Protein name Peptide methionine sulfoxide reductase msrB
Synonyms EC 1.8.4.12
Peptide-methionine (R)-S-oxide reductase
Gene name
Name: msrB
OrderedLocusNames: ACIAD2086
From
Acinetobacter sp. (strain ADP1) [TaxID: 62977] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan]
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.";
Nucleic Acids Res. 32:5766-5779(2004).
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
CR543861; CAG68895.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_046717.1; -.
3D structure databases
ModBase Q6FAL8.
Enzyme and pathway databases
BioCyc ASP62977:ACIAD2086-MON; -.
Ontologies
GO
GO:0033743; Molecular function: peptide-methionine (R)-S-oxide reductase activity (inferred from electronic annotation from EC).
GO:0008113; Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01400; -; 1.
PBIL [Tree]
InterPro IPR002579; MsrB.
Graphical view of domain structure.
Gene3D G3DSA:2.170.150.20; MsrB; 1.
Pfam PF01641; SelR; 1.
Pfam graphical view of domain structure.
ProDom PD004057; DUF25; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00357; MsrB; 1.
BLOCKS Q6FAL8.
ProtoNet Q6FAL8.
Genome annotation databases
GeneID 2879149; -.
GenomeReviews CR543861_GR; ACIAD2086.
KEGG aci:ACIAD2086; -.
NMPDR fig|62977.3.peg.1979; -.
Phylogenomic databases
HOGENOM Q6FAL8; -.
Genome annotation databases
CMR Q6FAL8; ACIAD2086.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Metal-binding; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   139  139     Peptide methionine sulfoxide reductase msrB. PRO_1000068261
ACT_SITE   119   119        Nucleophile (By similarity). 
METAL   47    47        Zinc (By similarity). 
METAL   50    50        Zinc (By similarity). 
METAL   96    96        Zinc (By similarity). 
METAL   99    99        Zinc (By similarity). 
Sequence information
Length: 139 AA [This is the length of the unprocessed precursor] Molecular weight: 15964 Da [This is the MW of the unprocessed precursor] CRC64: 781AE7B9E2068C3F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGKLNKTERE WQRELSPEEY RITRQKGTEP AFTGQYWNTK QSGTYVCRCC GTELFSSISK 

        70         80         90        100        110        120 
YDSGCGWPSF YKPINTTAIE EHDDFSHGMV RTEIVCHHCD AHLGHVFEDG PQPTGLRYCV 

       130 
NSASLQLKTD EKNDEETYP
Q6FAL8 in FASTA format

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