ID   VPRT_ASFB7              Reviewed;         273 AA.
AC   Q00946;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cysteine protease S273R;
DE            Short=pS273R;
DE            EC=3.4.22.-;
GN   OrderedLocusNames=Ba71V-111; ORFNames=S273R;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1316688; DOI=10.1016/0042-6822(92)90558-7;
RA   Garcia-Beato R., Freije J.M.P., Lopez-Otin C., Blasco R., Vinuela E.;
RT   "A gene homologous to topoisomerase II in African swine fever virus.";
RL   Virology 188:938-947(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [3]
RP   FUNCTION, CHARACTERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-168
RP   AND CYS-232, AND ACTIVE SITE.
RX   PubMed=11031264; DOI=10.1074/jbc.m006844200;
RA   Andres G., Alejo A., Simon-Mateo C., Salas M.L.;
RT   "African swine fever virus protease, a new viral member of the SUMO-1-
RT   specific protease family.";
RL   J. Biol. Chem. 276:780-787(2001).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=12634404; DOI=10.1128/jvi.77.7.4444-4448.2003;
RA   Rubio D., Alejo A., Rodriguez I., Salas M.L.;
RT   "Polyprotein processing protease of African swine fever virus: purification
RT   and biochemical characterization.";
RL   J. Virol. 77:4444-4448(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=12719549; DOI=10.1128/jvi.77.10.5571-5577.2003;
RA   Alejo A., Andres G., Salas M.L.;
RT   "African swine fever virus proteinase is essential for core maturation and
RT   infectivity.";
RL   J. Virol. 77:5571-5577(2003).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [7]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
CC   -!- FUNCTION: SUMO-1 cysteine protease catalyzes the maturation of the
CC       pp220 and pp62 polyprotein precursors into core-shell proteins.
CC       {ECO:0000269|PubMed:11031264, ECO:0000269|PubMed:12719549}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:11031264}.
CC       Virion {ECO:0000269|PubMed:11031264, ECO:0000269|PubMed:30185597}.
CC       Note=Found in the perinuclear cytoplasmic viral factories during
CC       assembly.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the peptidase C63 family. {ECO:0000305}.
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DR   EMBL; M88699; AAA42734.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65340.1; -; Genomic_DNA.
DR   PIR; A42549; A42549.
DR   RefSeq; NP_042804.1; NC_001659.2.
DR   SMR; Q00946; -.
DR   MEROPS; C63.001; -.
DR   GeneID; 22220340; -.
DR   KEGG; vg:22220340; -.
DR   Proteomes; UP000000624; 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   1: Evidence at protein level;
KW   Host cytoplasm; Hydrolase; Late protein; Protease; Reference proteome;
KW   Thiol protease; Virion.
FT   CHAIN           1..273
FT                   /note="Cysteine protease S273R"
FT                   /id="PRO_0000101738"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000305|PubMed:11031264"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000250|UniProtKB:P0C9B9"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:11031264"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         168
FT                   /note="H->R: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11031264"
FT   MUTAGEN         232
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11031264"
SQ   SEQUENCE   273 AA;  31550 MW;  C5AA778179C57C17 CRC64;
     MSILEKITSS PSECAEHLTN KDSCLSKKIQ KELTSFLEKK ETLGCDSESC VITHPAVKAY
     AQQKGLDLSK ELETRFKAPG PRNNTGLLTN FNIDETLQRW AIKYTKFFNC PFSMMDFERV
     HYKFNQVDMV KVYKGEELQY VEGKVVKRPC NTFGCVLNTD FSTGTGKHWV AIFVDMRGDC
     WSIEYFNSAG NSPPGPVIRW MERVKQQLLK IHHTVKTLAV TNIRHQRSQT ECGPYSLFYI
     RARLDNVSYA HFISARITDE DMYKFRTHLF RIA