ID   E10_VAR67               Reviewed;          95 AA.
AC   P0DOL5; P33821;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   12-AUG-2020, entry version 5.
DE   RecName: Full=Probable FAD-linked sulfhydryl oxidase E10;
DE            EC=1.8.3.2;
GN   ORFNames=E10R;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC       bond formation. The complete pathway for formation of disulfide bonds
CC       in intracellular virion membrane proteins sequentially involves
CC       oxidation of E10R, A2.5 and G4 (By similarity). {ECO:0000255|PROSITE-
CC       ProRule:PRU00654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC         Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC   -!- SUBUNIT: Interacts with A2.5; this interaction involves formation of a
CC       transient disulfide-bonded intermediate, allowing disulfide bond
CC       transfer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}. Note=Associated
CC       with crescent membranes, immature virions (IV) and mature virions (MV).
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the poxviridae E10 family. {ECO:0000305}.
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DR   EMBL; X69198; CAA48992.1; -; Genomic_DNA.
DR   PIR; D36842; D36842.
DR   RefSeq; NP_042095.1; NC_001611.1.
DR   GeneID; 1486405; -.
DR   KEGG; vg:1486405; -.
DR   Proteomes; UP000002060; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.120.310; -; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR006890; Sulphydryl_Oase_FAD-link_ERV1.
DR   Pfam; PF04805; Pox_E10; 1.
DR   PIRSF; PIRSF015696; VAC_E10R; 1.
DR   SUPFAM; SSF69000; SSF69000; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; Late protein; Membrane; Oxidoreductase;
KW   Redox-active center; Reference proteome; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..95
FT                   /note="Probable FAD-linked sulfhydryl oxidase E10"
FT                   /id="PRO_0000099466"
FT   TOPO_DOM        1..8
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..95
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..95
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        43..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   95 AA;  10836 MW;  9BCB0B4306397E27 CRC64;
     MNPKHWGRAA WTIIFIVLSQ AGLDGNIEAC KRKLYTIVST LPCPACRRHA TIAIEDNNIM
     SSNDLNYIYY FFIRLFNNLA SDPKYAIDVS KVKPL