ID   VPRT_ASFP4              Reviewed;         273 AA.
AC   P0C9B7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=SUMO-1 cysteine protease S273R {ECO:0000250|UniProtKB:P0C9B9};
DE            Short=pS273R;
DE            EC=3.4.22.-;
GN   OrderedLocusNames=Pret-123;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
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].
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 cytoplasmic viral
CC       factories during assembly.
CC   -!- INDUCTION: Expressed late after infection.
CC       {ECO:0000250|UniProtKB:Q00946}.
CC   -!- SIMILARITY: Belongs to the peptidase C63 family. {ECO:0000305}.
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DR   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9B7; -.
DR   Proteomes; UP000000859; 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="SUMO-1 cysteine protease S273R"
FT                   /id="PRO_0000373127"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250|UniProtKB:Q00946"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000250|UniProtKB:P0C9B9"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q00946"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   273 AA;  31533 MW;  0ED9DEBFAB6856D0 CRC64;
     MSILEKITSS PSECAEHLTN KDSCLSKKIQ KELTSFLQKK ETLGCDSESC VITHPAVKAY
     AQQKGLDLSK ELETRFKAPG PRNNTGLLTN FNIDETLQRW AIKYTKFFNC PFSMMDFERV
     HYKFNQVDMV KVYKGEELQY VEGKVVKRPC NTFGCVLNTD FSTGTGKHWV AIFVDMRGDC
     WSIEYFNSAG NAPPGPVIRW MERVKQQLLK IHHTVKTLAV TNIRHQRSQT ECGPYSLFYI
     RARLDNVSYA HFISARITDE DMYKFRTHLF RIA