ID   VPRT_ASFM2              Reviewed;         273 AA.
AC   Q65228;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cysteine protease S273R;
DE            Short=pS273R;
DE            EC=3.4.22.-;
GN   OrderedLocusNames=Mal-119; ORFNames=i6R;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
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 [GENOMIC DNA].
RX   PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA   Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA   Hammond J.M., Smith G.L.;
RT   "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT   a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL   J. Gen. Virol. 75:1655-1684(1994).
RN   [2]
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: SUMO-1 cysteine protease catalyzes the maturation of the
CC       pp220 and pp62 polyprotein precursors into core-shell proteins.
CC       {ECO:0000250|UniProtKB:Q00946}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q00946}.
CC       Virion {ECO:0000250|UniProtKB:Q00946}. Note=Found in the perinuclear
CC       cytoplasmic viral factories during assembly.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase C63 family. {ECO:0000305}.
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DR   EMBL; X71982; CAA50819.1; -; Genomic_DNA.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; Q65228; -.
DR   MEROPS; C63.001; -.
DR   PRIDE; Q65228; -.
DR   Proteomes; UP000000860; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   InterPro; IPR016510; VPRT.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   PIRSF; PIRSF007159; Peptidase_ASVF; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Hydrolase; Late protein; Protease; Thiol protease; Virion.
FT   CHAIN           1..273
FT                   /note="Cysteine protease S273R"
FT                   /id="PRO_0000101739"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   273 AA;  31493 MW;  D6AD6DAC62C25F3B CRC64;
     MSILEKITSS PSECAEHITN KDSCLSKKIQ KELTSFLQKK ETLGCDSESC VITHPAVKAY
     AQQKGLDLSK ELETRFKAPG PRNNTGLLTN FNIDETLQRW AIKYTKFFNC PFSMMDFESI
     HYKFNQVDMA KVYKGEELQY VEGKAVKRPC NTFGCVLNTD FSTGPGKHWV AIFVDMRGDC
     WSIEYFNSAG NSPPGPVIRW MERVKQQLLK IHHTVKTLAV TNIRHQRSQT ECGPYSLFYI
     RARLDNVSYT HFISTRITDE NMYKFRTHLF RIA