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P21050 (E10R_VACCC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable FAD-linked sulfhydryl oxidase E10

EC=1.8.3.2
Gene names
ORF Names:E10R
OrganismVaccinia virus (strain Copenhagen) (VACV) [Complete proteome]
Taxonomic identifier10249 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length95 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxydation of E10, A2.5 and G4 By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Interacts with A2.5; this interaction involves formation of a transient disulfide-bonded intermediate, allowing disulfide bond transfer By similarity.

Subcellular location

Virion membrane; Single-pass membrane protein Potential. Note: Associated with crescent membranes, immature virions (IV) and mature virions (MV) By similarity.

Induction

Expressed in the late phase of the viral replicative cycle.

Sequence similarities

Belongs to the poxviridae E10 family.

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Ontologies

Keywords
   Cellular componentMembrane
Viral envelope protein
Virion
   Developmental stageLate protein
   DomainRedox-active center
Transmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionthiol oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9595Probable FAD-linked sulfhydryl oxidase E10
PRO_0000099464

Regions

Transmembrane9 – 2517Helical; Potential
Domain1 – 9595ERV/ALR sulfhydryl oxidase

Amino acid modifications

Disulfide bond43 ↔ 46Redox-active Potential

Sequences

Sequence LengthMass (Da)Tools
P21050 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: F4A2FDC41599EA50

FASTA9510,851
        10         20         30         40         50         60 
MNPKHWGRAV WTIIFIVLSQ AGLDGNIEAC KRKLYTIVST LPCPACRRHA TIAIEDNNVM 

        70         80         90 
SSDDLNYIYY FFIRLFNNLA SDPKYAIDVS KVKPL 

« Hide

References

[1]"The complete DNA sequence of vaccinia virus."
Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., Paoletti E.
Virology 179:247-266(1990) [PubMed: 2219722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Appendix to 'The complete DNA sequence of vaccinia virus'."
Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., Paoletti E.
Virology 179:517-563(1990)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35027 Genomic DNA. Translation: AAA48051.1.
PIRE42509.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006863. Evr1_Alr.
IPR006890. Sulphydryl_Oase_FAD-link_ERV1.
[Graphical view]
Gene3DG3DSA:1.20.120.310. Evr1_Alr. 1 hit.
PfamPF04805. Pox_E10. 1 hit.
[Graphical view]
PIRSFPIRSF015696. VAC_E10R. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE10R_VACCC
AccessionPrimary (citable) accession number: P21050
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families