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O14144 (ERV1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial FAD-linked sulfhydryl oxidase erv1

EC=1.8.3.2
Gene names
Name:erv1
ORF Names:SPAC3G6.08
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS) By similarity.

Catalytic activity

2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.

Cofactor

FAD By similarity.

Subcellular location

Mitochondrion intermembrane space By similarity.

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182Mitochondrial FAD-linked sulfhydryl oxidase erv1
PRO_0000339121

Regions

Domain75 – 177103ERV/ALR sulfhydryl oxidase
Region160 – 17718FAD-binding By similarity

Amino acid modifications

Disulfide bond122 ↔ 125Redox-active By similarity
Disulfide bond153 ↔ 170 By similarity

Sequences

Sequence LengthMass (Da)Tools
O14144 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C8756CB2022F4746

FASTA18220,769
        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 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
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. expand/collapse author list , 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.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB16284.1.
PIRT38727.
RefSeqNP_594974.1. NM_001020405.2.

3D structure databases

ProteinModelPortalO14144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4670891.
STRING4896.SPAC3G6.08-1.

Proteomic databases

MaxQBO14144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3G6.08.1; SPAC3G6.08.1:pep; SPAC3G6.08.
GeneID2543175.
KEGGspo:SPAC3G6.08.

Organism-specific databases

PomBaseSPAC3G6.08.

Phylogenomic databases

eggNOGCOG5054.
HOGENOMHOG000195924.
KOK17783.
OMANLWKKRW.
OrthoDBEOG7WDNCT.
PhylomeDBO14144.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view]
PfamPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMSSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804200.
PROO14144.

Entry information

Entry nameERV1_SCHPO
AccessionPrimary (citable) accession number: O14144
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names