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UniProtKB/Swiss-Prot entry Q66FE1


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

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Entry information
Entry name DSBD_YERPS
Primary accession number Q66FE1
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 39)
Name and origin of the protein
Protein name Thiol:disulfide interchange protein dsbD [Precursor]
Synonyms EC 1.8.1.8
Protein-disulfide reductase
Disulfide reductase
Gene name
Name: dsbD
OrderedLocusNames: YPTB0399
From
Yersinia pseudotuberculosis [TaxID: 633] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Yersinia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IP32953 / Serotype I;
DOI=10.1073/pnas.0404012101; PubMed=15358858 [NCBI, ExPASy, EBI, Israel, Japan]
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.;
"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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
BX936398; CAH19639.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_068942.1; -.
3D structure databases
ModBase Q66FE1.
Enzyme and pathway databases
BioCyc YPSE273123:YPTB0399-MON; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0047134; Molecular function: protein-disulfide reductase activity (inferred from electronic annotation from HAMAP).
GO:0017004; Biological process: cytochrome complex assembly (inferred from electronic annotation from HAMAP).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00399; -; 1.
PBIL [Tree]
InterPro IPR003834; Cyt_c_assmbl_TM.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF02683; DsbD; 1.
PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.
PRINTS PR00421; THIOREDOXIN.
PROSITE PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q66FE1.
ProtoNet Q66FE1.
Genome annotation databases
GeneID 2955489; -.
GenomeReviews BX936398_GR; YPTB0399.
KEGG yps:YPTB0399; -.
NMPDR fig|273123.1.peg.526; -.
Phylogenomic databases
HOGENOM Q66FE1; -.
Genome annotation databases
CMR Q66FE1; YPTB0399.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Cytochrome c-type biogenesis; Electron transport; Membrane; NAD; Oxidoreductase; Redox-active center; Signal; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     Potential. 
CHAIN   25   595  571     Thiol:disulfide interchange protein dsbD. PRO_5000098386
TRANSMEM   197   217  21     Potential. 
TRANSMEM   233   253  21     Potential. 
TRANSMEM   270   290  21     Potential. 
TRANSMEM   311   331  21     Potential. 
TRANSMEM   332   352  21     Potential. 
TRANSMEM   353   373  21     Potential. 
TRANSMEM   384   404  21     Potential. 
TRANSMEM   411   431  21     Potential. 
TRANSMEM   435   455  21     Potential. 
DOMAIN   452   592  141     Thioredoxin. 
DISULFID   134   140        Redox-active (By similarity). 
DISULFID   209   331        Redox-active (By similarity). 
DISULFID   507   510        Redox-active (By similarity). 
Sequence information
Length: 595 AA [This is the length of the unprocessed precursor] Molecular weight: 64492 Da [This is the MW of the unprocessed precursor] CRC64: 4DBC4E2277788265 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQRFITLIL LLCSVLLAPH SAQSSLFGEN TSFGAKNSQS RFIPVDQAFA FDFHQQGDQL 

        70         80         90        100        110        120 
NLSWQIHPGY YLYRQQIKIV PQQAALGAFT LPEGITHHDE FYGEVEIFKQ QLTLKIPITQ 

       130        140        150        160        170        180 
AAEQASVSVT YQGCAEAGFC YPPETRVIPL DVVVAASTAS GTAAVNSSAT VNPPATTQPE 

       190        200        210        220        230        240 
GDATPVPSTL PFSPLWALLI GIGIAFTPCV LPMYPLISAV ILGREKPHSQ RRILILAVVY 

       250        260        270        280        290        300 
VQGMALTYTL LGLVVAAAGL QFQAALQHPY VLIGLSVLFV LLALSMFGLY SLQLPSSLQT 

       310        320        330        340        350        360 
RLTQWSNSQR GGSLAGVFAM GALAGLICSP CTTAPLSAIL LYIAQSGNML AGGGTLYLYA 

       370        380        390        400        410        420 
LGMGIPLVVV TLFGNKLIPR SGPWMQYVKE AFGFVILALP VFLLERVLGD VWGLRLWSLL 

       430        440        450        460        470        480 
AVAFFGWAFV LSLKAHAGWV RVCQLLLLAA LLIVARPLQD WAFNGNTQQN AVKHINFQPV 

       490        500        510        520        530        540 
ANLPQLQAVL AQAQGKPVML DLYADWCVAC KEFEKYTFSD DKVQRQLANT LLLQADVTAN 

       550        560        570        580        590 
NAEHATLLNK FNVLGLPTIL FFDSQGNEIT AARVTGFMDA AQFLQHLQNT PAVTK 

Q66FE1 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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