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P23373 (E10_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Probable FAD-linked sulfhydryl oxidase E10

EC=1.8.3.2
Gene names
Ordered Locus Names:VACWR066
ORF Names:E10R
OrganismVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]
Taxonomic identifier10254 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length95 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 thiol-disulfide transfer between E10, A2.5 and G4. Ref.4

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. Ref.4

Subcellular location

Virion membrane Probable. Note: Associated with crescent membranes, immature virions (IV) and mature virions (MV) Probable. Ref.3

Induction

Expressed in the late phase of the viral replicative cycle. Ref.3

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
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9595Probable FAD-linked sulfhydryl oxidase E10
PRO_0000099465

Regions

Topological domain1 – 88Intravirion Potential
Transmembrane9 – 2517Helical; Potential
Topological domain26 – 9570Virion surface Potential
Domain1 – 9595ERV/ALR sulfhydryl oxidase

Amino acid modifications

Disulfide bond43 ↔ 46Redox-active Potential

Sequences

Sequence LengthMass (Da)Tools
P23373 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: F4A2FAB4159DFA50

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

        70         80         90 
SSDDLNYIYY FFIRLFNNLA SDPKYAIDVT KVNPL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of rpo30, a vaccinia virus RNA polymerase gene with structural similarity to a eucaryotic transcription elongation factor."
Ahn B.-Y., Gershon P.D., Jones E.V., Moss B.
Mol. Cell. Biol. 10:5433-5441(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Vaccinia virus E10R protein is associated with the membranes of intracellular mature virions and has a role in morphogenesis."
Senkevich T.G., Weisberg A.S., Moss B.
Virology 278:244-252(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION.
[4]"Complete pathway for protein disulfide bond formation encoded by poxviruses."
Senkevich T.G., White C.L., Koonin E.V., Moss B.
Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH A2.5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36339 Genomic DNA. Translation: AAB59830.1.
AY243312 Genomic DNA. Translation: AAO89345.1.
PIRT30803.
RefSeqYP_232948.1. NC_006998.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3707599.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006890. Sulphydryl_Oase_FAD-link_ERV1.
[Graphical view]
PfamPF04805. Pox_E10. 1 hit.
[Graphical view]
PIRSFPIRSF015696. VAC_E10R. 1 hit.
SUPFAMSSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE10_VACCW
AccessionPrimary (citable) accession number: P23373
Secondary accession number(s): Q76ZV5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: May 14, 2014
This is version 61 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