VF347_IIV3
ID VF347_IIV3 Reviewed; 148 AA.
AC Q196W4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 23-FEB-2022, entry version 51.
DE RecName: Full=Putative FAD-linked sulfhydryl oxidase 096R;
DE EC=1.8.3.2;
GN ORFNames=IIV3-096R;
OS Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=345201;
OH NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH NCBI_TaxID=42431; Culex territans.
OH NCBI_TaxID=332058; Culiseta annulata.
OH NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH NCBI_TaxID=7183; Psorophora ferox.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA Kutish G.F., Rock D.L.;
RT "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT virus).";
RL J. Virol. 80:8439-8449(2006).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IIV-6 347L family. {ECO:0000305}.
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DR EMBL; DQ643392; ABF82126.1; -; Genomic_DNA.
DR RefSeq; YP_654668.1; NC_008187.1.
DR SMR; Q196W4; -.
DR GeneID; 4156240; -.
DR KEGG; vg:4156240; -.
DR Proteomes; UP000001358; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..148
FT /note="Putative FAD-linked sulfhydryl oxidase 096R"
FT /id="PRO_0000377497"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..103
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 48..51
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ SEQUENCE 148 AA; 16744 MW; 55AA1099C22FAB39 CRC64;
MSIDPKLWGN AFWSTLHHVA AGYNDHPSLG ARQVMTNFIQ SIPVLLPCAE CQDHAFDYIG
RADLDRVVSS RRQLFLFFFN FHNHVNARLN KPQLAAKTVF QRYRVPFDGE AAAATTEPPF
HWSPWLTTAL AVILVVVVAG IGHRSRFK