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UniProtKB/Swiss-Prot entry Q8PWF5


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

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Entry information
Entry name MSRB_METMA
Primary accession number Q8PWF5
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 35)
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: MM_1634
From
Methanosarcina mazei (Methanosarcina frisia) [TaxID: 2209] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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
AE008384; AAM31330.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_633658.1; -.
3D structure databases
HSSP P14930; 1L1D. [HSSP ENTRY / PDB]
ModBase Q8PWF5.
Enzyme and pathway databases
BioCyc MMAZ192952:MM1634-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.
ProtoNet Q8PWF5.
Genome annotation databases
GeneID 1479976; -.
GenomeReviews AE008384_GR; MM_1634.
KEGG mma:MM_1634; -.
NMPDR fig|192952.1.peg.1634; -.
Phylogenomic databases
HOGENOM Q8PWF5; -.
Genome annotation databases
CMR Q8PWF5; MM_1634.
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   140  140     Peptide methionine sulfoxide reductase msrB. PRO_1000068279
ACT_SITE   121   121        Nucleophile (By similarity). 
METAL   49    49        Zinc (By similarity). 
METAL   52    52        Zinc (By similarity). 
METAL   98    98        Zinc (By similarity). 
METAL   101   101        Zinc (By similarity). 
Sequence information
Length: 140 AA [This is the length of the unprocessed precursor] Molecular weight: 16038 Da [This is the MW of the unprocessed precursor] CRC64: 8D0E0710D963DED2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQNKIEKSE EDWKSVLTPE QYHVLRQKGT ERPFSGNLYY NKEKGIYTCA ACGQELFSSD 

        70         80         90        100        110        120 
TKFESGTGWP SFYDVISSDR VRLHEDNSYF MKRIEVVCSR CGSHLGHVFE DGPEPTGQRY 

       130        140 
CINSVSLGFT KEEDTGKEKE 

Q8PWF5 in FASTA format

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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)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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