ID   VF347_IIV6              Reviewed;         111 AA.
AC   Q91FH7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   12-AUG-2020, entry version 58.
DE   RecName: Full=Putative FAD-linked sulfhydryl oxidase 347L;
DE            EC=1.8.3.2;
GN   ORFNames=IIV6-347L;
OS   Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX   NCBI_TaxID=176652;
OH   NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH   NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH   NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH   NCBI_TaxID=58607; Gryllus campestris.
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA   Jakob N.J., Mueller K., Bahr U., Darai G.;
RT   "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT   coding strategy of the genome of Chilo iridescent virus.";
RL   Virology 286:182-196(2001).
RN   [2]
RP   GENOME REANNOTATION.
RX   PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA   Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT   "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT   defining the core set of iridovirus genes.";
RL   Virol. J. 4:11-11(2007).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC       bond formation. {ECO:0000255|PROSITE-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   -!- SIMILARITY: Belongs to the IIV-6 347L family. {ECO:0000305}.
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DR   EMBL; AF303741; AAK82208.1; -; Genomic_DNA.
DR   RefSeq; NP_149810.1; NC_003038.1.
DR   SMR; Q91FH7; -.
DR   GeneID; 1732986; -.
DR   KEGG; vg:1732986; -.
DR   Proteomes; UP000001359; Genome.
DR   GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.310; -; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; PTHR12645; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; SSF69000; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..111
FT                   /note="Putative FAD-linked sulfhydryl oxidase 347L"
FT                   /id="PRO_0000377498"
FT   DOMAIN          2..109
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   111 AA;  12912 MW;  092E6B2558F6906E CRC64;
     MTDIDPHIWG PSFWSTYHLY ASSYPIHPTP IIMDAARSFV KTIPFTLPCS SCTDHAFAYI
     KNIQKQDPDL ISIVSSKMLF EKFFIDFHNS VNYRLGKPLL PESVARKKWR F