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UniProtKB/Swiss-Prot entry O14144


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

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Entry information
Entry name ERV1_SCHPO
Primary accession number O14144
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name Mitochondrial FAD-linked sulfhydryl oxidase erv1
Synonym EC 1.8.3.2
Gene name
Name: erv1
ORFNames: SPAC3G6.08
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(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
CU329670; CAB16284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T38727; T38727.
RefSeq NP_594974.1; -.
3D structure databases
HSSP Q63042; 1OQC. [HSSP ENTRY / PDB]
ModBase O14144.
Organism-specific databases
GeneDB_Spombe SPAC3G6.08; -.
Gene expression databases
ArrayExpress O14144; -.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016972; Molecular function: thiol oxidase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006863; Evr1_Alr.
IPR001005; SANT_DNA-bd.
Graphical view of domain structure.
Gene3D G3DSA:1.20.120.310; Evr1_Alr; 1.
Pfam PF04777; Evr1_Alr; 1.
Pfam graphical view of domain structure.
PROSITE PS51324; ERV_ALR; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 2543175; -.
KEGG spo:SPAC3G6.08; -.
Other
ProtoNet O14144.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   182  182     Mitochondrial FAD-linked sulfhydryl oxidase erv1. PRO_0000339121
DOMAIN   75   177  103     ERV/ALR sulfhydryl oxidase. 
REGION   160   177  18     FAD-binding (By similarity). 
DISULFID   122   125        Redox-active (By similarity). 
DISULFID   153   170        By similarity. 
Sequence information
Length: 182 AA [This is the length of the unprocessed precursor] Molecular weight: 20769 Da [This is the MW of the unprocessed precursor] CRC64: C8756CB2022F4746 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVFGKRYRDK ETGIIYDENG RPCKTCNIFS SFRNVAQQPN SSTVPEVKSN TQLESKQSSI 

        70         80         90        100        110        120 
DCNTNAIPDS VSFPRLPDVA ELGRSTWTFL HAMAANFPKN PTPTQQNDMS SFLYNFSKFY 

       130        140        150        160        170        180 
PCWSCAEDLR IWMAKYGNSP RVDSRESLCE WICEAHNDVN ERLGKPLFNC QVWSKKASEL 


AD 

O14144 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)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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