FLSO_ASFWA
ID FLSO_ASFWA Reviewed; 119 AA.
AC P0C8G9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=FAD-linked sulfhydryl oxidase;
DE EC=1.8.3.2 {ECO:0000250|UniProtKB:Q65163};
DE AltName: Full=p14 {ECO:0000250|UniProtKB:Q65163};
GN OrderedLocusNames=War-083;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes the formation
CC of disulfide bonds in viral proteins produced in the cell cytoplasm (By
CC similarity). Involved in virion maturation (By similarity).
CC {ECO:0000250|UniProtKB:Q9JFM9, 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 Evidence={ECO:0000250|UniProtKB:Q65163};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBUNIT: Interacts with A151R. {ECO:0000250|UniProtKB:Q65163}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q65163}.
CC Virion {ECO:0000250|UniProtKB:Q65163}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the asfivirus B119L family. {ECO:0000305}.
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DR EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C8G9; -.
DR Proteomes; UP000000858; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; 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 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; Host cytoplasm; Late protein;
KW Oxidoreductase; Virion; Virulence.
FT CHAIN 1..119
FT /note="FAD-linked sulfhydryl oxidase"
FT /id="PRO_0000355537"
FT DOMAIN 1..97
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 44..47
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ SEQUENCE 119 AA; 14360 MW; DCFD2EF5DE1F3A87 CRC64;
MLHWGPKYWR ALHLYAIFFS DAPGWKEKYE AIQWILNFIE SLPCTRCRHH AFSYLTKNPL
TLNNSEDFQY WTFAFHNNVN NRLNKKIISW SEYKNIYEQS ILKTIEYGKT DFIGAWSSL