ID   FLSO_ASFK5              Reviewed;         119 AA.
AC   P0C8G8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   08-NOV-2023, entry version 40.
DE   RecName: Full=FAD-linked sulfhydryl oxidase {ECO:0000250|UniProtKB:Q65163};
DE            EC=1.8.3.2 {ECO:0000250|UniProtKB:Q65163};
DE   AltName: Full=p14;
GN   OrderedLocusNames=Ken-085;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus.
OX   NCBI_TaxID=561445;
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.
CC       {ECO:0000250|UniProtKB:Q65163}.
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; Evidence={ECO:0000255|PROSITE-
CC         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 the late phase of the replicative cycle.
CC       {ECO:0000250|UniProtKB:Q65163}.
CC   -!- SIMILARITY: Belongs to the asfivirus B119L family. {ECO:0000305}.
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DR   EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C8G8; -.
DR   Proteomes; UP000000861; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; ALR/ERV; 1.
DR   PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 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_0000355535"
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;  14390 MW;  7EFEBDF44C97DF40 CRC64;
     MLHWGPKFWR ALHLYAIFFS DAPNWKEKYE AIQWILNFIE SLPCTMCRHH AFSYLTKNPL
     TLNNSEDFQY WTFAFHNNVN KRLNKKIISW SEYKNIYEQS ILKTIEYGKT DFIGAWSSL
//